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Lookup NU author(s): Dr Carys WattsORCiD, Elizabeth Dridge, James Leaver, Dr Clive Butler
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A number of biochemically distinct systems have been characterized for the microbial reduction of the oxyanions, selenate (SeO42-) and nitrate (NO3-). Two classes of molybdenum-dependent nitrate reductase catalyse the respiratory-linked reduction of nitrate (NO 3-) to nitrite (NO2-). The main respiratory nitrate reductase (NAR) is membrane-anchored, with its active site facing the cytoplasmic compartment. The other enzyme (NAP) is water-soluble and located in the periplasm. In recent years, our understanding of each of these enzyme systems has increased significantly. The crystal structures of both NAR and NAP have now been solved and they provide new insight into the structure, function and evolution of these respiratory complexes. In contrast, our understanding of microbial selenate (SeO42-) reduction and respiration is at an early stage; however, similarities to the nitrate reductase systems are emerging. This review will consider some of the common themes and variations between the different classes of nitrate and selenate reductases. © 2005 Biochemical Society.
Author(s): Watts CA, Ridley H, Dridge EJ, Leaver JT, Reilly AJ, Richardson DJ, Butler CS
Publication type: Conference Proceedings (inc. Abstract)
Publication status: Published
Conference Name: 10th Nitrogen Cycle Meeting
Year of Conference: 2004
Pages: 173-175
ISSN: 0300-5127
Publisher: Biochemical Society Transactions: Portland Press Ltd.
URL: http://dx.doi.org/10.1042/BST0330173
DOI: 10.1042/BST0330173
PubMed id: 15667298
