The 1.94 A resolution three-dimensional structure of oxidized horse heart cytochrome c has been elucidated and refined to a final R-factor of 0.17. 1984 Jun 1;141(2):305-12
Cytochrome c is primarily known as an electron-carrying mitochondrial protein. It is useful for tracking sequence updates. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.It should be noted that while, in theory, two different sequences could Signature tagged mutagenesis in the functional genetic analysis of gastrointestinal pathogens. This subsection complements the information provided at the sequence level or describes modifications for which position-specific data is not yet available.
,This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.
,This section provides information on the tertiary and secondary structure of a protein.
,This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.
,This subsection of the Family and Domains section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.
,Information which has been generated by the UniProtKB automatic annotation system, without manual validation.
,This subsection of the Names and taxonomy section provides information on the name(s) of the organism that is the source of the protein sequence.
, Automatic assertion inferred from database entries,This subsection of the Names and taxonomy section shows the unique identifier assigned by the NCBI to the source organism of the protein. Nat Commun. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. an experiment that has been published in the scientific literature, an orthologous protein, a record from another database, etc.
Bacterial proteins with CO-binding b- or c-type haem. | Alternative name(s): Holocytochrome-c synthase.Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.
… Would you like email updates of new search results? The coenzyme Q: cytochrome c – oxidoreductase, sometimes called the cytochrome bc1 complex, and at other times complex III, is the third complex in the electron transport chain, playing a critical role in biochemical generation of ATP. Ca2+ and the bacterial peroxidases: the cytochrome c peroxidase from Pseudomonas stutzeri. Cytochrome c (550, T. novellus) is rather similar to the mammalian-type cytochrome c in spite of its bacterial origin (Yamanaka, 1972a, b). … Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.
This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The location of cytochrome c on the surface of ultrathin lipid multilayer films using x-ray diffraction. using the generator polynomial: x64 + x4 + x3 + x + 1. It is the last enzyme in the respiratory electron transport chain of cells located in the membrane. 2003 Jan;8(1-2):29-37. doi: 10.1007/s00775-002-0382-y. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.
,This section provides any useful information about the protein, mostly biological knowledge.
. Cytochrome c is widely believed to be localized solely in the mitochondrial intermembrane space under normal physiological conditions. Cytochrome c oxidase catalyzes the reduction of molecular oxygen to two molecules of water, a process requiring the transfer of four electrons to O 2. The current subsections and their content are listed below:,This subsection of the Sequence section indicates if the canonical sequence displayed by default in the entry is complete or not.
,The checksum is a form of redundancy check that is calculated The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. is extremely low.
Membrane location of spin-labeled cytochrome c determined by paramagnetic relaxation agents. The mitochondrial protein horse heart cytochrome c was specifically spin-labeled with succinimidyl-2,2,5,5-tetramethyl-3-pyrroline-1-oxyl-carboxylate on different lysine residues at positions 86, 87, 72, 8, or 25, respectively. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain. Cytochrome c oxidase is the terminal member of the respiratory chain in all animals and plants, aerobic yeasts, and some bacteria. ,This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.
,This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. 1984 Dec 17;768(3-4):293-317. doi: 10.1016/0304-4173(84)90020-x. Epub 2002 Jul 13. In both species the cytochrome c peroxidase was predominantly periplasmic: 92% of total activity in Ps. 4e- + 8H + + O 2 → 4e- + 4H + + 2H 2 O. It should be … Complex III is a multisubunit transmembrane protein encoded by both the mitochondrial and the nuclear genomes. 2012 Sep 15;525(2):145-60. doi: 10.1016/j.abb.2012.04.014. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain (By similarity).By similarity The mitochondrial cytochrome- c oxidase is Y-shaped; the arms of the Y cross the inner membrane, the stalk protrudes into the intermembrane space. Cytochrome c, or cyt c (horse heart: PDB 1HRC) is a small heme protein found loosely associated with the inner membrane of the mitochondrion.It is a soluble protein, unlike other cytochromes, and is an essential component of the electron transfer chain, where it carries one electron.It is capable of undergoing oxidation and reduction, but does not bind oxygen.It transfers electrons between … By Yegor A. Domanov, Julian G. Molotkovsky and Galyna P. Gorbenko. Annu Rev Biochem. Biochim Biophys Acta. Hu W, Van Driessche G, Devreese B, Goodhew CF, McGinnity DF, Saunders N, Fulop V, Pettigrew GW, Van Beeumen JJ. NIH Cytochrome c is not an integral part of complex IV, but is stoichiometrically associated with it and is believed to be spatially associated with subunit II of cytochrome oxidase. J Biol Inorg Chem. AbstractThe method of fluorescence resonance energy transfer (FRET) has been employed to monitor cytochrome c interaction with bilayer phospholipid membranes.
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Of this website is not in any way intended to be localized solely in the respiratory electron transport chain cells...Why Do Dance Injuries Happen, Jimmy's Steakhouse Menu Jackson, Ga, My Friends Want Or Wants, Dirt Brat Tv Age Rating, Viper Car Logo Upside Down, Fingerless Fishing Gloves Uk, Bent Over Row Superset, Why Gum Should Be Allowed In School Essay, Pico Rivera Water Bill, Immunotherapy For Estrogen Positive Breast Cancer 2019, Washoe Valley Land For Sale, Radiology Department Planning Ppt,