Cytochrome c: Difference between revisions

<StructureSection load='3cp5' size='450' side='right' scene='Cytochrome_c/Cyt_c/1' caption='Cytochrome c with heme complex with sulfate (PDB code [[3cp5]])'>

The '''cytochrome ''c''''' (cyt ''c'') proteins are a superfamily belonging to the class of [http://en.wikipedia.org/wiki/All-α_proteins all-α proteins], which are denoted as such by having an α-helical core. Each protein in this superfamily also contains one or more covalently-bound [http://en.wikipedia.org/wiki/Heme heme prosthetic groups].<ref>PMID:11697912</ref><ref name=main /> The cyt ''c'' superfamily contains many different families, some of which are better characterized than others. These families include monodomain and multi-domain C-type cytochromes, such as [http://proteopedia.org/wiki/index.php/1etp cyt c4], a diheme C-type cytochrome, and [http://proteopedia.org/wiki/index.php/2ozy NrfB], a pentaheme C-type cytochrome. In particular, the monoheme cyt ''c'' from ''Rhodothermus marinus'' has been previously studied and provides an excellent example of how some protein characteristics and structures can be extremely diverse, yet conserved, through evolution.  For details on decaheme cyt see [[MtrF]].

== Introduction ==

The <scene name='1e08/1e08-cofactors/1'>complex</scene> shows the specific interaction of the hydrogenase (light blue) with the cytochrome (pink), revealing the path of electron transport from the <scene name='1e08/1e08-activecluster/3'>active site metal cluster</scene>, through three iron-sulfur clusters, and ending in the cytochrome heme (colored red). Two <scene name='1e08/1e08-cys/2'>cysteine amino acids at the interface</scene>, CYS 38 in the hydrogenase and CYS10 in the cytochrome, are thought to provide the electron transfer pathway between the two proteins (these scenes were created by Jaime Prilusky, David S. Goodsell, and Eran Hodis).

</StructureSection>

==3D structures of cytochrome C==