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

Bamford, V.A., Berks, B.C. and Hemmings, A.M. ORCID: https://orcid.org/0000-0003-3053-3134 (2002) Novel domain packing in the crystal structure of a thiosulphate-oxidizing enzyme. Biochemical Society Transactions, 30. pp. 638-642. ISSN 1470-8752

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Abstract

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.

Item Type:	Article
Faculty \ School:	Faculty of Science > School of Biological Sciences
UEA Research Groups:	Faculty of Science > Research Groups > Biophysical Chemistry (former - to 2017) Faculty of Science > Research Groups > Molecular Microbiology Faculty of Science > Research Groups > Plant Sciences Faculty of Science > Research Groups > Chemistry of Life Processes Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry
Depositing User:	EPrints Services
Date Deposited:	01 Oct 2010 13:37
Last Modified:	15 Dec 2022 01:38
URI:	https://ueaeprints.uea.ac.uk/id/eprint/511
DOI:	10.1042/BST0300638

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