Pathways & interactions
Class III cytochrome C (IPR020942)
Short name: Cyt_c_III_dom
Overlapping homologous superfamilies
- Multiheme cytochrome superfamily (IPR036280)
- Multihaem cytochrome (IPR011031)
- Class III cytochrome C (IPR020942)
Cytochromes c (cytC) can be defined as electron-transfer proteins having one or several haem c groups, bound to the protein by one or, more generally, two thioether bonds involving sulphydryl groups of cysteine residues. The fifth haem iron ligand is always provided by a histidine residue. CytC possess a wide range of properties and function in a large number of different redox processes [PMID: 9293186].
Ambler [PMID: 1646017] recognised four classes of cytC.
Class III comprises the low redox potential multiple haem cytochromes: cyt C7 (trihaem), C3 (tetrahaem), and high-molecular-weight cytC, HMC (hexadecahaem), with only 30-40 residues per haem group. The haem c groups, all bis-histidinyl coordinated, are structurally and functionally nonequivalent and present different redox potentials in the range 0 to -400 mV [PMID: 7830606]. The 3D structures of a number of cyt C3 proteins have been determined. The proteins consist of 4-5 alpha-helices and 2 beta-strands wrapped around a compact core of four non-parallel haems, which present a relatively high degree of exposure to the solvent. The overall protein architecture, haem plane orientations and iron-iron distances are highly conserved [PMID: 7830606].
- PF02085 (Cytochrom_CIII)