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Literature summary 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

Organism

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

EC Number Subunits Comment Organism
2.8.5.2 heterodimer
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 Rhodovulum sulfidophilum

Synonyms

EC Number Synonyms Comment Organism
2.8.5.2 SoxAX complex
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 Rhodovulum sulfidophilum

Cofactor

EC Number Cofactor Comment Organism Structure
2.8.5.2 cytochrome c SoxAX is a naturally occurring c-type cytochrome in which a thiolate-coordinated heme is identified Rhodovulum sulfidophilum
2.8.5.2 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

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