Proteins that contain an iron-porphyrin, or heme, prosthetic group resembling that of hemoglobin. (From Lehninger, Principles of Biochemistry, 1982, p480)
A conjugated protein which is the oxygen-transporting pigment of muscle. It is made up of one globin polypeptide chain and one heme group.
The color-furnishing portion of hemoglobin. It is found free in tissues and as the prosthetic group in many hemeproteins.
The rate dynamics in chemical or physical systems.

Anoxic function for the Escherichia coli flavohaemoglobin (Hmp): reversible binding of nitric oxide and reduction to nitrous oxide. (1/1062)

The flavohaemoglobin Hmp of Escherichia coli is inducible by nitric oxide (NO) and provides protection both aerobically and anaerobically from inhibition of growth by NO and agents that cause nitrosative stress. Here we report rapid kinetic studies of NO binding to Fe(III) Hmp with a second order rate constant of 7.5 x 10(5) M(-1) s(-1) to generate a nitrosyl adduct that was stable anoxically but decayed in the presence of air to reform the Fe(III) protein. NO displaced CO bound to dithionite-reduced Hmp but, remarkably, CO recombined after only 2 s at room temperature indicative of NO reduction and dissociation from the haem. Addition of NO to anoxic NADH-reduced Hmp also generated a nitrosyl species which persisted while NADH was oxidised. These results are consistent with direct demonstration by membrane-inlet mass spectrometry of NO consumption and nitrous oxide production during anoxic incubation of NADH-reduced Hmp. The results demonstrate a new mechanism by which Hmp may eliminate NO under anoxic growth conditions.  (+info)

Five-coordinate iron-porphyrin as a model for the active site of hemoproteins. Characterization and coordination properties. (2/1062)

Preparation of iron(III)-deuteroporphyrin 6(7)-methyl ester, 7(6)-(histidine methyl ester) by coupling histidine methyl ester to deuterohemin has been performed using the mixed carboxylic/carbonic-acid-anhydride method. This compound, which is very soluble in various organic solvents, can be considered as a prosthetic group model for the active site of five-coordinate hemoproteins. In the oxidized state a basic, a neutral or an acid form can be isolated. The basic and acid forms are monomeric at all concentrations. The neutral form is found dimeric in concentrated solutions while it is monomeric at low concentration. The coordination state of iron in these various species is investigated. The neutral form reacts with ligands, such as nitrogenous organic bases, leading to six-coordinate well-known hemichromes which exhibit low-spin electron spin resonance (ESR) spectra. The reaction of anionic ligands, such as F-, CN-, NO-2 and N-3, with the neutral form model leads to unsymmetrical six-coordinate complexes whose optical and ESR spectra are similar to those of synthetic deuteromyoglobin. In benzene, toluene or dichloromethane solutions iron (II)-deuteroporphyrin 6(7)-methyl ester, 7(6)-histidine methyl ester), obtained from ferric forms by heterogeneous reduction with aqueous dithionite, exhibits an optical spectrum characteristic of a five-coordinate high-spin ferrous complex. At low temperature important spectral modifications are observed indicating a dimeric association. At room temperature it binds one nitrogenous base molecule leading to the well-known hemochrome. It reacts also with carbon monoxide with a very high affinity constant (4.5 X 10(8) M-1), comparable to that of the isolated human hemoglobin alpha and beta chains, but much higher than the values reported for other various models, suggesting that the side-chain length bearing the fifth ligand may have an important influence upon the reactivity of the sixth position of the iron ion. At low temperature in toluene or dichloromethane, this compound reversibly binds oxygen without oxidation of the iron ion while oxidation occurs at room temperature. The significance of these results is discussed in relation with the local environment, the electronic nature of the base and the immobilization of the heme group in hemoproteins.  (+info)

An anomaly in the resonance Raman spectra of cytochrome P-450cam in the ferrous high-spin state. (3/1062)

