Novel domain packing in the crystal structure of a thiosulphate-oxidizing enzyme

V.A. Bamford, B.C. Berks, A.M. Hemmings

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)


A key component of the oxidative biogeochemical sulphur cycle involves the utilization by bacteria of reduced inorganic sulphur compounds as electron donors to photosynthetic or respiratory electron transport chains. The SoxAX protein of the photosynthetic bacterium Rhodovulum sulfidophilum is a heterodimeric c-type cytochrome that is involved in the oxidation of thiosulphate and sulphide. The recently solved crystal structure of the SoxAX complex represents the first structurally characterized example of a productive electron transfer complex between haemoproteins where both partners adopt the c-type cytochrome fold. The packing of c-type cytochrome domains both within SoxA and at the interface between the subunits of the complex has been compared with other examples and found to be unique.
Original languageEnglish
Pages (from-to)638-642
Number of pages5
JournalBiochemical Society Transactions
Publication statusPublished - 2002

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