Heme electron interaction between cytochrome. Medical search. Frequent questions

corresponding heme arrangements are observed in other multi-heme proteins. (rcsb.org)
The cytochromes are proteins with characteristic strong absorption of visible light, due to their iron-containing heme prosthetic groups. (biochemden.com)
The Cytochromes of type a and b and some of type "C" are integral proteins of the inner mitochondrial membrane. (biochemden.com)
To study the mechanism of this reaction, we have formed the metastable 0 2 adduct of the heme-heme oxygenase complex and observed that its resonance Raman spectrum displays an oxygen isotope shift pattem unlike those of any other 02-bound heme proteins. (datapdf.com)
The team found cytochrome c proteins initially exist in a wide variety of unfolded states. (tunisiesoir.com)
On the formation of bile pigments from heme proteins. (nyu.edu)

The redox partner of microsomal CYPs (including CYP1A1) is NADPH cytochrome P450 oxidoreductase (CPR). (biologists.com)
Herein, molecular dynamics simulations are performed to understand the binding and ET mechanism of the cobalt(II) sepulchrate with the heme domain of cytochrome P450 BM-3. (dechema-dfi.de)
The biosynthetic pathway leading to the potent antioxidant carnosic acid involves several successive oxidation events catalyzed by two cytochrome P450 enzymes (CYPs). (europa.eu)
Monoacetylhydrazine is associated with hepatotoxicity via formation of a reactive intermediate metabolite when N-hydroxylated by the cytochrome P450 mixed oxidase system. (illumina.com)
CW EPR parameters reveal cytochrome P450 ligand binding modes. (washington.edu)
Heme Binding Biguanides Target Cytochrome P450-Dependent Cancer Cell Mitochondria. (washington.edu)
Characterization of ritonavir-mediated inactivation of cytochrome P450 3A4. (washington.edu)
Introduction Heme oxygenase (HO), the first and rate limiting enzyme of the microsomal heme degradation pathway, captures iron protoporphyrin-IX (heme) and converts it into billiverdin-IXa, carbon monoxide, and free iron by using molecular oxygen and electrons donated by cytochrome P450 reductase. (datapdf.com)
Cytochromes P450 monooxygenases represent a large superfamily of heme enzymes, which require a dioxygen molecule and two electrons supplied by a NAD(P)H-dependent protein redox partner to form catalytically active high-valent ferryl-oxo intermediate. (schoolbag.info)
Cytochromes P450 represent a superfamily of heme enzymes with a common fold and mechanism that requires an atmospheric dioxygen molecule, two electrons from NAD(P)H, and one or two protons available from solvent water to form an active catalytic ferryl-oxo intermediate (1). (schoolbag.info)
All cytochromes P450 have one heme b (protoporphyrin IX) buried deeply in the protein globule, with molecular masses in the range 45-60 kDa. (schoolbag.info)
Most reactions performed by cytochromes P450 can be catalyzed effectively by Compound I, which is formally the same high-valent intermediate in all isozymes (5, 6). (schoolbag.info)
Thus, the broad range of metabolized substrates and the unprecedented variability of the chemical reactions catalyzed by cytochromes P450 can be attributed largely to the differences in substrate binding properties of different isozymes. (schoolbag.info)
With respect to their functional roles in living organisms, cytochromes P450 can be separated tentatively into the enzymes essential for biosynthetic pathways and the xenobiotic metabolizing enzymes (1). (schoolbag.info)
The former group includes cytochromes P450 involved into the biosynthesis of steroid hormones, antibiotics, and the transformation of vitamins and cofactors such as retinoids, carotenoids, eicosanoids, and fatty acid derivatives as well as those involved in endogenous intracellular and extracellular signaling. (schoolbag.info)
As a result, some cytochromes P450 from this group are critical for normal life cycle, and deficiencies can lead to serious diseases (7). (schoolbag.info)
In contrast, most cytochromes P450 that belong to the latter group can metabolize a variety of substrates of different sizes through multiple chemical mechanisms and even can form several different products from one substrate. (schoolbag.info)
Despite the unprecedented variability of chemical reactions catalyzed by cytochromes P450, all the important features of their mechanism can be attributed to the oxidative transformations driven by the main catalytic intermediate, which is a ferryl-oxo heme complex with the porphyrin pi-cation radical, or Compound I (3, 4, 8). (schoolbag.info)
Nonclassic reactions catalyzed by some cytochromes P450, which do not use oxygen, and thus deviate from the main P450 mechanism, include direct reductive processes driven by the heme iron (conversion of nitric oxide to nitrous oxide by CYP55, reductive dehalogenation, reduction of azo compounds and quinines, etc. (schoolbag.info)