Resonance Raman spectra of cytochrome P-450cam (P-450cam) and its enzymatically inactive form (P-420) in various oxidation and spin states were measured for the first time. The Raman spectrum of reduced P-450cam was unusual in the sense that the "oxidation-state marker" appeared at an unexpectedly lower frequency (1346 cm-1) in comparison with those of other reduced hemoproteins (approximately 1355-approximately 1365 cm-1), whereas that of oxidized P-450cam was located at a normal frequency. This anomaly in the Raman spectrum of reduced P-450cam can be explained by assuming electron delocalization from the fifth ligand, presumably a thiolate anion, to the antibonding pi orbital of the porphyrin ring. The corresponding Raman line of reduced P-420 appeared at a normal frequency (1360 cm-1), suggesting a status change or replacement of the fifth ligand upon conversion from P-450cam to P-420. The Raman spectrum of reduced P-450cam-metyrapone complex was very similar to that of ferrous cytochrome b5.  (+info)

Structure and function of a cysBJIH gene cluster in the purple sulphur bacterium Thiocapsa roseopersicina. (4/1062)

A gene cluster containing homologues of the genes cysB, cysJI and cysH was found in the genome of the sulphur-oxidizing purple bacterium Thiocapsa roseopersicina. The nucleotide sequence indicated four open reading frames encoding homologues of 3'-phosphoadenylylsulphate (PAPS) reductase (CysH), sulphite reductase flavoprotein (CysJ) and haem protein (CysI) subunits, and a transcriptional regulator (CysB). Genes cysJIH are separated by a short cis-active intergenic region from cysB which is transcribed divergently. cysB encodes a polypeptide of 35.9 kDa consisting of 323 amino acid residues with 40% identity to the CysB regulator from enterobacteria. cysH encodes a protein with 239 amino acid residues and a calculated mass of 27.7 kDa; cysJ encodes a protein with 522 amino acid residues and a mass of 57.8 kDa; and cysI encodes a protein with 559 amino acid residues and a mass of 62.3 kDa. The cysJIH gene products have been expressed and used for complementation of cys mutants from Escherichia coli Biochemical analysis. The gene product CysH is a thioredoxin-dependent PAPS reductase (EC 1.8.99.4). It was repressed under photoautotrophic growth using hydrogen sulphide as electron donor and derepressed under conditions of sulphate deficiency. Products of the cysJI genes were identified as the two subunits of NADPH-sulphite reductase (EC 1.8.1.2). cysJ encoded the flavoprotein, with > or = 39% identity to the protein from E. coli, and cysI encoded the haem protein, with > or = 53% identity. A cysI clone was used to complement the corresponding mutant from E. coli and to express enzymically active methylviologen-sulphite reductase.  (+info)

Oxygen sensing in yeast: evidence for the involvement of the respiratory chain in regulating the transcription of a subset of hypoxic genes. (5/1062)

Oxygen availability affects the transcription of a number of genes in nearly all organisms. Although the molecular mechanisms for sensing oxygen are not precisely known, heme is thought to play a pivotal role. Here, we address the possibility that oxygen sensing in yeast, as in mammals, involves a redox-sensitive hemoprotein. We have found that carbon monoxide (CO) completely blocks the anoxia-induced expression of two hypoxic genes, OLE1 and CYC7, partially blocks the induction of a third gene, COX5b, and has no effect on the expression of other hypoxic or aerobic genes. In addition, transition metals (Co and Ni) induce the expression of OLE1 and CYC7 in a concentration-dependent manner under aerobic conditions. These findings suggest that the redox state of an oxygen-binding hemoprotein is involved in controlling the expression of at least two hypoxic yeast genes. By using mutants deficient in each of the two major yeast CO-binding hemoproteins (cytochrome c oxidase and flavohemoglobin), respiratory inhibitors, and cob1 and rho0 mutants, we have found that the respiratory chain is involved in the anoxic induction of these two genes and that cytochrome c oxidase is likely the hemoprotein "sensor." Our findings also indicate that there are at least two classes of hypoxic genes in yeast (CO sensitive and CO insensitive) and imply that multiple pathways/mechanisms are involved in modulating the expression of hypoxic yeast genes.  (+info)

