An iron-sulfur protein which serves as an electron carrier in enzymatic steroid hydroxylation reactions in adrenal cortex mitochondria. The electron transport system which catalyzes this reaction consists of adrenodoxin reductase, NADP, adrenodoxin, and cytochrome P-450.
An enzyme that catalyzes the oxidation and reduction of FERREDOXIN or ADRENODOXIN in the presence of NADP. EC 1.18.1.2 was formerly listed as EC 1.6.7.1 and EC 1.6.99.4.
A mitochondrial cytochrome P450 enzyme that catalyzes the side-chain cleavage of C27 cholesterol to C21 pregnenolone in the presence of molecular oxygen and NADPH-FERRIHEMOPROTEIN REDUCTASE. This enzyme, encoded by CYP11A1 gene, catalyzes the breakage between C20 and C22 which is the initial and rate-limiting step in the biosynthesis of various gonadal and adrenal steroid hormones.
The outer layer of the adrenal gland. It is derived from MESODERM and comprised of three zones (outer ZONA GLOMERULOSA, middle ZONA FASCICULATA, and inner ZONA RETICULARIS) with each producing various steroids preferentially, such as ALDOSTERONE; HYDROCORTISONE; DEHYDROEPIANDROSTERONE; and ANDROSTENEDIONE. Adrenal cortex function is regulated by pituitary ADRENOCORTICOTROPIN.
A mitochondrial cytochrome P450 enzyme that catalyzes the 11-beta-hydroxylation of steroids in the presence of molecular oxygen and NADPH-FERRIHEMOPROTEIN REDUCTASE. This enzyme, encoded by CYP11B1 gene, is important in the synthesis of CORTICOSTERONE and HYDROCORTISONE. Defects in CYP11B1 cause congenital adrenal hyperplasia (ADRENAL HYPERPLASIA, CONGENITAL).
A group of oxidoreductases that act on NADH or NADPH. In general, enzymes using NADH or NADPH to reduce a substrate are classified according to the reverse reaction, in which NAD+ or NADP+ is formally regarded as an acceptor. This subclass includes only those enzymes in which some other redox carrier is the acceptor. (Enzyme Nomenclature, 1992, p100) EC 1.6.
A 21-carbon steroid, derived from CHOLESTEROL and found in steroid hormone-producing tissues. Pregnenolone is the precursor to GONADAL STEROID HORMONES and the adrenal CORTICOSTEROIDS.
Carbodiimide cross-linking reagent.
Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.
Iron-containing proteins that transfer electrons, usually at a low potential, to flavoproteins; the iron is not present as in heme. (McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
A superfamily of hundreds of closely related HEMEPROTEINS found throughout the phylogenetic spectrum, from animals, plants, fungi, to bacteria. They include numerous complex monooxygenases (MIXED FUNCTION OXYGENASES). In animals, these P-450 enzymes serve two major functions: (1) biosynthesis of steroids, fatty acids, and bile acids; (2) metabolism of endogenous and a wide variety of exogenous substrates, such as toxins and drugs (BIOTRANSFORMATION). They are classified, according to their sequence similarities rather than functions, into CYP gene families (>40% homology) and subfamilies (>59% homology). For example, enzymes from the CYP1, CYP2, and CYP3 gene families are responsible for most drug metabolism.
The study of the characteristics, behavior, and internal structures of the atomic nucleus and its interactions with other nuclei. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
The process by which ELECTRONS are transported from a reduced substrate to molecular OXYGEN. (From Bennington, Saunders Dictionary and Encyclopedia of Laboratory Medicine and Technology, 1984, p270)
Sorbitan mono-9-octadecanoate poly(oxy-1,2-ethanediyl) derivatives; complex mixtures of polyoxyethylene ethers used as emulsifiers or dispersing agents in pharmaceuticals.
Cytochrome P-450 monooxygenases (MIXED FUNCTION OXYGENASES) that are important in steroid biosynthesis and metabolism.
Semiautonomous, self-reproducing organelles that occur in the cytoplasm of all cells of most, but not all, eukaryotes. Each mitochondrion is surrounded by a double limiting membrane. The inner membrane is highly invaginated, and its projections are called cristae. Mitochondria are the sites of the reactions of oxidative phosphorylation, which result in the formation of ATP. They contain distinctive RIBOSOMES, transfer RNAs (RNA, TRANSFER); AMINO ACYL T RNA SYNTHETASES; and elongation and termination factors. Mitochondria depend upon genes within the nucleus of the cells in which they reside for many essential messenger RNAs (RNA, MESSENGER). Mitochondria are believed to have arisen from aerobic bacteria that established a symbiotic relationship with primitive protoeukaryotes. (King & Stansfield, A Dictionary of Genetics, 4th ed)
Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed)
A group of cytochromes with covalent thioether linkages between either or both of the vinyl side chains of protoheme and the protein. (Enzyme Nomenclature, 1992, p539)
Carbodiimides are chemical compounds containing two nitrogen atoms and one carbon atom, often used in biochemistry for the formation of amide bonds, particularly in peptide synthesis and cross-linking of proteins or other biomolecules.
Characteristics of ELECTRICITY and magnetism such as charged particles and the properties and behavior of charged particles, and other phenomena related to or associated with electromagnetism.
An NAPH-dependent cytochrome P450 enzyme that catalyzes the oxidation of the side chain of sterol intermediates such as the 27-hydroxylation of 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol.
The rate dynamics in chemical or physical systems.
A technique applicable to the wide variety of substances which exhibit paramagnetism because of the magnetic moments of unpaired electrons. The spectra are useful for detection and identification, for determination of electron structure, for study of interactions between molecules, and for measurement of nuclear spins and moments. (From McGraw-Hill Encyclopedia of Science and Technology, 7th edition) Electron nuclear double resonance (ENDOR) spectroscopy is a variant of the technique which can give enhanced resolution. Electron spin resonance analysis can now be used in vivo, including imaging applications such as MAGNETIC RESONANCE IMAGING.
A pair of glands located at the cranial pole of each of the two KIDNEYS. Each adrenal gland is composed of two distinct endocrine tissues with separate embryonic origins, the ADRENAL CORTEX producing STEROIDS and the ADRENAL MEDULLA producing NEUROTRANSMITTERS.
A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).
The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.
Inorganic salts of the hypothetical acid, H3Fe(CN)6.

Luteinization and proteolysis in ovarian follicles of Meishan and Large White gilts during the preovulatory period. (1/164)

This experiment was conducted to determine why follicles luteinize faster in the Meishan breed than in the Large White breed of pig. Follicles were recovered during the late follicular phase from ovaries of both breeds before and after administration of hCG given to mimic the LH surge. First, the patterns of cholesterol transporters (high and low density lipoproteins: HDL and LDL) were compared. Cholesterol transporters detected in follicular fluid consisted of HDL only. Similar amounts of Apolipoprotein A-I were found in all samples. There was no obvious breed effect on minor lipoproteins found in the HDL-rich fraction, and this pattern was altered similarly by hCG in the two breeds. The LDL-rich samples of serum from both breeds contained similar amounts of protein. Second, three steroidogenic enzymes, adrenodoxin, 17 alpha-hydroxylase-lyase (P450(17) alpha) and 3 beta-hydroxysteroid-dehydrogenase (3 beta-HSD) were detected by immunohistochemistry and quantified by image analysis on sections of the two largest follicles. Before hCG treatment, theca interna cells demonstrated immunoreactivities for adrenodoxin (strong), P450(17) alpha and 3 beta-HSD (very strong), whereas granulosa cells displayed immunoreactivities for adrenodoxin only. After hCG treatment, the localization of the enzymes was unchanged but the staining intensity of adrenodoxin on granulosa cells and 3 beta-HSD on theca cells increased (P < 0.01 and P < 0.05, respectively). Breed effects were detected for the amounts of adrenodoxin in theca cells (Meishan > Large White; P < 0.05) and of 17 alpha-hydroxylase (Large White > Meishan, P < 0.01). Breed x treatment interactions were never detected. Finally, gelatinases, plasminogen activator, plasminogen activator inhibitor, tissue inhibitors of metalloproteases (TIMP-1 and TIMP-2) were visualized by direct or reverse zymography or western blotting. Whatever the stage relative to LH administration, follicular fluid from Large White gilts contained more TIMP-1, and TIMP-2 (P < 0.02 and P < 0.01, respectively). No breed effect was detected for the amounts of gelatinases and plasminogen activator inhibitor 1. However, for these parameters, a significant breed x time interaction was obvious, as the Meishan follicles had a greater response to hCG (P < 0.01). Since proteolysis plays a key role in the bioavailability of growth factors such as insulin-like growth factor 1, fibroblast growth factor and transforming growth factor beta, which have the ability to alter gonadotrophin-induced progesterone production in pigs, the differences observed in its control in the present study may explain, at least in part, the different patterns of luteinization observed in Meishan and Large White follicles.  (+info)

