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 (NO3−) 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.
Skip Nav Destination
Article navigation
February 2005
-
Cover Image
Cover Image
- PDF Icon PDF LinkFront Matter
- PDF Icon PDF LinkTable of Contents
Conference Article|
February 01 2005
Microbial reduction of selenate and nitrate: common themes and variations
C.A. Watts;
C.A. Watts
*Institute for Cell and Molecular Biosciences, University of Newcastle, Newcastle upon Tyne NE2 4HH, U.K.
Search for other works by this author on:
H. Ridley;
H. Ridley
*Institute for Cell and Molecular Biosciences, University of Newcastle, Newcastle upon Tyne NE2 4HH, U.K.
Search for other works by this author on:
E.J. Dridge;
E.J. Dridge
*Institute for Cell and Molecular Biosciences, University of Newcastle, Newcastle upon Tyne NE2 4HH, U.K.
Search for other works by this author on:
J.T. Leaver;
J.T. Leaver
*Institute for Cell and Molecular Biosciences, University of Newcastle, Newcastle upon Tyne NE2 4HH, U.K.
Search for other works by this author on:
A.J. Reilly;
A.J. Reilly
†School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, U.K.
Search for other works by this author on:
D.J. Richardson;
D.J. Richardson
†School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, U.K.
Search for other works by this author on:
C.S. Butler
C.S. Butler
1
*Institute for Cell and Molecular Biosciences, University of Newcastle, Newcastle upon Tyne NE2 4HH, U.K.
1To whom correspondence should be addressed (email c.s.butler@ncl.ac.uk).
Search for other works by this author on:
Publisher: Portland Press Ltd
Received:
August 26 2004
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2005 The Biochemical Society
2005
Biochem Soc Trans (2005) 33 (1): 173–175.
Article history
Received:
August 26 2004
Citation
C.A. Watts, H. Ridley, E.J. Dridge, J.T. Leaver, A.J. Reilly, D.J. Richardson, C.S. Butler; Microbial reduction of selenate and nitrate: common themes and variations. Biochem Soc Trans 1 February 2005; 33 (1): 173–175. doi: https://doi.org/10.1042/BST0330173
Download citation file:
Sign in
Don't already have an account? Register
Sign in to your personal account
You could not be signed in. Please check your email address / username and password and try again.
Captcha Validation Error. Please try again.