Non-enzymatic nitric oxide synthesis in biological systems. (6/1062)

Nitric oxide (NO) is an important regulator of a variety of biological functions, and also has a role in the pathogenesis of cellular injury. It had been generally accepted that NO is solely generated in biological tissues by specific nitric oxide synthases (NOS) which metabolize arginine to citrulline with the formation of NO. However, NO can also be generated in tissues by either direct disproportionation or reduction of nitrite to NO under the acidic and highly reduced conditions which occur in disease states, such as ischemia. This NO formation is not blocked by NOS inhibitors and with long periods of ischemia progressing to necrosis, this mechanism of NO formation predominates. In postischemic tissues, NOS-independent NO generation has been observed to result in cellular injury with a loss of organ function. The kinetics and magnitude of nitrite disproportionation have been recently characterized and the corresponding rate law of NO formation derived. It was observed that the generation and accumulation of NO from typical nitrite concentrations found in biological tissues increases 100-fold when the pH falls from 7.4 to 5.5. It was also observed that ischemic cardiac tissue contains reducing equivalents which reduce nitrite to NO, further increasing the rate of NO formation more than 40-fold. Under these conditions, the magnitude of enzyme-independent NO generation exceeds that which can be generated by tissue concentrations of NOS. The existence of this enzyme-independent mechanism of NO formation has important implications in our understanding of the pathogenesis and treatment of tissue injury.  (+info)

Nitric oxide and iron proteins. (7/1062)

Nitric oxide interactions with iron are the most important biological reactions in which NO participates. Reversible binding to ferrous haem iron is responsible for the observed activation of guanylate cyclase and inhibition of cytochrome oxidase. Unlike carbon monoxide or oxygen, NO can also bind reversibly to ferric iron. The latter reaction is responsible for the inhibition of catalase by NO. NO reacts with the oxygen adduct of ferrous haem proteins (e.g. oxyhaemoglobin) to generate nitrate and ferric haem; this reaction is responsible for the majority of NO metabolism in the vasculature. NO can also interact with iron-sulphur enzymes (e.g. aconitase, NADH dehydrogenase). This review describes the underlying kinetics, thermodynamics, mechanisms and biological role of the interactions of NO with iron species (protein and non-protein bound). The possible significance of iron reactions with reactive NO metabolites, in particular peroxynitrite and nitroxyl anion, is also discussed.  (+info)

Phospholipid bound to the flavohemoprotein from Alcaligenes eutrophus. (8/1062)

The structurally characterized flavohemoprotein from Alcaligenes eutrophus (FHP) contains a phospholipid-binding site with 1-16 : 0-2-cyclo-17 : 0-diacyl-glycerophospho-ethanolamine and 1-16 : 0-2-cyclo-17 : 0-diacyl-glycerophospho-glycerol as the major occupying compounds. The structure of the phospholipid is characterized by its compact form, due to the -sc/beta/-sc conformation of the glycerol and the nonlinear arrangement of the sn-1- and sn-2-fatty acid chains. The phospholipid-binding site is located adjacent to the heme molecule at the bottom of a large cavity. The fatty acid chains form a large number of van der Waal's contacts with nonpolar side chains, whereas the glycerophosphate moiety, which points towards the entrance of the channel, is linked to the protein matrix by polar interactions. The thermodynamically stable globin module of FHP, obtained after cleaving off the oxidoreductase module, also contains the phospholipid and can therefore be considered as a phospholipid-binding protein. Single amino acid exchanges designed to decrease the lipid-binding site revealed both the possibility of blocking incorporation of the phospholipid and its capability to evade steric barriers. Conformational changes in the phospholipid can also be induced by binding heme-ligating compounds. Phospholipid binding is not a general feature of flavohemoproteins, because the Escherichia coli and the yeast protein exhibit less and no lipid affinity, respectively.  (+info)

Heme proteins are a type of protein that contain a heme group, which is a prosthetic group composed of an iron atom contained in the center of a large organic ring called a porphyrin. The heme group gives these proteins their characteristic red color. Hemeproteins have various important functions in biological systems, including oxygen transport (e.g., hemoglobin), electron transfer (e.g., cytochromes), and enzymatic catalysis (e.g., peroxidases and catalases). The heme group can bind and release gases, such as oxygen and carbon monoxide, and can participate in redox reactions due to the ease with which iron can change its oxidation state.

