FAD binding, cobinamide binding and active site communication in the corrin reductase (CobR)

Lawrence, Andrew D. and Taylor, Samantha L and Scott, Alan and Rowe, Michelle L. and Johnson, Christopher M and Rigby, Stephen E J and Geeves, Michael A. and Pickersgill, Richard W and Howard, Mark J. and Warren, Martin J. (2014) FAD binding, cobinamide binding and active site communication in the corrin reductase (CobR). Bioscience Reports, 34 (4). pp. 345-355. ISSN 0144-8463. E-ISSN 1573-4935. (doi:https://doi.org/10.1042/BSR20140060) (Full text available)

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Abstract

Adenosylcobalamin, the coenzyme form of vitamin B12, is one Nature's most complex coenzyme whose de novo biogenesis proceeds along either an anaerobic or aerobic metabolic pathway. The aerobic synthesis involves reduction of the centrally chelated cobalt metal ion of the corrin ring from Co(II) to Co(I) before adenosylation can take place. A corrin reductase (CobR) enzyme has been identified as the likely agent to catalyse this reduction of the metal ion. Herein, we reveal how Brucella melitensis CobR binds its coenzyme FAD (flavin dinucleotide) and we also show that the enzyme can bind a corrin substrate consistent with its role in reduction of the cobalt of the corrin ring. Stopped-flow kinetics and EPR reveal a mechanistic asymmetry in CobR dimer that provides a potential link between the two electron reduction by NADH to the single electron reduction of Co(II) to Co(I).

Item Type: Article
Subjects: Q Science
Q Science > QH Natural history > QH301 Biology
Divisions: Faculties > Sciences > School of Biosciences
Faculties > Sciences > School of Biosciences > Protein Science Group
Depositing User: M.J. Howard
Date Deposited: 06 Nov 2014 17:19 UTC
Last Modified: 19 Jan 2015 12:01 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/44133 (The current URI for this page, for reference purposes)
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