Enzymatic properties of vesicle-reconstituted human cytochrome P450SCC (CYP11A1) differences in functioning of the mitochondrial electron-transfer chain using human and bovine adrenodoxin and activation by cardiolipin. (2/164)

The recently reported heterologous expression and purification of both human cytochrome P450SCC and adrenodoxin [Woods, S.T., Sadleir, J., Downs, T., Triantopoulos, T., Haedlam, M.J. & Tuckey, R.C. (1998) Arch. Biochem. Biophys. 353, 109-115] has enabled us to perform studies with the membrane-reconstituted human enzymes to better understand the side-chain cleavage reaction in humans. Human P450SCC was successfully reconstituted into dioleoylphosphatidylcholine vesicles with and without cardiolipin and its enzymatic properties characterized in the membrane-bound state. Enhancement of the P450SCC activity and significant activation by cardiolipin were observed when human adrenodoxin instead of bovine adrenodoxin was used as electron donor. In the absence of cardiolipin, Km for cholesterol was decreased twice in the case of human adrenodoxin indicating enhanced cholesterol binding. On the other hand, in the presence of cardiolipin in the membrane both Km and V for cholesterol were decreased with human adrenodoxin as electron donor. Kinetic analysis of the interaction between human P450SCC and its redox partners provided evidence for enhanced binding of the human electron donor to human P450SCC indicated by both an increased V and decreased Kd for human adrenodoxin compared with the values with bovine adrenodoxin. Because no similar effects were observed in Tween 20 micelles, these results suggest that the phospholipid membrane may play an important role in the interaction of human adrenodoxin with human P450SCC.  (+info)

Interaction of CYP11B1 (cytochrome P-45011 beta) with CYP11A1 (cytochrome P-450scc) in COS-1 cells. (3/164)

The interactions of CYP11B1 (cytochrome P-45011beta), CYP11B2 (cytochrome P-450aldo) and CYP11A1 (cytochrome P-450scc) were investigated by cotransfection of their cDNA into COS-1 cells. The effect of CYP11A1 on CYP11B isozymes was examined by studying the conversion of 11-deoxycorticosterone to corticosterone, 18-hydroxycorticosterone and aldosterone. It was shown that when human or bovine CYP11B1 and CYP11A1 were cotransfected they competed for the reducing equivalents from the limiting source contained in COS-1 cells; this resulted in a decrease of the CYP11B activities without changes in the product formation patterns. The competition of human CYP11A1 with human CYP11B1 and CYP11B2 could be diminished with excess expression of bovine adrenodoxin. However, the coexpression of bovine CYP11B1 and CYP11A1 in the presence of adrenodoxin resulted in a stimulation of 11beta-hydroxylation activity of CYP11B1 and in a decrease of the 18-hydroxycorticosterone and aldosterone formation. These results suggest that the interactions of CYP11A1 with CYP11B1 and CYP11B2 do not have an identical regulatory function in human and in bovine adrenal tissue.  (+info)

Modulation of aldosterone biosynthesis by adrenodoxin mutants with different electron transport efficiencies. (4/164)

Aldosterone biosynthesis is highly regulated on different levels by hormones, potassium, lipid composition of the membrane and the molecular structure of its gene. Here, the influence of the electron transport efficiency from adrenodoxin (Adx) to CYP11B1 on the activities of bovine CYP11B1 has been investigated using a liposomal reconstitution system with truncated mutants of Adx. It could be clearly demonstrated that Adx mutants Adx 4-114 and Adx 4-108, possessing enhanced electron transfer abilities, produce increases in corticosterone and aldosterone biosynthesis. Based on the Vmax values of corticosterone and aldosterone formation, Adx 4-108 and Adx 4-114 enhance corticosterone synthesis 1.3-fold and aldosterone formation threefold and twofold, respectively. The production of 18-hydroxycorticosterone was changed only slightly in these Adx mutants. The effect of Adx 1-108 on the product patterns of bovine CYP11B1, human CYP11B1 and human CYP11B2 was confirmed in COS-1 cells by cotransfection of CYP11B- and Adx-containing expression vectors. It could be shown that Adx 1-108 enhances the formation of aldosterone by bovine CYP11B1 and by human CYP11B2, and stimulates the production of corticosterone by bovine CYP11B1 and human CYP11B1 and CYP11B2 also.  (+info)

Enzymatic properties of human 25-hydroxyvitamin D3 1alpha-hydroxylase coexpression with adrenodoxin and NADPH-adrenodoxin reductase in Escherichia coli. (5/164)

We have cloned human 25-hydroxyvitamin D3 1alpha-hydroxylase cDNAs from normal subjects and patients with pseudovitamin D-deficient rickets (PDDR), and expressed the cDNAs in Escherichia coli JM109 cells. Kinetic analysis of normal 1alpha-hydroxylase in the reconstituted system revealed that Km values for 25(OH)D3 and (24R), 25(OH)2D3 were 2.7 and 1.1 microM, respectively. The lower Km value and higher Vmax/Km value for (24R),25(OH)2D3 indicated that it is a better substrate than 25(OH)D3 for 1alpha-hydroxylase. These results are quite similar to those of mouse 1alpha-hydroxylase. To establish a highly sensitive in vivo system, 1alpha-hydroxylase, adrenodoxin and NADPH-adrenodoxin reductase were coexpressed in E. coli cells. The recombinant E. coli cells showed remarkably high 1alpha-hydroxylase activity, suggesting that the electrons were efficiently transferred from NADPH-adrenodoxin reductase through adrenodoxin to 1alpha-hydroxylase in E. coli cells. Using this system, the activities of four mutants of 1alpha-hydroxylase, R107H, G125E, R335P and P382S, derived from patients with PDDR were examined. Although no significant reduction in expression of these mutants was observed, none showed detectable activity. These results strongly suggest that the mutations found in the patients with PDDR completely abolished 1alpha-hydroxylase activity by replacement of one amino acid residue.  (+info)

A mitochondrial ferredoxin is essential for biogenesis of cellular iron-sulfur proteins. (6/164)

Iron-sulfur (Fe/S) cluster-containing proteins catalyze a number of electron transfer and metabolic reactions. The components and molecular mechanisms involved in the assembly of the Fe/S clusters have been identified only partially. In eukaryotes, mitochondria have been proposed to execute a crucial task in the generation of intramitochondrial and extramitochondrial Fe/S proteins. Herein, we identify the essential ferredoxin Yah1p of Saccharomyces cerevisiae mitochondria as a central component of the Fe/S protein biosynthesis machinery. Depletion of Yah1p by regulated gene expression resulted in a 30-fold accumulation of iron within mitochondria, similar to what has been reported for other components involved in Fe/S protein biogenesis. Yah1p was shown to be required for the assembly of Fe/S proteins both inside mitochondria and in the cytosol. Apparently, at least one of the steps of Fe/S cluster biogenesis within mitochondria requires reduction by ferredoxin. Our findings lend support to the idea of a primary function of mitochondria in the biosynthesis of Fe/S proteins outside the organelle. To our knowledge, Yah1p is the first member of the ferredoxin family for which a function in Fe/S cluster formation has been established. A similar role may be predicted for the bacterial homologs that are encoded within iron-sulfur cluster assembly (isc) operons of prokaryotes.  (+info)

Construction and characterization of a catalytic fusion protein system: P-450(11beta)-adrenodoxin reductase-adrenodoxin. (7/164)