Myoglobin is a protein found in the muscle tissue, particularly in red or skeletal muscles. It belongs to the globin family and has a similar structure to hemoglobin, another oxygen-binding protein found in red blood cells. Myoglobin's primary function is to store oxygen within the muscle cells, making it readily available for use during periods of increased oxygen demand, such as during physical exertion.

Myoglobin contains heme groups that bind to and release oxygen molecules. The protein has a higher affinity for oxygen than hemoglobin, allowing it to maintain its bound oxygen even in low-oxygen environments. When muscle cells are damaged or undergo necrosis (cell death), myoglobin is released into the bloodstream and can be detected in serum or urine samples. Elevated levels of myoglobin in the blood or urine may indicate muscle injury, trauma, or diseases affecting muscle integrity, such as rhabdomyolysis or muscular dystrophies.

Heme is not a medical term per se, but it is a term used in the field of medicine and biology. Heme is a prosthetic group found in hemoproteins, which are proteins that contain a heme iron complex. This complex plays a crucial role in various biological processes, including oxygen transport (in hemoglobin), electron transfer (in cytochromes), and chemical catalysis (in peroxidases and catalases).

The heme group consists of an organic component called a porphyrin ring, which binds to a central iron atom. The iron atom can bind or release electrons, making it essential for redox reactions in the body. Heme is also vital for the formation of hemoglobin and myoglobin, proteins responsible for oxygen transport and storage in the blood and muscles, respectively.

In summary, heme is a complex organic-inorganic structure that plays a critical role in several biological processes, particularly in electron transfer and oxygen transport.

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.