Cytochrome cd(1) is a respiratory nitrite reductase found in the periplasm of denitrifying bacteria. (ox.ac.uk)
Ubiquinol-cytochrome c reductase pumps protons into the intermembrane space, creating an electrochemical gradient. (yeastgenome.org)
Thus, I aimed to mimic the phospholipid composition of plant ER membrane in yeast and evaluate the activity of the two plant CYPs expressed in this host and their interactions with a suitable reductase (POR). (europa.eu)

Cyt.oxidase thus constitute the last carrier in the chain of electron transport and is referred to as the "terminal oxidase4" of the cytochrome chain. (biochemden.com)
The high potential chain, consisting of the iron sulfur protein, cyt c1 and cyt c2, transfers the first electron from quinol to an acceptor (cytochrome oxidase). (yeastgenome.org)
a) Cytochrome oxidase is a hemoprotein widely distributed in plants and animal tissues. (biologydiscussion.com)
2 at-oms of Cu are also present which are asso-ciated with the cytochrome oxidase ac-tivity. (biologydiscussion.com)
Transcripts binning to the genomes of Fe(III)-reducers Anaeromyxobacter , Geobacter , and Pelosinus indicated significant differences in extracellular electron transport (e.g., multiheme cytochrome c , multicopper oxidase, and type-IV pilin gene expression), adhesion/contact (e.g. (biomedcentral.com)

M.S. Shadrina, G.H. Peslherbe and A.M. English ( 2015 ) O 2 and water migration pathways between the solvent and heme pockets of hemoglobin with open and closed conformations of the distal HisE7 , Biochemistry 54 , 5279-5289. (concordia.ca)
The results were compared to those of cytochrome c electrostatically adsorbed at carboxylic acid terminated SAMs, distinguishing the electron transfer mechanism and electron transfer pathways. (pitt.edu)
However, among the observed binding sites, only few of them provide efficient ET pathways to heme iron. (dechema-dfi.de)
The scientists found that non-functional unfolded forms of the protein cytochrome c follow different pathways and timelines to reach a stable functional folded state. (tunisiesoir.com)

Cyt c554 functions in the latter process by accepting pairs of electrons from HAO and transferring them to a cytochrome acceptor. (rcsb.org)
One such electron acceptor is Fe 2 O 3 , which is commonly found in the clay hematite. (kenyon.edu)
In soils, Fe(III) is typically the most abundant terminal electron acceptor for microbial respiration after O 2 . (biomedcentral.com)
Pulsing of O 2 or a return to O 2 -rich conditions following microbial Fe(III) reduction to Fe(II) promotes the re-precipitation of SRO Fe(III) phases, thereby renewing Fe(III) as an available electron acceptor for microbial respiration should low-O 2 conditions return [ 5 ]. (biomedcentral.com)

Ascorbate-dependent peroxidase activity was first reported in 1979,, more than 150 years after the first observation of peroxidase activity in horseradish plants and almost 40 years after the discovery of the closely related cytochrome c peroxidase enzyme. (wikipedia.org)
This structure provides new rationalization of the unusual functional features of the related cytochrome c peroxidase enzyme, and a mechanism for electron transfer from the substrate to the heme has been prepared (Chapter 3). (le.ac.uk)

Heme peroxidases catalyse the H2O2-dependent oxidation of a wide range of different, usually organic, substrates in biology. (wikipedia.org)
M. Kathiresan and A.M. English ( 2018 ) LC-MS/MS proteoform profiling exposes cytochrome c peroxidase self-oxidation in mitochondria and functionally important hole hopping from its heme , J. Am. Chem. (concordia.ca)
Substrate oxidation-driven electron transfer is coupled to the translocation of protons across the IMM to generate an electrochemical gradient harvested by the ATP synthase (CV) for ATP production. (biorxiv.org)
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. (unl.pt)
It was also shown that the order of oxidation of the hemes is pH independent, but the protein is designed to couple e-/H+ transfer exclusively at physiological pH. (unl.pt)
Quinol oxidation occurs in a bifurcated reaction, in which one electron is transferred to a high potential chain and the other to a low potential chain. (yeastgenome.org)
Photosynthetic water oxidation in cytochrome b559 mutants containing a disrupted heme-binding pocket. (bio.net)