Cortisol is an important intermediate for the production of steroidal drugs and can only be synthesized chemically by rather complicated multi-step procedures. The most critical step is the 11beta-hydroxylation of 11-deoxycortisol, which is catalyzed by a mitochondrial enzyme, P-450(11beta). Various fusion constructs of P-450(11beta) with its electron transfer components, adrenodoxin and adrenodoxin reductase, were produced by cDNA manipulation and were successfully expressed in COS-1 cells from which the hydroxylation activities were assayed. It was demonstrated that the fusion protein required both adrenodoxin reductase and adrenodoxin for its activity and was not able to receive electrons from an external source. The fusion protein with all three components had less activity than P-450(11beta) alone, receiving electrons from coexpressed or internal electron transfer components. The activities of the fusion proteins were determined mainly by the fusion sequence. The fusion protein with a sequence of P-450(11beta)-adrenodoxin reductase-adrenodoxin was more active than that of P-450(11beta)-adrenodoxin-adrenodoxin reductase, 1.5- and 3-fold for bovine and human P-450(11beta), respectively. Modification of the linker region by extending the size of the linker with various peptide sequences in the bovine P-450(11beta)-adrenodoxin reductase-adrenodoxin fusion protein indicated that the linker did not have significant effect on the P-450 activity. Taken together, the fusion protein obtained here can serve as a model for the investigation of electron transfer in P-450 systems and is of potential importance for biotechnological steroid production.  (+info)

Dual metabolic pathway of 25-hydroxyvitamin D3 catalyzed by human CYP24. (8/164)

Human 25-hydroxyvitamin D3 (25(OH)D3) 24-hydroxylase (CYP24) cDNA was expressed in Escherichia coli, and its enzymatic and spectral properties were revealed. The reconstituted system containing the membrane fraction prepared from recombinant E. coli cells, adrenodoxin and adrenodoxin reductase was examined for the metabolism of 25(OH)D3, 1alpha,25(OH)2D3 and their related compounds. Human CYP24 demonstrated a remarkable metabolism consisting of both C-23 and C-24 hydroxylation pathways towards both 25(OH)D3 and 1alpha,25(OH)2D3, whereas rat CYP24 showed almost no C-23 hydroxylation pathway [Sakaki, T. Sawada, N. Nonaka, Y. Ohyama, Y. & Inouye, K. (1999) Eur. J. Biochem. 262, 43-48]. HPLC analysis and mass spectrometric analysis revealed that human CYP24 catalyzed all the steps of the C-23 hydroxylation pathway from 25(OH)D3 via 23S, 25(OH)2D3, 23S,25,26(OH)3D3 and 25(OH)D3-26,23-lactol to 25(OH)D3-26, 23-lactone in addition to the C-24 hydroxylation pathway from 25(OH)D3 via 24R,25(OH)2D3, 24-oxo-25(OH)D3, 24-oxo-23S,25(OH)2D3 to 24,25,26,27-tetranor-23(OH)D3. On 1alpha,25(OH)2D3 metabolism, similar results were observed. These results strongly suggest that the single enzyme human CYP24 is greatly responsible for the metabolism of both 25(OH)D3 and 1alpha,25(OH)2D3. We also succeeded in the coexpression of CYP24, adrenodoxin and NADPH-adrenodoxin reductase in E. coli. Addition of 25(OH)D3 to the recombinant E. coli cell culture yielded most of the metabolites in both the C-23 and C-24 hydroxylation pathways. Thus, the E. coli expression system for human CYP24 appears quite useful in predicting the metabolism of vitamin D analogs used as drugs.  (+info)

Adrenodoxin is a small iron-sulfur protein that plays a crucial role in the steroidogenesis process within the mitochondria of cells. It functions as an electron carrier in the final steps of steroid hormone biosynthesis, specifically during the conversion of cholesterol to pregnenolone. This conversion is catalyzed by the cytochrome P450 side-chain cleavage enzyme (P450scc), which requires adrenodoxin to donate electrons for its activity. Adrenodoxin itself receives electrons from another protein, adrenodoxin reductase, in a series of redox reactions. Proper adrenodoxin function is essential for the production of various steroid hormones, including cortisol, aldosterone, and sex hormones.

Ferredoxin-NADP Reductase (FDNR) is an enzyme that catalyzes the electron transfer from ferredoxin to NADP+, reducing it to NADPH. This reaction plays a crucial role in several metabolic pathways, including photosynthesis and nitrogen fixation.

In photosynthesis, FDNR is located in the stroma of chloroplasts and receives electrons from ferredoxin, which is reduced by photosystem I. The enzyme then transfers these electrons to NADP+, generating NADPH, which is used in the Calvin cycle for carbon fixation.

In nitrogen fixation, FDNR is found in the nitrogen-fixing bacteria and receives electrons from ferredoxin, which is reduced by nitrogenase. The enzyme then transfers these electrons to NADP+, generating NADPH, which is used in the reduction of nitrogen gas (N2) to ammonia (NH3).

FDNR is a flavoprotein that contains a FAD cofactor and an iron-sulfur cluster. The enzyme catalyzes the electron transfer through a series of conformational changes that bring ferredoxin and NADP+ in close proximity, allowing for efficient electron transfer.

The Cholesterol Side-Chain Cleavage Enzyme, also known as Steroidogenic Acute Regulatory (StAR) protein or P450scc, is a complex enzymatic system that plays a crucial role in the production of steroid hormones. It is located in the inner mitochondrial membrane of steroid-producing cells, such as those found in the adrenal glands, gonads, and placenta.

The Cholesterol Side-Chain Cleavage Enzyme is responsible for converting cholesterol into pregnenolone, which is the first step in the biosynthesis of all steroid hormones, including cortisol, aldosterone, sex hormones, and vitamin D. This enzymatic complex consists of two components: a flavoprotein called NADPH-cytochrome P450 oxidoreductase, which provides electrons for the reaction, and a cytochrome P450 protein called CYP11A1, which catalyzes the actual cleavage of the cholesterol side chain.

Defects in the Cholesterol Side-Chain Cleavage Enzyme can lead to various genetic disorders, such as congenital lipoid adrenal hyperplasia (CLAH), a rare autosomal recessive disorder characterized by impaired steroidogenesis and accumulation of cholesteryl esters in the adrenal glands and gonads.

The adrenal cortex is the outer portion of the adrenal gland, which is located on top of the kidneys. It plays a crucial role in producing hormones that are essential for various bodily functions. The adrenal cortex is divided into three zones:

1. Zona glomerulosa: This outermost zone produces mineralocorticoids, primarily aldosterone. Aldosterone helps regulate sodium and potassium balance and thus influences blood pressure by controlling the amount of fluid in the body.
2. Zona fasciculata: The middle layer is responsible for producing glucocorticoids, with cortisol being the most important one. Cortisol regulates metabolism, helps manage stress responses, and has anti-inflammatory properties. It also plays a role in blood sugar regulation and maintaining the body's response to injury and illness.
3. Zona reticularis: The innermost zone produces androgens, primarily dehydroepiandrosterone (DHEA) and its sulfate form (DHEAS). These androgens are weak compared to those produced by the gonads (ovaries or testes), but they can be converted into more potent androgens or estrogens in peripheral tissues.

Disorders related to the adrenal cortex can lead to hormonal imbalances, affecting various bodily functions. Examples include Addison's disease (insufficient adrenal cortical hormone production) and Cushing's syndrome (excessive glucocorticoid levels).

Steroid 11-beta-hydroxylase is a crucial enzyme involved in the steroidogenesis pathway, specifically in the synthesis of cortisol and aldosterone, which are vital hormones produced by the adrenal glands. This enzyme is encoded by the CYP11B1 gene in humans.

The enzyme's primary function is to catalyze the conversion of 11-deoxycortisol to cortisol and 11-deoxycorticosterone to aldosterone through the process of hydroxylation at the 11-beta position of the steroid molecule. Cortisol is a critical glucocorticoid hormone that helps regulate metabolism, immune response, and stress response, while aldosterone is a mineralocorticoid hormone responsible for maintaining electrolyte and fluid balance in the body.

