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Literature summary for 2.8.5.2 extracted from

  • Cheesman, M.; Little, P.; Berks, B.
    Novel heme ligation in a c-type cytochrome involved in thiosulfate oxidation EPR and MCD of SoxAX from Rhodovulum sulfidophilum (2001), Biochemistry, 40, 10562-10569 .
No PubMed abstract available
Search for more literature for 2.8.5.2

Organism

Organism UniProt Comment Textmining
Rhodovulum sulfidophilum Q939U1 AND Q939U4 Q939U1: subunit SoxA, Q939U4: subunit SoxX
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Subunits

Subunits Comment Organism
heterodimer
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 Rhodovulum sulfidophilum

Synonyms

Synonyms Comment Organism
SoxAX complex
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 Rhodovulum sulfidophilum

Cofactor

Cofactor Comment Organism Structure
cytochrome c SoxAX is a naturally occurring c-type cytochrome in which a thiolate-coordinated heme is identified Rhodovulum sulfidophilum
heme analysis of three heme sites. Heme-3 in the ferric state is characterized by a large EPR signal and has histidine and methionine axial heme iron ligands which are retained on reduction to the ferrous state. Heme-1 and heme-2 both have thiolate plus nitrogenous ligand sets in the ferric state and give rise to rhombic EPR spectra. Heme-1, whose ligands derive from cysteinate and histidine residues, remains ferric in the presence of dithionite ion. Ferric heme-2 exists with a preparation-dependent mixture of two different ligand sets, one being cysteinate/histidine, the other an unidentified pair with a weaker crystal-field strength. Upon reduction of the SoxAX complex with dithionite, a change occurs in the ligands of heme-2 in which the thiolate is either protonated or replaced by an unidentified ligand Rhodovulum sulfidophilum

General Information

General Information Comment Organism
metabolism the enzyme plays an essential role in photosynthetic thiosulfate and sulfide oxidation Rhodovulum sulfidophilum