Eisenstein, Laura (1976). "Molecular tunneling in heme proteins". International Journal of Quantum Chemistry. 10 (S3): 21-27. ... "Dynamics of carbon monoxide binding by heme proteins". Science. 181 (4099): 541-543. Bibcode:1973Sci...181..541A. doi:10.1126/ ... "Tunneling in ligand binding to heme proteins". Science. 192 (4243): 1002-1004. Bibcode:1976Sci...192.1002A. doi:10.1126/science ...
e.g. hemeproteins, flavoproteins,Cu/Zn proteins, etc.). Occasionally, some proteins that lack the above cofactors but have high ...
Basak, Pijush; Pattanayak, Rudradip; Bhattacharyya, Maitree (2015). "Transition Metal Induced Conformational Change of Heme Proteins ... function and interactions with special interest to hemeproteins, biomolecular interaction. Bhattacharyya's most cited ...
Hemeproteins have diverse biological functions including oxygen transport, which is completed via hemeproteins including ... Being hemeproteins, they both contain a heme prosthetic group. His-F8 of the myoglobin, also known as the proximal histidine, ... Hemeproteins also enable electron transfer as they form part of the electron transport chain. Cytochrome a, cytochrome b, and ... Hemeproteins probably evolved to incorporate the iron atom contained within the protoporphyrin IX ring of heme into proteins. ...
Huang X, Groves JT (March 2018). "Oxygen Activation and Radical Transformations in Heme Proteins and Metalloporphyrins". ...
Sampath V, Zhao XJ, Caughey WS (Apr 27, 2001). "Anesthetic-like interactions of nitric oxide with albumin and hemeproteins. A ...
One diverse set of examples is the heme proteins, which consist of a porphyrin ring coordinated to iron. Iron-sulfur clusters ... Li T, Bonkovsky HL, Guo JT (March 2011). "Structural analysis of heme proteins: implications for design and prediction". BMC ...
This class of compounds includes the heme proteins hemoglobin and myoglobin. An exotic and unusual reaction occurs with PtF 6, ...
... ppm of carbon monoxide from degradation of heme proteins.[clarification needed] 1 ppm of ammonia. Trace many hundreds of ...
"Nature of O2 and CO binding to metalloporphyrins and heme proteins". Proceedings of the National Academy of Sciences of the ...
Histidine is a common ligand for many hemeproteins including hemoglobin and myoglobin. Heme A in the cytochrome a portion of ...
... geminate recombination has first been studied in the solution phase using iodine molecules and heme proteins. In the solid ... "A comparison of the geminate recombination kinetics of several monomeric heme proteins". Journal of Biological Chemistry. 263 ( ...
Cytochromes are hemeproteins involved in the generation of ATP via electron transport. S. violacea contains three main types of ...
"The Smallest Biomolecules: Diatomics and their Interactions with Heme Proteins - 1st Edition". www.elsevier.com. Retrieved 3 ... in the course of which he derived significant new insight into the problem diatomic ligand discrimination by heme proteins. ... Diatomics and their Interactions with Heme Proteins (Elsevier, 2008), a monograph on the subject, and Letters to a Young ...
Hemoglobin, erythrocruorin, and chlorocruorin are all globins, iron-heme proteins with a common core. Their color comes from ...
The binding of O2 by reduced (Fe2+) heme proteins involves formation of Fe(III) superoxide complex. The assay of superoxide ...
The compound is used in the preparation of models for the prosthetic group in heme proteins. It is a dark purple solid that is ...
Gibson started his career with studies of hemoglobin, and continued with much other work on heme proteins. In keeping with his ...
"Mössbauer Quadrupole Splittings and Electronic Structure in Heme Proteins and Model Systems: A Density Functional Theory ...
After transferring to the bone marrow cells, iron forms a complex with heme proteins for hemoglobin synthesis. Different dosage ...
This method has been used to examine gas binding in hemeproteins and the catalytic cycle of various enzymes. Using ultraviolet ...
Nitrite reacts with heme proteins and metal ions, neutralizing free radicals by nitric oxide (one of its byproducts). ...
There, he continued his research on heme proteins, studying ligand migration within these proteins and its effects on the ... mainly on heme proteins. Since 1997, he has been appointed as an adjunct professor. In 1996, he accepted an offer to become ...
... studies of low-spin ferriheme centers and their corresponding heme proteins". Coordination Chemistry Reviews. 185-186: 471-534 ...
Typical cases involve the nitrosylation of heme proteins like cytochromes, thereby disabling the normal enzymatic activity of ...
Computer simulation of heme proteins of physiopathological relevance. Gustavo Henrique Goldman, Professor of Molecular Biology ...
... or have receptors that bind directly to iron/heme proteins. In eukaryotes, other strategies to enhance iron solubility and ...