Deficiencies or mutations in the CYP11B1 gene can lead to various disorders, such as congenital adrenal hyperplasia (CAH), which may result in impaired cortisol and aldosterone production, causing hormonal imbalances and associated symptoms.

NADH, NADPH oxidoreductases are a class of enzymes that catalyze the redox reaction between NADH or NADPH and various electron acceptors. These enzymes play a crucial role in cellular metabolism by transferring electrons from NADH or NADPH to other molecules, which is essential for many biochemical reactions.

NADH (nicotinamide adenine dinucleotide hydrogen) and NADPH (nicotinamide adenine dinucleotide phosphate hydrogen) are coenzymes that act as electron carriers in redox reactions. They consist of a nicotinamide ring, which undergoes reduction or oxidation by accepting or donating electrons and a proton (H+).

NADH, NADPH oxidoreductases are classified based on their structure and mechanism of action. Some examples include:

1. Dehydrogenases: These enzymes catalyze the oxidation of NADH or NADPH to NAD+ or NADP+ while reducing an organic substrate. Examples include lactate dehydrogenase, alcohol dehydrogenase, and malate dehydrogenase.
2. Oxidases: These enzymes catalyze the oxidation of NADH or NADPH to NAD+ or NADP+ while reducing molecular oxygen (O2) to water (H2O). Examples include NADH oxidase and NADPH oxidase.
3. Reductases: These enzymes catalyze the reduction of various electron acceptors using NADH or NADPH as a source of electrons. Examples include glutathione reductase, thioredoxin reductase, and nitrate reductase.

Overall, NADH, NADPH oxidoreductases are essential for maintaining the redox balance in cells and play a critical role in various metabolic pathways, including energy production, detoxification, and biosynthesis.

Pregnenolone is defined as a steroid hormone produced in the body from cholesterol. It's often referred to as the "mother hormone" since many other hormones, including cortisol, aldosterone, progesterone, testosterone, and estrogen, are synthesized from it.

Pregnenolone is primarily produced in the adrenal glands but can also be produced in smaller amounts in the brain, skin, and sex organs (ovaries and testes). It plays a crucial role in various physiological processes such as maintaining membrane fluidity, acting as an antioxidant, and contributing to cognitive function.

However, it's important to note that while pregnenolone is a hormone, over-the-counter supplements containing this compound are not approved by the FDA for any medical use or condition. As always, consult with a healthcare provider before starting any new supplement regimen.

Ethyldimethylaminopropyl carbodiimide (EDC) is a type of chemical compound known as a carbodiimide, which is commonly used in the field of biochemistry and molecular biology as a cross-linking agent. EDC can react with carboxylic acid groups to form an active ester intermediate, which can then react with amino groups to form an amide bond. This property makes it useful for conjugating proteins, peptides, and other molecules that contain carboxyl and amino groups.

The medical definition of EDC is not well established since it is primarily used in research settings rather than in clinical practice. However, it is important to note that EDC can be toxic at high concentrations and should be handled with care. It may also cause irritation to the skin, eyes, and respiratory tract, so appropriate safety precautions should be taken when working with this compound.

"Cattle" is a term used in the agricultural and veterinary fields to refer to domesticated animals of the genus *Bos*, primarily *Bos taurus* (European cattle) and *Bos indicus* (Zebu). These animals are often raised for meat, milk, leather, and labor. They are also known as bovines or cows (for females), bulls (intact males), and steers/bullocks (castrated males). However, in a strict medical definition, "cattle" does not apply to humans or other animals.

Ferredoxins are iron-sulfur proteins that play a crucial role in electron transfer reactions in various biological systems, particularly in photosynthesis and nitrogen fixation. They contain one or more clusters of iron and sulfur atoms (known as the iron-sulfur cluster) that facilitate the movement of electrons between different molecules during metabolic processes.

Ferredoxins have a relatively simple structure, consisting of a polypeptide chain that binds to the iron-sulfur cluster. This simple structure allows ferredoxins to participate in a wide range of redox reactions and makes them versatile electron carriers in biological systems. They can accept electrons from various donors and transfer them to different acceptors, depending on the needs of the cell.

In photosynthesis, ferredoxins play a critical role in the light-dependent reactions by accepting electrons from photosystem I and transferring them to NADP+, forming NADPH. This reduced form of nicotinamide adenine dinucleotide phosphate (NADPH) is then used in the Calvin cycle for carbon fixation and the production of glucose.

In nitrogen fixation, ferredoxins help transfer electrons to the nitrogenase enzyme complex, which reduces atmospheric nitrogen gas (N2) into ammonia (NH3), making it available for assimilation by plants and other organisms.

Overall, ferredoxins are essential components of many metabolic pathways, facilitating electron transfer and energy conversion in various biological systems.

The Cytochrome P-450 (CYP450) enzyme system is a group of enzymes found primarily in the liver, but also in other organs such as the intestines, lungs, and skin. These enzymes play a crucial role in the metabolism and biotransformation of various substances, including drugs, environmental toxins, and endogenous compounds like hormones and fatty acids.

The name "Cytochrome P-450" refers to the unique property of these enzymes to bind to carbon monoxide (CO) and form a complex that absorbs light at a wavelength of 450 nm, which can be detected spectrophotometrically.

The CYP450 enzyme system is involved in Phase I metabolism of xenobiotics, where it catalyzes oxidation reactions such as hydroxylation, dealkylation, and epoxidation. These reactions introduce functional groups into the substrate molecule, which can then undergo further modifications by other enzymes during Phase II metabolism.

There are several families and subfamilies of CYP450 enzymes, each with distinct substrate specificities and functions. Some of the most important CYP450 enzymes include:

1. CYP3A4: This is the most abundant CYP450 enzyme in the human liver and is involved in the metabolism of approximately 50% of all drugs. It also metabolizes various endogenous compounds like steroids, bile acids, and vitamin D.
2. CYP2D6: This enzyme is responsible for the metabolism of many psychotropic drugs, including antidepressants, antipsychotics, and beta-blockers. It also metabolizes some endogenous compounds like dopamine and serotonin.
3. CYP2C9: This enzyme plays a significant role in the metabolism of warfarin, phenytoin, and nonsteroidal anti-inflammatory drugs (NSAIDs).
4. CYP2C19: This enzyme is involved in the metabolism of proton pump inhibitors, antidepressants, and clopidogrel.
5. CYP2E1: This enzyme metabolizes various xenobiotics like alcohol, acetaminophen, and carbon tetrachloride, as well as some endogenous compounds like fatty acids and prostaglandins.

Genetic polymorphisms in CYP450 enzymes can significantly affect drug metabolism and response, leading to interindividual variability in drug efficacy and toxicity. Understanding the role of CYP450 enzymes in drug metabolism is crucial for optimizing pharmacotherapy and minimizing adverse effects.

I'm sorry for any confusion, but "nuclear physics" is not a term that has a medical definition. Nuclear physics is a branch of physics that deals with the properties and behavior of atomic nuclei, including their composition, structure, and reactions. It is studied in order to better understand the nature of matter and energy, and it has important applications in fields such as nuclear power, nuclear medicine, and nuclear weapons. However, it is not a term that is used in the context of medical diagnosis or treatment. If you have any questions about a medical term or concept, I would be happy to try to help!

The Electron Transport Chain (ETC) is a series of complexes in the inner mitochondrial membrane that are involved in the process of cellular respiration. It is the final pathway for electrons derived from the oxidation of nutrients such as glucose, fatty acids, and amino acids to be transferred to molecular oxygen. This transfer of electrons drives the generation of a proton gradient across the inner mitochondrial membrane, which is then used by ATP synthase to produce ATP, the main energy currency of the cell.

The electron transport chain consists of four complexes (I-IV) and two mobile electron carriers (ubiquinone and cytochrome c). Electrons from NADH and FADH2 are transferred to Complex I and Complex II respectively, which then pass them along to ubiquinone. Ubiquinone then transfers the electrons to Complex III, which passes them on to cytochrome c. Finally, cytochrome c transfers the electrons to Complex IV, where they combine with oxygen and protons to form water.