E.A. Orabi and A.M. English ( 2016 ) Sulfur-Aromatic Interactions: Modeling Cysteine and Methionine Binding toTyrosinate and Histidinium Ions to Assess Their Influence on Protein Electron Transfer , Isr. (concordia.ca)
Protein electrophoresis showed that the c -type cytochrome and general protein compositions of P. delaneyi changed when grown on ferrihydrite relative to nitrate. (umass.edu)
The crystal structure of cyt c554 at 2.6 A resolution shows a predominantly alpha-helical protein with four covalently attached hemes. (rcsb.org)
Heterogeneous electron transfer of protein, porphyrins through self-assembled monolayer (SAM) at gold electrodes was studied. (pitt.edu)
The electron transfer mechanism was explored by changing the distance between the electrode and protein, the composition of the SAM chains, the type of cytochrome c (horse heart cytochrome, rat cytochrome c and its mutants), and the conditions of electrolyte solutions. (pitt.edu)
We show that under these conditions carbon monoxide (CO) binds to cyt c, with very high affinity (similar to 5 x 10(7) M(-1)), in contrast to the native cyt c protein involved in respiratory electron shuttling that does not bind CO. Binding of CO to the cyt c-CL complex inhibits its peroxidase activity. (essex.ac.uk)
Our data imply that CL leads to substantial changes in protein conformation and flexibility, allowing access of ligands to the heme. (essex.ac.uk)
Cyt.c of mitochondria, a soluble protein that associates through electrostatic interactions with the outer surface of the inner membrane. (biochemden.com)
Cytochrome a and a 3 possess and identical type of iron - porphyrin complex called "Heme.a",but their location to apo-protein are different. (biochemden.com)
In this work, we have investigated the effect of a physiological electron donor to cytochrome cd(1), the copper protein pseudoazurin, on the mechanism of nitrite reduction by the enzyme. (ox.ac.uk)
In contrast, redox-inert zinc pseudoazurin did not affect cd(1)-X, indicating a crucial role for electron movement between monomers or individual enzyme dimers rather than simply a protein-protein interaction. (ox.ac.uk)
It is clear that cytochrome cd(1) functions significantly differently in the presence of its two substrates, nitrite and electron donor protein, than in the presence of nitrite alone. (ox.ac.uk)
Although imidazole ligand binding to cytochrome c is not directly related to its physiological function, it has the potential to provide valuable information on the molecular and electronic structure of the protein. (rcsb.org)
It represents the chemical composition of hemoglobin, composed of four protein subunits, each containing a heme group with an iron atom in the center. (biochemden.com)
A red-colored conjugated protein (made up of heme and Globin) is present inside the RBC. (biochemden.com)
Ihee's team developed an approach using an X-ray scattering technique to uncover how the protein cytochrome c folds from its initial unfolded state. (tunisiesoir.com)
This protein is composed of a chain of 104 amino acids with an iron-containing heme molecule. (tunisiesoir.com)
Ihee hopes this approach can improve the accuracy of models that simulate protein interactions by including information on their unstructured states. (tunisiesoir.com)

