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

Andrew D. Lawrence; Alan Scott; Samantha L. Taylor; Michelle L. Rowe; Christopher M. Johnson; Stephen E. J. Rigby; Michael A. Geeves; Richard W. Pickersgill; Mark J. Howard; Martin J. Warren

doi:10.1042/BSR20140060

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

Journal article

Open access

Peer reviewed

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

Andrew D. Lawrence, Alan Scott, Samantha L. Taylor, Michelle L. Rowe, Christopher M. Johnson, Stephen E. J. Rigby, Michael A. Geeves, Richard W. Pickersgill, Mark J. Howard and Martin J. Warren

Bioscience reports, Vol.34, e00120

2014

DOI: https://doi.org/10.1042/BSR20140060

PMID: 24909839

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Abstract

Biochemistry & Molecular Biology

Cell Biology

Life Sciences & Biomedicine

Science & Technology

Adenosylcobalamin, the coenzyme form of vitamin B-12, 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(l).

Details

Title: FAD binding, cobinamide binding and active site communication in the corm reductase (CobR)
Authors/Creators: Andrew D. Lawrence - Univ Kent, Sch Biosci, Canterbury CT2 7NJ, Kent, England
Alan Scott - Univ Kent, Sch Biosci, Canterbury CT2 7NJ, Kent, England
Samantha L. Taylor - Univ Kent, Sch Biosci, Canterbury CT2 7NJ, Kent, England
Michelle L. Rowe - Univ Kent, Sch Biosci, Canterbury CT2 7NJ, Kent, England
Christopher M. Johnson - MRC, Mol Biol Lab, Cambridge CB2 OQH, England
Stephen E. J. Rigby - Univ Manchester, Manchester Inst Biotechnol, Manchester M1 7DN, Lancs, England
Michael A. Geeves - Univ Kent, Sch Biosci, Canterbury CT2 7NJ, Kent, England
Richard W. Pickersgill - Univ London, Sch Biol & Chem Sci, London E1 4NS, England
Mark J. Howard - Univ Kent, Sch Biosci, Canterbury CT2 7NJ, Kent, England
Martin J. Warren - Univ Kent, Sch Biosci, Canterbury CT2 7NJ, Kent, England
Publication Details: Bioscience reports, Vol.34, e00120
Publisher: Portland Press Ltd
Identifiers: 991005587769107891
Murdoch Affiliation: Centre for Computational and Systems Medicine
Language: English
Resource Type: Journal article

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Collaboration types: Domestic collaboration
Citation topics: 2 Chemistry; 2.276 Metalloenzymes; 2.276.1947 Radical Enzymes
Web Of Science research areas: Biochemistry & Molecular Biology; Cell Biology
ESI research areas: Molecular Biology & Genetics