The transfer of electrons through the ETC is accompanied by the pumping of protons from the mitochondrial matrix to the intermembrane space, creating a proton gradient. The flow of protons back across the inner membrane through ATP synthase drives the synthesis of ATP from ADP and inorganic phosphate.

Overall, the electron transport chain is a crucial process for generating energy in the form of ATP in the cell, and it plays a key role in many metabolic pathways.

Polysorbates are a type of nonionic surfactant (a compound that lowers the surface tension between two substances, such as oil and water) commonly used in pharmaceuticals, foods, and cosmetics. They are derived from sorbitol and reacted with ethylene oxide to create a polyoxyethylene structure. The most common types of polysorbates used in medicine are polysorbate 20, polysorbate 40, and polysorbate 60, which differ in the number of oxyethylene groups in their molecular structure.

Polysorbates are often added to pharmaceutical formulations as emulsifiers, solubilizers, or stabilizers. They help to improve the solubility and stability of drugs that are otherwise insoluble in water, allowing for better absorption and bioavailability. Polysorbates can also prevent the aggregation and precipitation of proteins in injectable formulations.

In addition to their use in pharmaceuticals, polysorbates are also used as emulsifiers in food products such as ice cream, salad dressings, and baked goods. They help to mix oil and water-based ingredients together and prevent them from separating. In cosmetics, polysorbates are used as surfactants, solubilizers, and stabilizers in a variety of personal care products.

It is important to note that some people may have allergic reactions to polysorbates, particularly those with sensitivities to sorbitol or other ingredients used in their production. Therefore, it is essential to carefully consider the potential risks and benefits of using products containing polysorbates in individuals who may be at risk for adverse reactions.

Steroid hydroxylases are enzymes that catalyze the addition of a hydroxyl group (-OH) to a steroid molecule. These enzymes are located in the endoplasmic reticulum and play a crucial role in the biosynthesis of various steroid hormones, such as cortisol, aldosterone, and sex hormones. The hydroxylation reaction catalyzed by these enzymes increases the polarity and solubility of steroids, allowing them to be further metabolized and excreted from the body.

The most well-known steroid hydroxylases are part of the cytochrome P450 family, specifically CYP11A1, CYP11B1, CYP11B2, CYP17A1, CYP19A1, and CYP21A2. Each enzyme has a specific function in steroid biosynthesis, such as converting cholesterol to pregnenolone (CYP11A1), hydroxylating the 11-beta position of steroids (CYP11B1 and CYP11B2), or performing multiple hydroxylation reactions in the synthesis of sex hormones (CYP17A1, CYP19A1, and CYP21A2).

Defects in these enzymes can lead to various genetic disorders, such as congenital adrenal hyperplasia, which is characterized by impaired steroid hormone biosynthesis.

Mitochondria are specialized structures located inside cells that convert the energy from food into ATP (adenosine triphosphate), which is the primary form of energy used by cells. They are often referred to as the "powerhouses" of the cell because they generate most of the cell's supply of chemical energy. Mitochondria are also involved in various other cellular processes, such as signaling, differentiation, and apoptosis (programmed cell death).

Mitochondria have their own DNA, known as mitochondrial DNA (mtDNA), which is inherited maternally. This means that mtDNA is passed down from the mother to her offspring through the egg cells. Mitochondrial dysfunction has been linked to a variety of diseases and conditions, including neurodegenerative disorders, diabetes, and aging.

NADP (Nicotinamide Adenine Dinucleotide Phosphate) is a coenzyme that plays a crucial role as an electron carrier in various redox reactions in the human body. It exists in two forms: NADP+, which functions as an oxidizing agent and accepts electrons, and NADPH, which serves as a reducing agent and donates electrons.

NADPH is particularly important in anabolic processes, such as lipid and nucleotide synthesis, where it provides the necessary reducing equivalents to drive these reactions forward. It also plays a critical role in maintaining the cellular redox balance by participating in antioxidant defense mechanisms that neutralize harmful reactive oxygen species (ROS).

In addition, NADP is involved in various metabolic pathways, including the pentose phosphate pathway and the Calvin cycle in photosynthesis. Overall, NADP and its reduced form, NADPH, are essential molecules for maintaining proper cellular function and energy homeostasis.

Cytochrome c is a small protein that is involved in the electron transport chain, a key part of cellular respiration in which cells generate energy in the form of ATP. Cytochrome c contains a heme group, which binds to and transports electrons. The cytochrome c group refers to a class of related cytochromes that have similar structures and functions. These proteins are found in the mitochondria of eukaryotic cells (such as those of plants and animals) and in the inner membranes of bacteria. They play a crucial role in the production of energy within the cell, and are also involved in certain types of programmed cell death (apoptosis).

Carbodiimides are a class of chemical compounds with the general formula R-N=C=N-R, where R can be an organic group. They are widely used in the synthesis of various chemical and biological products due to their ability to act as dehydrating agents, promoting the formation of amide bonds between carboxylic acids and amines.

In the context of medical research and biochemistry, carbodiimides are often used to modify proteins, peptides, and other biological molecules for various purposes, such as labeling, cross-linking, or functionalizing. For example, the carbodiimide cross-linker EDC (1-ethyl-3-(3-dimethylaminopropyl)carbodiimide) is commonly used to create stable amide bonds between proteins and other molecules in a process known as "EDC coupling."

It's important to note that carbodiimides can be potentially toxic and should be handled with care. They can cause irritation to the skin, eyes, and respiratory tract, and prolonged exposure can lead to more serious health effects. Therefore, appropriate safety precautions should be taken when working with these compounds in a laboratory setting.

Electromagnetic phenomena refer to the interactions and effects that occur due to the combination of electrically charged particles and magnetic fields. These phenomena are described by the principles of electromagnetism, a branch of physics that deals with the fundamental forces between charged particles and their interaction with electromagnetic fields.

Electromagnetic phenomena can be observed in various forms, including:

1. Electric fields: The force that exists between charged particles at rest or in motion. Positive charges create an electric field that points away from them, while negative charges create an electric field that points towards them.
2. Magnetic fields: The force that exists around moving charges or current-carrying wires. Magnets and moving charges produce magnetic fields that exert forces on other moving charges or current-carrying wires.
3. Electromagnetic waves: Self-propagating disturbances in electric and magnetic fields, which can travel through space at the speed of light. Examples include visible light, radio waves, microwaves, and X-rays.
4. Electromagnetic induction: The process by which a changing magnetic field generates an electromotive force (EMF) in a conductor, leading to the flow of electric current.
5. Faraday's law of induction: A fundamental principle that relates the rate of change of magnetic flux through a closed loop to the induced EMF in the loop.
6. Lenz's law: A consequence of conservation of energy, which states that the direction of an induced current is such that it opposes the change in magnetic flux causing it.
7. Electromagnetic radiation: The emission and absorption of electromagnetic waves by charged particles undergoing acceleration or deceleration.
8. Maxwell's equations: A set of four fundamental equations that describe how electric and magnetic fields interact, giving rise to electromagnetic phenomena.

In a medical context, electromagnetic phenomena can be harnessed for various diagnostic and therapeutic applications, such as magnetic resonance imaging (MRI), electrocardiography (ECG), electromyography (EMG), and transcranial magnetic stimulation (TMS).

Cholestanetriol 26-monooxygenase is an enzyme that is involved in the metabolism of bile acids and steroids in the body. This enzyme is responsible for adding a hydroxyl group (-OH) to the cholestanetriol molecule at position 26, which is a critical step in the conversion of cholestanetriol to bile acids.

The gene that encodes this enzyme is called CYP3A4, which is located on chromosome 7 in humans. Mutations in this gene can lead to various metabolic disorders, including impaired bile acid synthesis and altered steroid hormone metabolism.

Deficiency or dysfunction of cholestanetriol 26-monooxygenase has been associated with several diseases, such as liver disease, cerebrotendinous xanthomatosis, and some forms of cancer. Therefore, understanding the function and regulation of this enzyme is essential for developing new therapies and treatments for these conditions.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

Electron Spin Resonance (ESR) Spectroscopy, also known as Electron Paramagnetic Resonance (EPR) Spectroscopy, is a technique used to investigate materials with unpaired electrons. It is based on the principle of absorption of energy by the unpaired electrons when they are exposed to an external magnetic field and microwave radiation.