Ascorbate peroxidase (or L-ascorbate peroxidase, APX) (EC 1.11.1.11) is an enzyme that catalyzes the chemical reaction L-ascorbate + H2O2 ⇌ {\displaystyle \rightleftharpoons } dehydroascorbate + 2 H2O It is a member of the family of heme-containing peroxidases. (wikipedia.org)
APX has high sequence identity to cytochrome c peroxidase, which is also a class I peroxidase enzyme. (wikipedia.org)
This suggests that the binding of CaM is responsible for a structural reorganisation of nNOS rd that "unlocks" the conformation of the enzyme and enables the FMN sub-domain motion in order to shuttle an electron from FAD cofactor to the heme. (ndltd.org)
It appears that the "locked" conformation of the enzyme, believed to inhibit the electron transfer to the heme, is specific for the NADP(H). (ndltd.org)
The other heme.a called heme.a 3 is located along with the second copper ion at the binding site for molecular O 2 on subunit-I and functions as aerobic reducing unit of the enzyme complex. (biochemden.com)
When fully reduced Paracoccus pantotrophus cytochrome cd(1) is mixed with nitrite in a stopped-flow apparatus in the absence of excess reductant, a kinetically stable complex of enzyme and product forms, assigned as a mixture of cFe(II) d(1)Fe(II)-NO(+) and cFe(III) d(1)Fe(II)-NO (cd(1)-X). However, in order for the enzyme to achieve steady-state turnover, product (NO) release must occur. (ox.ac.uk)
Our data clearly show that initially oxidized pseudoazurin causes rapid further turnover by the enzyme to give a final product that we assign as all-ferric cytochrome cd(1) with nitrite bound to the d(1) heme (i.e. from which NO had dissociated). (ox.ac.uk)
Abstract: Heme oxygenase is the first and rate limiting enzyme of the microsomal heme degradation pathway. (datapdf.com)
Heme (iron protoporphyrin-IX), a co-factor and substrate of the enzyme, is catabolized through a process in which the key step involves the hydroxylation of the a-meso carbon of the porphyrin macrocycle by heme-bound oxygen. (datapdf.com)
The enzyme, once complexed with its substrate heme, has optical absorption characteristic of myoglobin and hem~globin. (datapdf.com)
In the human body, iron is present in all cells and has several vital functions -- as a carrier of oxygen to the tissues from the lungs in the form of hemoglobin (Hb), as a facilitator of oxygen use and storage in the muscles as myoglobin, as a transport medium for electrons within the cells in the form of cytochromes, and as an integral part of enzyme reactions in various tissues. (cdc.gov)

APX enzymes show high specificity for ascorbate as an electron donor, but most APXs will also oxidise other organic substrates that are more characteristic of the class III peroxidases (such as horseradish peroxidase), in some cases at rates comparable to that of ascorbate itself. (wikipedia.org)
Cytochrome P450s (CYP450s) are part of the superfamily of xenobiotic-metabolising enzymes that have been investigated for their effects on various drugs and toxins. (biologists.com)
The interactions of these molecules with enzymes have not yet been elucidated at the molecular level. (dechema-dfi.de)
Key role in aerobic respiration, in which mitochondrial enzymes accept electrons from electron carriers reduced in glycolysis and the tricarboxylic acid cycle. (yeastgenome.org)
As the bioeconomy era unfolds, yeast emerge as robust cell factories for production of a broad range of products from medicines to small molecules, enzymes and vaccines, components of human breast milk, heme for meat substitutes, bioplastics, biomaterials and even biofuels. (europa.eu)
These heme enzymes are found in most organisms from all biological kingdoms and catalyze various oxidative chemical transformations important for the biosynthesis of steroid hormones, vitamins, signaling molecules, and many other compounds, as well as for the metabolism of xenobiotics. (schoolbag.info)

Dysfunction of the mitochondrial electron transport chain (mETC) is a major cause of human mitochondrial diseases. (biorxiv.org)
OXPHOS depends on the mitochondrial electron transport chain (mETC), which transfers electrons from NADH and succinate to molecular oxygen. (biorxiv.org)

one electron oxidised form of substrate). (wikipedia.org)
The binding interaction of soybean cytosolic APX with its physiological substrate, ascorbate, and with a number of other substrates are also known. (wikipedia.org)
Substrate binding at the distal site of the heme brings the target chemical group into the close proximity of the reactive iron-oxygen catalytic intermediate, often in the regiospecific and stereospecific mode, to provide the selectivity of the chemical transformation. (schoolbag.info)

Current research focuses on the cytochrome bc1 complex which sits in the mitochondrial membrane and uses electron transport to pump protons across the membrane and provide the driving force for ATP synthase. (ua.edu)

M. Kathiresan and A.M. English ( 2017 ) LC-MS/MS reveals that hole hopping in cytochrome c peroxidaseprotects its heme from oxidative modification by excess H 2 O 2 , Chem. (concordia.ca)
P. Ponka, A.D. Sheftel, A.M. English, D.S. Bohle and D. Garcia-Santosa ( 2017 ) Do mammalian cells really need to export and import heme ? (concordia.ca)