She received her Ph.D. in Medical Sciences with a focus on the ultrafast vibrational dynamics of heme proteins in 1994. ... The focus of the remainder of her PhD research was the ultrafast vibrational dynamics of heme proteins, the oxygen-carrying ...
Nanosecond transient circular dichroism and birefringence measurements with applications to the photolysis of heme proteins (Ph ...
In the case of ferric heme proteins, MCD is capable of determining both oxidation and spin state to a remarkably exquisite ...
Hemeproteins. Below are the last 250 changes in the last 30 days, as of 10:41, 2 October 2023. Show last 50 , 100 , 250 , 500 ...
The dispute centers on the use of meaty-tasting heme proteins in plant-based meat alternatives, an area in which both companies ... In a lawsuit filed in March 2022, Impossible accused Motif of infringing its 761 patent, which covers the application of heme proteins ... Motif FoodWorks suffers setback in IP row with Impossible Foods over heme proteins, but remains confident in our legal ... Motif FoodWorks has suffered a setback in its dispute with Impossible Foods over meaty-tasting heme proteins in meat ...
The objective of this proposal is to elucidate the protein-ligand interactions and structure/function relationships in three new bacterial hemoglobins (Hb) and two mammalian prostaglandin H synthases (PGHS-1 and PGHS-2). The two bacterial hemoglobins from Mycobacterium tuberculosis (HbN and HbO) belong to a newly discovered truncated hemoglobin family, which are characterized by a novel two-over-two alpha-helical sandwich motif, the absence of the A- helix and the presence of an extended loop substituting for most of the F-helix. The physiological functions of HbN and HbO are not established but because O2 delivery in unicellular organisms is a diffusion-controlled process, functions other than oxygen transport have been put forth. The bacterial hemoglobin from E. coli (Hmp) is a flavohemoglobin consisting of a heme-containing globin-like domain and a FAD-containing reductase domain. It is believed that the function of Hmp is to detoxify NO and other reactive nitrogen species. The structural ...
Fast reactions in carbon monoxide binding to heme proteins. / Alberding, N.; Austin, R. H.; Chan, S. S. et al. In: Biophysical ... Fast reactions in carbon monoxide binding to heme proteins. N. Alberding, R. H. Austin, S. S. Chan, L. Eisenstein, H. ... Fast reactions in carbon monoxide binding to heme proteins. In: Biophysical Journal. 1978 ; Vol. 24, No. 1. pp. 319-334. ... Fast reactions in carbon monoxide binding to heme proteins. Biophysical Journal. 1978;24(1):319-334. doi: 10.1016/S0006-3495(78 ...
... are compared and analyzed in an attempt to understand the structural basis for ligand specificity in hemeproteins. Pulsed and ... Evidence for Proximal Control of Ligand Specificity in Hemeproteins: Absorption and Raman Studies of Cryogenically Trapped ... Evidence for proximal control of ligand specificity in hemeproteins: Absorption and Raman studies of cryogenically trapped ... are compared and analyzed in an attempt to understand the structural basis for ligand specificity in hemeproteins. Pulsed and ...
... Title (en). ... Pharmaceutical composition containing S-nitroso-heme proteins and use thereof. Title (de). Pharmazeutische Zusammensetzung ...
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The Geobacter metallireducens bacterium can couple the oxidation of a wide range of compounds to the reduction of several extracellular electron acceptors, including pollutants or electrode surfaces for current production in microbial fuel cells. For these reasons, G. metallireducens are of interest for practical biotechnological applications. The use of such electron acceptors relies on a mechanism that permits electrons to be transferred to the cell exterior. The cytochrome PpcA from G. metallireducens is a member of a family composed by five periplasmic triheme cytochromes, which are important to bridge the electron transfer from the cytoplasmic donors to the extracellular acceptors. Using NMR and visible spectroscopic techniques, a detailed thermodynamic characterization of PpcA was obtained, including the determination of the heme reduction potentials and their redox and redox-Bohr interactions. These parameters revealed unique features for PpcA from G. metallireducens compared to other ...
Eisenstein, Laura (1976). "Molecular tunneling in heme proteins". International Journal of Quantum Chemistry. 10 (S3): 21-27. ... "Dynamics of carbon monoxide binding by heme proteins". Science. 181 (4099): 541-543. Bibcode:1973Sci...181..541A. doi:10.1126/ ... "Tunneling in ligand binding to heme proteins". Science. 192 (4243): 1002-1004. Bibcode:1976Sci...192.1002A. doi:10.1126/science ...