In this technique, a sample is placed in a magnetic field and microwave radiation is applied. The unpaired electrons in the sample absorb energy and change their spin state when the energy of the microwaves matches the energy difference between the spin states. This absorption of energy is recorded as a function of the magnetic field strength, producing an ESR spectrum.

ESR spectroscopy can provide information about the number, type, and behavior of unpaired electrons in a sample, as well as the local environment around the electron. It is widely used in physics, chemistry, and biology to study materials such as free radicals, transition metal ions, and defects in solids.

The adrenal glands are a pair of endocrine glands that are located on top of the kidneys. Each gland has two parts: the outer cortex and the inner medulla. The adrenal cortex produces hormones such as cortisol, aldosterone, and androgens, which regulate metabolism, blood pressure, and other vital functions. The adrenal medulla produces catecholamines, including epinephrine (adrenaline) and norepinephrine (noradrenaline), which help the body respond to stress by increasing heart rate, blood pressure, and alertness.

Oxidation-Reduction (redox) reactions are a type of chemical reaction involving a transfer of electrons between two species. The substance that loses electrons in the reaction is oxidized, and the substance that gains electrons is reduced. Oxidation and reduction always occur together in a redox reaction, hence the term "oxidation-reduction."

In biological systems, redox reactions play a crucial role in many cellular processes, including energy production, metabolism, and signaling. The transfer of electrons in these reactions is often facilitated by specialized molecules called electron carriers, such as nicotinamide adenine dinucleotide (NAD+/NADH) and flavin adenine dinucleotide (FAD/FADH2).

The oxidation state of an element in a compound is a measure of the number of electrons that have been gained or lost relative to its neutral state. In redox reactions, the oxidation state of one or more elements changes as they gain or lose electrons. The substance that is oxidized has a higher oxidation state, while the substance that is reduced has a lower oxidation state.

Overall, oxidation-reduction reactions are fundamental to the functioning of living organisms and are involved in many important biological processes.

Spectrophotometry is a technical analytical method used in the field of medicine and science to measure the amount of light absorbed or transmitted by a substance at specific wavelengths. This technique involves the use of a spectrophotometer, an instrument that measures the intensity of light as it passes through a sample.

In medical applications, spectrophotometry is often used in laboratory settings to analyze various biological samples such as blood, urine, and tissues. For example, it can be used to measure the concentration of specific chemicals or compounds in a sample by measuring the amount of light that is absorbed or transmitted at specific wavelengths.

In addition, spectrophotometry can also be used to assess the properties of biological tissues, such as their optical density and thickness. This information can be useful in the diagnosis and treatment of various medical conditions, including skin disorders, eye diseases, and cancer.

Overall, spectrophotometry is a valuable tool for medical professionals and researchers seeking to understand the composition and properties of various biological samples and tissues.

Ferricyanides are a class of chemical compounds that contain the ferricyanide ion (Fe(CN)6−3). The ferricyanide ion is composed of a central iron atom in the +3 oxidation state, surrounded by six cyanide ligands. Ferricyanides are strong oxidizing agents and are used in various chemical reactions, including analytical chemistry and as reagents in organic synthesis.

It's important to note that while ferricyanides themselves are not highly toxic, they can release cyanide ions if they are decomposed or reduced under certain conditions. Therefore, they should be handled with care and used in well-ventilated areas.