The use of such electron acceptors relies on a mechanism that permits electrons to be transferred to the cell exterior. (unl.pt)
A unified theoretical model, i.e. a gradual transition of the mechanism from a friction controlled reaction at short distance to tunneling controlled reaction at long distance, was applied to these ¡°heme-wired¡± systems. (pitt.edu)
Analysis of the spectra suggests that the Fe-0-0 unit is highly bent, showing that steric interactions between the bound 0 2 and the residues of the distal pocket result in a unique mechanism of oxygen activation. (datapdf.com)

Cytochrome bc1 complexes are ubiquinol:cytochrome c oxidoreductases, and as such, they are centrally important components of respiratory and photosynthetic electron transfer chains in many species of bacteria and in mitochondria. (diamond.ac.uk)

H2O [3] In ascorbate peroxidase, Compound I is a transient (green) species and contains a high-valent iron species (known as ferryl heme, FeIV) and a porphyrin pi-cation radical,, as found in horseradish peroxidase. (wikipedia.org)

M. Kathiresan, D.Martins and A.M. English ( 2014 ) Respiration triggers heme transfer from cytochrome c peroxidase to catalase in yeast mitochondria , Proc. (concordia.ca)
Metalloproteins play crucial roles in all living organisms, being involved in catalysis and regulation of a wide array of different reactions, in electron transfer chains associated with respiration and photosynthesis, in signaling events, in O 2 transport, in metal ion trafficking, and in replication of the genetic information. (mdpi.com)
High amounts of reduced manganese in the lake led to the discovery of the Shewanella model species: Shewanella oniedensis MR-1, which transfers electrons to insoluble oxidized manganese as a form of respiration. (kenyon.edu)
Interestingly, oxidized manganese is insoluble, which indicated that the bacteria have a way to transfer electrons to metal outside of their cells for respiration. (kenyon.edu)

Unlike the pendulum, the ion's oscillation is driven by electrostatic interactions with electrons inside the nanotube wall as shown in the figure. (uiuc.edu)
Marti, D. N. & Bosshard, H. R. Electrostatic interactions in leucine zippers: thermodynamic analysis of the contributions of Glu and His residues and the effect of mutating salt bridges. (uzh.ch)
Dürr, E., Jelesarov, I. & Bosshard, H. R. Extremely fast folding of a very stable leucine zipper with a strengthened hydrophobic core and lacking electrostatic interactions between helices. (uzh.ch)

In Cyt.c case the heme group binds tightly by covalently through "Cys" residues. (biochemden.com)

The original microbiota in the raw material (sukumo: composted indigo plant) should be appropriately converged toward the extracellular electron transfer (EET)-occurring microbiota by adjusting environmental factors for indigo reduction. (bvsalud.org)
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. (unl.pt)
These data also suggest that diverse Fe(III)-reducer functions, including cytochrome-dependent extracellular electron transport, are associated with type-III fibronectin domains. (biomedcentral.com)

So one Hb molecule possesses four heme units. (biochemden.com)
Heme pockets of α-subunits are just the adequate size to allow entry of an O 2 molecule. (biochemden.com)
Under some conditions, the cytochrome bc1 complex can be diverted into producing the toxic molecule superoxide. (ua.edu)

A two-electron transfer step between a redox partner and a heme cofactor (HEME) is often the rate-limiting step of the CYP catalytic cycle ( preprint Figure 1 ) [5]. (biologists.com)
The iron serves as a sole redox center in the catalytic cycle, which accepts two electrons sequentially and channels them to coordinated dioxygen to form a (hydro)peroxo-ferric intermediate. (schoolbag.info)

The heme as prosthetic group to this cytochromes, but not covalently in Cyt.a and Cyt.b types. (biochemden.com)
Strong interactions in covalently stacked trimeric porphyrins. (nyu.edu)

Each set of genes for flavin adenine dinucleotide (FAD) transportation to modify the flavin mononucleotide (FMN)-associated family, electron transfer from NADH to the FMN-associated family, and demethylmenaquinone (DMK) synthesis were identified in the genome sequence. (bvsalud.org)

