 | ||
| Mitochondrial cytochrome bc1 complex | ||
| Identifiers | ||
|---|---|---|
| Symbol | Cytochrom_B_N | |
| Pfam | PF00033 | |
| InterPro | IPR005797 | |
| PROSITE | PDOC00171 | |
| SCOP | 3bcc | |
| TCDB | 3.D.3 | |
| OPM family | 3 | |
| OPM protein | 1bcc | |
| Available PDB structures: 1bccC:10-205 2e74A:10-205 1l0lC:9-204 1ntkC:9-204 1ntmC:9-204 1ntzC:9-204 1sqqC:9-204 1l0nC:9-204 1sqxC:9-204 1nu1C:9-204 1sqvC:9-204 1sqbC:9-204 1be3C:9-204 1sqpC:9-204 1kb9C:8-205 1p84C:8-205 1kyoC:8-205 1q90B:9-210 1vf5A:9-210 2d2cN:9-210 | ||
Cytochrome b/b6 is main subunit of transmembrane cytochrome bc1 and b6f complexes. The coenzyme Q: cytochrome c — oxidoreductase, sometimes called the cytochrome bc 1 complex, and at other times complex III Pfam is a large collection of Multiple sequence alignment and Hidden Markov models covering many common protein domains and families InterPro is a database of protein families domains and functional sites in which identifiable features found in known proteins can be applied to new protein sequences PROSITE is a database of Protein families and domains. It consists of entries describing the domains families and functional sites as well as amino acid The Structural Classification of Proteins (SCOP database is a largely manual classification of protein Structural domains based on similarities of their Amino acid Transporter Classification database (or TCDB) is an IUBMB approved classification system for membrane Transport proteins including Ion channels Orientations of Proteins in Membranes (OPM database provides spatial positions of protein three-dimensional structures with respect to the Lipid bilayer. Orientations of Proteins in Membranes (OPM database provides spatial positions of protein three-dimensional structures with respect to the Lipid bilayer. The Protein Data Bank ( PDB) is a repository for 3-D structural data of Proteins and Nucleic acids These data typically obtained by X-ray crystallography The coenzyme Q: cytochrome c — oxidoreductase, sometimes called the cytochrome bc 1 complex, and at other times complex III The cytochrome b 6 f complex (plastoquinol&mdashplastocyanin reductase) of Chloroplasts and Cyanobacteria transfers electrons between the
In the mitochondrion of eukaryotes and in aerobic prokaryotes, cytochrome b is a component of respiratory chain complex III (EC 1.10.2.2) - also known as the bc1 complex or ubiquinol-cytochrome c reductase. An electron transport chain couples a chemical reaction between an electron donor (such as NADH) and an electron acceptor (such as O2) to the transfer This article is about the Enzyme Commission codes For the European Commission system for coding chemicals see EC-No. In plant chloroplasts and cyanobacteria, there is an analogous protein, cytochrome b6, a component of the plastoquinone-plastocyanin reductase (EC 1.10.99.1), also known as the b6f complex. This article is about the Enzyme Commission codes For the European Commission system for coding chemicals see EC-No. These complexes are involved in electron transport and the generation of ATP and thus play a vital role in the cell. Adenosine-5'-triphosphate ( ATP) is a multifunctional Nucleotide that is most important as a " molecular currency" of intracellular Energy
Cytochrome b/b6[1][2] is an integral membrane protein of approximately 400 amino acid residues that probably has 8 transmembrane segments. In plants and cyanobacteria, cytochrome b6 consists of two subunits encoded by the petB and petD genes. Cytochrome b/b6 non-covalently binds two heme groups, known as b562 and b566. A heme ( American English) or haem ( British English) is a Prosthetic group that consists of an Iron atom contained in the center of Four conserved histidine residues are postulated to be the ligands of the iron atoms of these two heme groups. In Chemistry, a ligand is either an Atom, Ion, or Molecule (see also Functional group) that bonds to a central metal generally
References
- ^ Howell N (1989). "Evolutionary conservation of protein regions in the protonmotive cytochrome b and their possible roles in redox catalysis". J. Mol. Evol. 29 (2): 157–169. doi:. A digital object identifier ( DOI) is a permanent identifier given to an Electronic document. PMID 2509716.
- ^ Esposti MD, Crimi M, Ghelli A, Patarnello T, Meyer A, De Vries S (1993). "Mitochondrial cytochrome b: evolution and structure of the protein". Biochim. Biophys. Acta 1143 (3): 243–271. doi:. A digital object identifier ( DOI) is a permanent identifier given to an Electronic document. PMID 8329437.
Human proteins containing this domain
References
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