... (Enzyme Nomenclature name: adrenodoxin-NADP+ reductase, EC 1.18.1.6), was first isolated from bovine ... Müller JJ, Lapko A, Bourenkov G, Ruckpaul K, Heinemann U (Jan 2001). "Adrenodoxin reductase-adrenodoxin complex structure ... It catalyzes the following reaction: NADPH + 2 oxidized adrenodoxin -→ 2 reduced adrenodoxin + NADP+ + H+ The cDNA for ... Hanukoglu I, Hanukoglu Z (May 1986). "Stoichiometry of mitochondrial cytochromes P-450, adrenodoxin and adrenodoxin reductase ...
... (EC 1.18.1.6, adrenodoxin reductase, nicotinamide adenine dinucleotide phosphate-adrenodoxin ... Hanukoglu I, Hanukoglu Z (May 1986). "Stoichiometry of mitochondrial cytochromes P-450, adrenodoxin and adrenodoxin reductase ... 2 oxidized adrenodoxin + NADPH + H+ Adrenodoxin-NADP+ reductase is a flavoprotein (FAD). Omura T, Sanders E, Estabrook RW, ... Adrenodoxin-NADP++reductase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 1.18.1 ...
... adrenodoxin transfers an electron from NADPH:adrenodoxin reductase to membrane-bound cytochrome P450. In bacteria, ... Adrenodoxin (adrenal ferredoxin; InterPro: IPR001055), putidaredoxin, and terpredoxin make up a family of soluble Fe2S2 ... Ewen KM, Ringle M, Bernhardt R (June 2012). "Adrenodoxin--a versatile ferredoxin". IUBMB Life. 64 (6): 506-12. doi:10.1002/iub. ... Despite low sequence similarity between adrenodoxin-type and plant-type ferredoxins, the two classes have a similar folding ...
Hanukoglu I (2017). "Conservation of the Enzyme-Coenzyme Interfaces in FAD and NADP Binding Adrenodoxin Reductase-A Ubiquitous ... Phylogenetic analysis of the NADP binding enzyme adrenodoxin reductase revealed that from prokaryotes, through metazoa and up ... Hanukoglu I, Gutfinger T (March 1989). "cDNA sequence of adrenodoxin reductase. Identification of NADP-binding sites in ...
Hanukoglu I, Hanukoglu Z (May 1986). "Stoichiometry of mitochondrial cytochromes P-450, adrenodoxin and adrenodoxin reductase ... "Electron leakage from the mitochondrial NADPH-adrenodoxin reductase-adrenodoxin-P450scc (cholesterol side chain cleavage) ... His lab was the first to clone the cDNAs and the gene coding for adrenodoxin reductase - the first enzyme in the electron ... Cholesterol and adrenodoxin interactions at equilibrium and during turnover". The Journal of Biological Chemistry. 256 (9): ...
An FAD containing adrenodoxin reductase (AR) and a small iron-sulfur group containing protein named adrenodoxin. FAD is ... The two electrons in reduced FAD are transferred one a time to adrenodoxin which in turn donates the single electron to the ... Ziegler GA, Vonrhein C, Hanukoglu I, Schulz GE (Jun 1999). "The structure of adrenodoxin reductase of mitochondrial P450 ... Hanukoglu I (2017). "Conservation of the Enzyme-Coenzyme Interfaces in FAD and NADP Binding Adrenodoxin Reductase-A Ubiquitous ...
Adrenodoxin is a small iron-sulfur protein that can accept and carry a single electron. Adrenodoxin functions as an electron ... Adrenal ferredoxin (also adrenodoxin (ADX), adrenodoxin, mitochondrial, hepatoredoxin, ferredoxin-1 (FDX1)) is a protein that ... These two electrons are transferred one a time to adrenodoxin. Adrenodoxin in return reduces mitochondrial cytochrome P450. ... adrenodoxin to 11q22; adrenodoxin reductase to 17q24-q25; and P450c17 to 10q24-q25". DNA Cell Biol. 10 (5): 359-65. doi:10.1089 ...
Adrenodoxin reductase: This enzyme is present ubiquitously in most organisms. It transfers two electrons from NADPH to FAD. In ... Hanukoglu I (December 2017). "Conservation of the Enzyme-Coenzyme Interfaces in FAD and NADP Binding Adrenodoxin Reductase-A ...
Geren LM, Millett F (October 1981). "Fluorescence energy transfer studies of the interaction between adrenodoxin and cytochrome ...
In the adrenal cortex, the concentration of adrenodoxin is similar to that of P450scc, but adrenodoxin reductase is expressed ... The electrons are transferred from NADPH to P450scc via two electron transfer proteins: adrenodoxin reductase and adrenodoxin. ... P450scc is associated with the inner mitochondrial membrane, facing the interior (matrix). Adrenodoxin and adrenodoxin ... Hanukoglu I, Hanukoglu Z (May 1986). "Stoichiometry of mitochondrial cytochromes P-450, adrenodoxin and adrenodoxin reductase ...
The mitochondrial P450 system electron transport chain including adrenodoxin reductase and adrenodoxin has been shown to leak ... "Electron leakage from the mitochondrial NADPH-adrenodoxin reductase-adrenodoxin-P450scc (cholesterol side chain cleavage) ... plasma levels of progesterone increase in parallel to the levels of P450scc and its electron donor adrenodoxin, indicating that ...
They include cytochrome c, cupredoxins, high potential iron protein, adrenodoxin reductase, some flavoproteins, and others. ...
"Electron leakage from the mitochondrial NADPH-adrenodoxin reductase-adrenodoxin-P450scc (cholesterol side chain cleavage) ...
Hanukoglu I (2017). "Conservation of the Enzyme-Coenzyme Interfaces in FAD and NADP Binding Adrenodoxin Reductase-A Ubiquitous ... the specific residues involved in the binding of the electron transfer protein adrenodoxin to its reductase were identified as ... two basic Arg residues on the surface of the reductase and two acidic Asp residues on the adrenodoxin. More recent work on the ...
The flavin is generally tightly bound (as in adrenodoxin reductase, wherein the FAD is buried deeply). About 5-10% of ... The flavoprotein family contains a diverse range of enzymes, including: Adrenodoxin reductase that is involved in steroid ... "Conservation of the Enzyme-Coenzyme Interfaces in FAD and NADP Binding Adrenodoxin Reductase-A Ubiquitous Enzyme". Journal of ...
Mitochondrial P450 systems which employ adrenodoxin reductase and adrenodoxin to transfer electrons from NADPH to P450. ...
Hanukoglu I (December 2017). "Conservation of the Enzyme-Coenzyme Interfaces in FAD and NADP Binding Adrenodoxin Reductase-A ...
... by immunohistochemistry and absolute dependence on mitochondrial electron donors adrenodoxin reductase and adrenodoxin. Rabbit ...
They are located within the mitochondria and require adrenodoxin as a cofactor (except 21-hydroxylase and 17α-hydroxylase). ...
2 reduced adrenodoxin + 2 H+ + O2 ⇌ calcitriol + 2 oxidized adrenodoxin + H2O The enzyme is also able to oxidize ercalcidiol ( ... "Enzymatic properties of human 25-hydroxyvitamin D3 1alpha-hydroxylase coexpression with adrenodoxin and NADPH-adrenodoxin ...
They are located within the mitochondria and require adrenodoxin as a cofactor (except 21-hydroxylase and 17α-hydroxylase). ...
In mitochondrial monooxygenase systems, adrenodoxin functions as a soluble electron carrier between NADPH:adrenodoxin reductase ... The general scheme of electron flow in the P450 systems containing adrenodoxin-type ferredoxins is: The sterol demethylase ...
The glutathione-reductase-type FNRs (InterPro: IPR022890, InterPro: IPR021163), sometimes named adrenodoxin-NADP+ reductase for ... Other names in common use include: adrenodoxin reductase, ferredoxin-NADP+ reductase, ferredoxin-NADP+ oxidoreductase, ... reduced nicotinamide adenine dinucleotide phosphate-adrenodoxin, reductase, and TPNH-ferredoxin reductase During photosynthesis ...
A coenzyme system called adrenodoxin reductase transfers electrons to the P450 enzyme which initiates the oxidation-reduction ...
2 reduced adrenodoxin + 2 H+ + O2 = all-trans-3,4-didehydroretinol + 2 oxidized adrenodoxin + 2 H2O. The catalytic efficiency ...
... adrenodoxin - aequorin - aerobic respiration - agonist - alanine - albumin - alcohol - alcoholic fermentation - alicyclic ...
... a surgical procedure Adrenodoxin-NADP+ reductase, an enzyme ADR (treaty), a treaty governing transport of hazardous materials ...
... adrenodoxin MeSH D12.776.556.579.374.375.150 - ferredoxin-nitrite reductase MeSH D12.776.556.579.374.375.275 - ferredoxins MeSH ...
... adrenodoxin - aerobic organism - age structure - agonist - AIDS - albumin - aldehydes - aldosterone - algae - allantois - ...
HtrA serine peptidase 2 Adrenodoxin reductase Heme biosynthesis Protoporphyrinogen oxidase Ferrochelatase Uncoupling protein ...
Adrenodoxin reductase (Enzyme Nomenclature name: adrenodoxin-NADP+ reductase, EC 1.18.1.6), was first isolated from bovine ... Müller JJ, Lapko A, Bourenkov G, Ruckpaul K, Heinemann U (Jan 2001). "Adrenodoxin reductase-adrenodoxin complex structure ... It catalyzes the following reaction: NADPH + 2 oxidized adrenodoxin -→ 2 reduced adrenodoxin + NADP+ + H+ The cDNA for ... Hanukoglu I, Hanukoglu Z (May 1986). "Stoichiometry of mitochondrial cytochromes P-450, adrenodoxin and adrenodoxin reductase ...
Bovine adrenodoxin (Adx) and adrenodoxin reductase (AdR) are involved in steroid hormone biosynthesis in the adrenal gland ... Lambeth, J. D. & Kamin, H. Adrenodoxin reductase and adrenodoxin. Mechanisms of reduction of ferricyanide and cytochrome c. J. ... Muller, J. J., Lapko, A., Bourenkov, G., Ruckpaul, K. & Heinemann, U. Adrenodoxin reductase-adrenodoxin complex structure ... Direct expression of adrenodoxin reductase in Escherichia coli and the functional characterization. Biol. Pharm. Bull. 16, 627- ...
Adrenodoxin and cytochromes P450 ea0012s15 * Hexose-6-phosphate dehydrogenase and glucocorticoid metabolism ...
Adrenodoxin. 9e-24. At4g05450. adrenodoxin-like ferredoxin 2. C.G.. S.X.. Please select. KEGG (integral). Gramene (integral). ...