These data help to elucidate the mechanisms by which hyperthermophilic crenarchaea generate energy and transfer electrons across the membrane to iron oxide minerals. (umass.edu)
First, the presence of CPR appeared to weaken peripheral CYP-membrane interactions. (biologists.com)
This is achieved by oxidizing ubiquinol (ubihydroquinone) which reacts from the membrane phase, reducing cytochrome c in the intermembrane space, and using the free energy change to transport H+ ions across the membrane from the matrix to the inter membrane space. (yeastgenome.org)
The low potential chain consists of two cyt b hemes, which serve as a pathway through which electrons are transferred across the coupling membrane. (yeastgenome.org)

Electron Paramagnetic Resonance (EPR) is a branch of spectroscopy that observes the spin of unpaired electrons in free radicals, excited states of molecules, metal ions and magnetic materials. (ua.edu)

may control both electron transfers between the FAD and FMN and from FMN to heme by modulating the potential of the FAD hydroquinone. (ndltd.org)
Because flavoproteins can participate in either one-or-two electron transfers, they can serve as intermediate between reactions in which two electrons are donated and these in which only one electron is accepted. (biochemden.com)

Pseudoazurin dramatically enhances the reaction profile of nitrite reduction by Paracoccus pantotrophus cytochrome cd1 and facilitates release of product nitric oxide. (ox.ac.uk)

Metalloproteins contain one or more permanently bound metal ions, which can be coordinated to the sidechain of specific aminoacids, can be incorporated into metal cofactors (such as heme, other tetrapyrrolic rings, and molybdopterin), or can form inorganic clusters (such as FeS clusters and FeMo cofactor of nitrogenase). (mdpi.com)
The accessibility of the FMN cofactor to the heme was assessed. (ndltd.org)

Compound II contains only the ferryl heme. (wikipedia.org)
Some important exceptions involve the hydroperoxoferric complex, Compound 0, and perhaps the one-electron reduced Cpd I, ferryl oxo heme complex Compound II (1, 3, 4, 9). (schoolbag.info)

Dissimilatory iron reduction by hyperthermophilic archaea occurs in many geothermal environments and generally relies on microbe-mineral interactions that transform various iron oxide minerals. (umass.edu)
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. (unl.pt)
These parameters revealed unique features for PpcA from G. metallireducens compared to other triheme cytochromes from different microorganisms, namely the less negative heme reduction potentials and concomitant functional working potential ranges. (unl.pt)

Cloning, Expression and Physico-Chemical Characterization of a New Di-Heme Cytochrome c from Shewanella baltica OS155. (unimore.it)

a globular catalytic HEME-containing domain, an N-terminal transmembrane (TM) α-helical domain, and a flexible linker region connecting both the HEME-containing and the N-terminal TM domain. (biologists.com)

The electron transfer rate constants of cytochrome c immobilized on a SAM by directly ¡°wiring¡± its heme through a variety of nitrogen ligands (pyridine, imidazole or nitrilE) were measured by cyclic voltammetry. (pitt.edu)

There are five different kinds of electron carriers that participate in the transport of electrons from substrates as they are oxidized in the mitochondria. (biochemden.com)

Shewanella are gram-negative, proteobacteria that are facultative anaerobes and can respire on a tremendous variety of inorganic and organic electron acceptors. (kenyon.edu)
Upon experimentation,they discovered a species of Shewanella that respires by transferring electrons to Mn 4+ . (kenyon.edu)

In the resting state, heme iron is oxidized (Fe 3+ ) and is coordinated with the thiolate sulfur atom of cysteine as the fifth axial ligand with the sixth position vacant or occupied by water. (schoolbag.info)
Model studies on the active site of cytochrome P-450: An iron(II)-porphyrin carrying a strapped thiolate ligand. (nyu.edu)

Results showed that the specificity of NADPH in inducing nNOS rd conformational change relies upon the interaction of both the tightly-bound ADP substituents and the labile nicotinamide substituents and that the tightly bound ADP substituents is essential to position the nicotinamide moieties for full electron transfer repression. (ndltd.org)
Oxygen-Bound Heme-Heme Oxygenase Complex: Evidence for a Highly Bent Structure of the Coordinated Oxygen Satoshi Takahashi? (datapdf.com)

Pseudoazurin catalyzed this effect even when present at only one-tenth the stoichiometry of cytochrome cd(1). (ox.ac.uk)

