| Type: | Family | Name: | Cytochrome c6 |
| Description: | Cytochrome c (CytC) proteins 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. Ambler [] recognised four classes of cytC.Class I includes the low-spin soluble CytC of mitochondria and bacteria, with the haem-attachment site towards the N terminus, and the sixth ligand provided by a methionine residue about 40 residues further on towards the C terminus. On the basis of sequence similarity, class I CytC were further subdivided into five classes, IA to IE. Class IC, 'split-alpha-band' Cyt C, possess a widened or split alpha-band of lowered absorptivity. This class includes dihaem Cyt C4 and monohaem Cyt C6 (Cyt C-553) and Cyt C-554.The 3D structures of Chlamydomonas reinhardtiiCyt C6 [] and Desulfovibrio vulgarisCyt C-553 [] have been determined. The proteins consist of 4 alpha-helices; three 'core' helices form a 'basket' around the haem group, with one haem edge exposed to the solvent. | Short Name: | Cyt_C6 |