2Dbidimensional3Dtridimensional8-HQ8-hydroxyquinolineαSynα-synucleinµwmicrowaveAβamyloid βAAZTA6-amino-6-methylperhydro-1,4-diazepinetetraacetic acidAdRadrenoxi
The electron transport system which catalyzes this reaction consists of adrenodoxin reductase, NADP, adrenodoxin, and ... Adrenodoxin. An iron-sulfur protein which serves as an electron carrier in enzymatic steroid hydroxylation reactions in adrenal ... An enzyme that catalyzes the oxidation and reduction of FERREDOXIN or ADRENODOXIN in the presence of NADP. EC 1.18.1.2 was ... 4-alpha-GlucosidaseCarboxylic AcidsAdrenodoxinHydroxylaminesRabbitsIndicators and ReagentsCyanogen BromideBromosuccinimide ...
Adrenodoxin * Fmn Reductase * Saccharomyces Cerevisiae * Reverse Transcriptase Polymerase Chain Reaction * Transcription ...
NADPH:adrenodoxin oxidoreductase, mitochondrial. MASRCWRWWGWSAWPRTRLPPAGSTPSFCHHFSTQEKTPQICVVGSGPAG.... unknown. Peroxisomal ...
NADPH-adrenodoxin reductase activity. go/ molecular_function. Pyrimidine metabolism. kegg/ kegg pathway. ...
Self-association of adrenodoxin studied by using analytical ultracentrifugation.. Behlke, J. and Ristau, O. and Mueller, E.C. ...
The mitochondrial P450 system electron transport chain including adrenodoxin reductase and adrenodoxin has been shown to leak ... "Electron leakage from the mitochondrial NADPH-adrenodoxin reductase-adrenodoxin-P450scc (cholesterol side chain cleavage) ... plasma levels of progesterone increase in parallel to the levels of P450scc and its electron donor adrenodoxin, indicating that ...
Monooxygenase reactions demand electron donation from NADPH by way of adrenodoxin reductase and adrenodoxin [26,27]. Here, ...
An enzyme that catalyzes the oxidation and reduction of FERREDOXIN or ADRENODOXIN in the presence of NADP. EC 1.18.1.2 was ...
Li J, Saxena S, Pain D, Dancis A: Adrenodoxin reductase homolog (Arh1p) of yeast mitochondria required for iron homeostasis. J ... a new essential gene that codes for a protein homologous to the human adrenodoxin reductase. Yeast. 1998, 14 (9): 839-846. ... a new essential gene that codes for a protein homologous to human adrenodoxin. Gene. 1999, 233 (1-2): 197-203. ...
Assignment of the Functional Gene for Human Adrenodoxin to Chromosome 11q13-,qter and of Adrenodoxin Pseudogenes to Chromosome ...
General mechanism protein adrenodoxin is mandatory for far back as the if you do need their jobs and have a great body without ...
73 Desager K, Vermeulen F, Bodart E. They are located within the mitochondria and require adrenodoxin as a cofactor except 21 ...
... adrenodoxin reductase (Adrp), and adrenodoxin (Adxp), and the yield was 60 mg/L (Duport et al. 1998). The P450-catalyzed ...
... coli will be the active display of dimeric adrenodoxin, dimeric sorbit dehydrogenase, mul timeric nitrilase and dimeric prenyl ...
Hanukoglu, I.; Gutfinger, T. 1988: Complementary dna sequence of adrenodoxin reductase identification of a consensus sequence ...
Adrenodoxin [D12.776.556.579.374.375.025] Adrenodoxin * Electron Transport Complex I [D12.776.556.579.374.375.140] ...
Adrenodoxin. *Electron Transport Complex I. *Electron Transport Complex II. *Electron Transport Complex III ...
Cholesterol_sulfate + reduced_adrenodoxin + O2 <=> pregnenolone_sulfate + 17alpha-hydroxypregnenolone + dehydroepiandrosterone_ ...
They are located within the mitochondria and require adrenodoxin as a cofactor (except 21-hydroxylase and 17α-hydroxylase). ...
The best quality, top Feline Leukemia Virus, p27 (FeLV) Antibody, Feline Leukemia Virus, p27 (FeLV) Antibody, FEN1 antibody, FER Antibody, FERMT2 antibody products prices, the best delivery. ...
  • However, HPTE did not change mRNA levels of the P450scc system (P450scc, adrenodoxin reductase and adrenodoxin) as well as P450scc protein levels. (cdc.gov)
  • The mitochondrial P450 system electron transport chain including adrenodoxin reductase and adrenodoxin has been shown to leak electrons leading to the formation of superoxide radical. (hyperlinked.wiki)
  • Monooxygenase reactions demand electron donation from NADPH by way of adrenodoxin reductase and adrenodoxin [26,27]. (piminhibitor.com)
  • Later, in some studies, the enzyme was also referred to as a "ferredoxin reductase", as adrenodoxin is a ferredoxin. (wikipedia.org)
  • The assignment of the name "ferredoxin reductase" has been criticized as a misnomer because determination of the structure of adrenodoxin reductase revealed that it is completely different from that of plant ferredoxin reductase and there is no homology between these two enzymes. (wikipedia.org)
  • Adrenodoxin reductase (Enzyme Nomenclature name: adrenodoxin-NADP+ reductase, EC 1.18.1.6), was first isolated from bovine adrenal cortex where it functions as the first enzyme in the mitochondrial P450 systems that catalyze essential steps in steroid hormone biosynthesis. (wikipedia.org)
  • Bovine adrenodoxin (Adx) and adrenodoxin reductase (AdR) are involved in steroid hormone biosynthesis in the adrenal gland mitochondria. (nature.com)
  • During the bovine estrous cycle, plasma levels of progesterone increase in parallel to the levels of P450scc and its electron donor adrenodoxin, indicating that progesterone secretion is a result of enhanced expression of P450scc in the corpus luteum. (hyperlinked.wiki)
  • The electron transport system which catalyzes this reaction consists of adrenodoxin reductase, NADP, adrenodoxin, and cytochrome P-450. (lookformedical.com)
  • Adrenodoxin reductase is a flavoprotein as it carries a FAD type coenzyme. (wikipedia.org)
  • Adrenodoxin functions as a mobile shuttle that transfers electrons between ADXR and mitochondrial P450s. (wikipedia.org)
  • The FAD coenzyme receives two electrons from NADPH and transfers them one at a time to the electron transfer protein adrenodoxin. (wikipedia.org)
  • It catalyzes the following reaction: NADPH + 2 oxidized adrenodoxin -→ 2 reduced adrenodoxin + NADP+ + H+ The cDNA for adrenodoxin reductase was first cloned in 1987. (wikipedia.org)
  • Adrenodoxin reductase has two domains that bind NADPH and FAD separately. (wikipedia.org)
  • An enzyme that catalyzes the oxidation and reduction of FERREDOXIN or ADRENODOXIN in the presence of NADP. (lookformedical.com)
  • Examination of complete genome sequences revealed that adrenodoxin reductase gene is present in most metazoans and prokaryotes. (wikipedia.org)
  • The name of the enzyme was coined based on its function to reduce a [2Fe-2S] (2 iron, 2 sulfur) electron-transfer protein that was named adrenodoxin. (wikipedia.org)
  • Adrenodoxin reductase (Enzyme Nomenclature name: adrenodoxin-NADP+ reductase, EC 1.18.1.6), was first isolated from bovine adrenal cortex where it functions as the first enzyme in the mitochondrial P450 systems that catalyze essential steps in steroid hormone biosynthesis. (wikipedia.org)
  • Examination of complete genome sequences revealed that adrenodoxin reductase gene is present in most metazoans and prokaryotes. (wikipedia.org)
  • Later, in some studies, the enzyme was also referred to as a "ferredoxin reductase", as adrenodoxin is a ferredoxin. (wikipedia.org)
  • The assignment of the name "ferredoxin reductase" has been criticized as a misnomer because determination of the structure of adrenodoxin reductase revealed that it is completely different from that of plant ferredoxin reductase and there is no homology between these two enzymes. (wikipedia.org)
  • Adrenodoxin reductase is a flavoprotein as it carries a FAD type coenzyme. (wikipedia.org)
  • It catalyzes the following reaction: NADPH + 2 oxidized adrenodoxin -→ 2 reduced adrenodoxin + NADP+ + H+ The cDNA for adrenodoxin reductase was first cloned in 1987. (wikipedia.org)
  • Adrenodoxin reductase has two domains that bind NADPH and FAD separately. (wikipedia.org)
  • Seven of the 57 human cytochrome P450 (P450) enzymes are mitochondrial and carry out important reactions with steroids and vitamins A and D. These seven P450s utilize an electron transport chain that includes NADPH, NADPH-adrenodoxin reductase (AdR), and adrenodoxin (Adx) instead of the diflavin NADPH-P450 reductase (POR) used by the other P450s in the endoplasmic reticulum. (nih.gov)
  • 4. Immunohistochemical demonstration of adrenodoxin reductase in bovine and human adrenals. (nih.gov)
  • The electron transport system which catalyzes this reaction consists of adrenodoxin reductase, NADP , adrenodoxin, and cytochrome P-450. (nih.gov)
  • Pyridoxal phosphate induced association reactions of adrenodoxin and adrenodoxin-reductase. (mdc-berlin.de)
  • Through redox partners combination screening, we reveal the optimal redox partner pair of S. scrofa adrenodoxin and C. hircus adrenodoxin reductase. (hhu.de)
  • Furthermore, such spectral data are acquired for complexes with the natural redox partner, adrenodoxin (Adx), revealing protein-protein-induced active site structural perturbations. (marquette.edu)
  • NHIP = non-heme iron protein (in the adrenal, adrenodoxin) SOURCE: Omura, T. (43,48). (nih.gov)
  • The name of the enzyme was coined based on its function to reduce a [2Fe-2S] (2 iron, 2 sulfur) electron-transfer protein that was named adrenodoxin. (wikipedia.org)
  • The FAD coenzyme receives two electrons from NADPH and transfers them one at a time to the electron transfer protein adrenodoxin. (wikipedia.org)
  • and Kincaid, James R., "Active Site Structures of CYP11A1 in the Presence of Its Physiological Substrates and Alterations upon Binding of Adrenodoxin" (2017). (marquette.edu)