Our data indicate that OCIAD1 is required for maintenance of normal steady state levels of Complex III and the proteolytic processing of the catalytic subunit cytochrome c 1 (CYC1). (biorxiv.org)

M. Kathiresan and A.M. English ( 2016 ) Targeted proteomics identify metabolism-dependent interactors of yeast cytochrome c peroxidase: Implications in stress response and heme trafficking , Metallomics 8 , 434 -443. (concordia.ca)

Application areas span many topics ranging from electrochemical energy storage, charge and energy transport in correlated materials, light-matter interactions, and how non-covalent interactions influence drug binding, biomolecular structure, and crystal packing. (gatech.edu)
Heme is also the active site of electron transport in cytochromes. (medscape.com)

The separate addition of an exogenous electron shuttle (anthraquinone-2,6-disulfonate), a metal chelator (nitrilotriacetic acid), and 75% spent cell-free supernatant did not stimulate growth with or without the barrier. (umass.edu)
Soluble electron-transfer (ET) mediators like cobalt(II) sepulchrate have been proposed as a cost-effective alternative to shuttle electrons between an inexpensive electron source and an enzyme's redox center. (dechema-dfi.de)

The interaction of mitochondrial cytochrome (cyt) c with cardiolipin (CL) is involved in the initial stages of apoptosis. (essex.ac.uk)

These annotations have been derived from physical molecular interaction evidence extracted from the literature and cross-referenced in the entry, or by curator inference from information on homologs in closely related species or by inference from scientific background. (yeastgenome.org)
f) The terminal cytochrome aa 3 is responsi-ble for the final combination of reducing equivalents with molecular oxygen. (biologydiscussion.com)

Striking structural similarities are evident between the tetra-heme core of cyt c554 and hemes 3-6 of HAO, which suggests an evolutionary relationship between these redox partners. (rcsb.org)
The electron delocalization on the heme moiety and the magnetic susceptibility tensor are consistent with these structural features. (rcsb.org)

Iron is a part of heme, which is the active site of peroxidases that protect cells from oxidative injury by reducing peroxides to water. (medscape.com)

One heme group is located along with one copper ion. (biochemden.com)

A putative 8-heme c -type cytochrome was 60-fold more abundant in iron-grown cells and was unique to the Pyrodictiaceae . (umass.edu)
e) It is a metalloflavoprotein containing non-heme iron and molybdenum. (biologydiscussion.com)
This process provides electrons to cytochrome c, reducing the iron within it from the ferric to the ferrous form, which initiates folding. (tunisiesoir.com)

In a study of photo-induced electron transfer of porphyrins through SAMs with chiral structure, an asymmetrical effect on the efficiency of electron transfer through these chiral chain structures was found. (pitt.edu)
Synthetic porphyrins containing adjacent, redox-active species models of biological electron transfer sites. (nyu.edu)

Both pea APX and soybean APX have been used in electron microscopy studies for cellular imaging. (wikipedia.org)

Cytochrome c peroxidase Manganese peroxidase Kelly GJ, Latzko E (December 1979). (wikipedia.org)

Heme structure does not vary from species to species. (biochemden.com)

Anatomy13

Organisms20

Diseases1

Chemicals and Drugs148

Analytical, Diagnostic and Therapeutic Techniques and Equipment25

Phenomena and Processes43

Disciplines and Occupations2

Information Science4

Health Care1

Proteins6

P45019

Reductase3

Oxidase5

Pathways4

Acceptor4

Related cytochrome c peroxidase enzy2

Oxidation7

Protein18

Enzyme11

Enzymes6

Mitochondrial elect2

Substrate3

Protons1

20172

Mechanism3

Ubiquinol-cytochrome1

Porphyrin pi-cation radical1

Respiration4

Electrostatic interactions3

Group binds1

Extracellular3

Molecule3

Catalytic cycle2

Covalently2

NADH1

Membrane4

Spectroscopy1

Transfers2

Nitric Oxide1

Cofactor2

Ferryl2

Reduction3

Characterization1

Globular1

Ligands1

Substrates1

Shewanella2

Ligand2

Bound2

Stoichiometry1

Complex1

Metabolism1

TRANSPORT2

Shuttle2

Cardiolipin1

Molecular2

Structural2

Oxidative1

Copper1

Iron3

Porphyrins2

Microscopy1

Manganese1

Species1