Hemeproteins / antagonists & inhibitors* * Hydrogen-Ion Concentration * Hydrophobic and Hydrophilic Interactions * Inhibitory ...
Gene Ontology Analysis Identifies Iron and Heme Proteins Linked to HDL. Previously, HDL-associated proteins have been linked to ...
Balla, J, Jacob, HS, Balla, G, Nath, K & Vercellotti, GM 1992, Endothelial cell heme oxygenase and ferritin induction by heme proteins ... Endothelial cell heme oxygenase and ferritin induction by heme proteins: a possible mechanism limiting shock damage. ... Endothelial cell heme oxygenase and ferritin induction by heme proteins : a possible mechanism limiting shock damage. In: ... Endothelial cell heme oxygenase and ferritin induction by heme proteins: a possible mechanism limiting shock damage. / Balla, J ...
The thermodynamic model of five interacting charge centres (four haems and an ionisable centre), which was used in the characterisation of the thermodynamic properties of Desulfovibrio vulgaris (Hildenborough) cytochrome c3 (c3DvH), is now used to reevaluate the thermodynamic properties in Desulfovibrio vulgaris (Miyazaki F) cytochrome c3 (c3DvM) on the basis of published data (Park, J.-S., Ohmura, T., Kano, K., Sagara, T., Niki, K., Kyogoku, Y. and Akutsu, H. (1996) Biochim. Biophys. Acta 1293, 45-54). Contrary to the assertion of Park et al. (1996), the pH dependence of the proton chemical shifts of haem methyls in c3DvM in several stages of oxidation is well described by the model, which involves both homotropic (e-/e-) and heterotropic (e-/H+) cooperativity. This shows that the pH dependence observed for c3DvM is not significantly more complicated than that observed for c3DvH. Since the parameters which we now obtain for c3DvM are generated with the same model as those from c3DvH, albeit ...
Reports from National University Describe Recent Advances in Hemeproteins [Systematic Revision of Thomasomys Cinereus (Rodentia ... Reports from National University Describe Recent Advances in Hemeproteins [Systematic Revision of Thomasomys Cinereus (Rodentia ...
Arcovito A, Della Longa S. Local structure and dynamics of hemeproteins by X-ray absorption near edge structure spectroscopy. ... Arcovito, A., & Della Longa, S. (2012). Local structure and dynamics of hemeproteins by X-ray absorption near edge structure ... Local structure and dynamics of hemeproteins by X-ray absorption near edge structure spectroscopy. In: Journal of Inorganic ... Arcovito, A & Della Longa, S 2012, Local structure and dynamics of hemeproteins by X-ray absorption near edge structure ...
Heme reconstitution with porphyrin analogs is a powerful approach toward understanding the molecular function of heme proteins ...
... corresponding heme arrangements are observed in other multi-heme proteins. Striking structural similarities are evident between ...
Categories: Hemeproteins Image Types: Photo, Illustrations, Video, Color, Black&White, PublicDomain, CopyrightRestricted 22 ...
These heme-proteins may enhance vasoconstriction through interactions with nitric oxide (NO) and endothelin receptors. The ...
Time-resolved surface-enhanced resonance Raman spectro-electrochemistry of heme proteins. Spectroscopy-an International Journal ...
Time-resolved surface-enhanced resonance Raman spectro-electrochemistry of heme proteins. Spectroscopy-an International Journal ...
On the formation of bile pigments from heme proteins.. Heterocycles 1977, 7(2), 817-829.. DOI: 10.3987/S-1977-02-0817 ...
Heme proteins such as myoglobin or hemoglobin, when released into the extracellular space, can instigate tissue toxicity. ... In the glycerol model of this syndrome, we demonstrate that the kidney responds to such inordinate amounts of heme proteins by ...
Kachalova, G.S. et al., A steric mechanism for inhibition of CO binding to heme proteins. Science (1999) Release Date. 1999-05- ...
"Nature of Oxygen and Carbon Monoxide Binding to Metalloporphyrins and Heme Proteins". Proceedings of the National Academy of ...
Hemeproteins [D12.776.422]. *Cytochromes [D12.776.422.220]. *Cytochrome P-450 Enzyme System [D12.776.422.220.453] ...
Evaluation of different methods to calculated reduction potentials for heme proteins. Automated methods to determine hydrogen ...
Biological applications: Substrate free radical, flavins and metal free flavin proteins, photosynthesis, Heme proteins, Iron- ...
Francis R. T. Jr, Becker B. B. 1984; Specific indication of hemeproteins in polyacrylamide gels using a double-staining process ...
  • Therefore, porphyrins and hemeproteins are among the materials that have spin-filtering property to be applied in spintronics. (intechopen.com)
  • The catalytic properties of porphyrins and related compounds such as the hemeproteins are also applicable in the fabrication of micro-/nanomotors (MNMs). (intechopen.com)
  • Local structure and dynamics of hemeproteins by X-ray absorption near edge structure spectroscopy. (unicatt.it)