Functional, biochemical and genetic diversity of prokaryotic nitrate reductases

Richardson, D. J. ORCID: https://orcid.org/0000-0002-6847-1832, Berks, B. C., Russell, D. A., Spiro, S. and Taylor, C. J. (2001) Functional, biochemical and genetic diversity of prokaryotic nitrate reductases. Cellular and Molecular Life Sciences, 58 (2). pp. 165-178. ISSN 1420-682X

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Abstract

Prokaryotic nitrate reduction can serve a number of physiological roles and can be catalysed by a number of biochemically distinct nitrate reductases. Three distinct nitrate reductase classes can be indentified in prokaryotes, NAS, NAR and NAP. NAS is located in the cytoplasmic compartment and participates in nitrogen assimilation. NAR is usually a three-subunit complex anchored to the cytoplasmic face of the membrane with its active site located in the cytoplasmic compartment and is involved in anaerobic nitrate respiration. NAP is a two-subunit complex, located in the periplasmic compartment, that is coupled to quinol oxidation via a membrane anchored tetraheme cytochrome. It shows considerable functional flexibility by participating in anaerobic respiration or redox energy dissipation depending on the organism in which it is found. The members of all three classes of enzymes bind the bis-molybdopterin guanine dinucleotide cofactor at the active site, but they differ markedly in the number and nature of cofactors used to transfer electrons to this site. Analysis of prokaryotic genome sequences available at the time of writing reveals that the different nitrate reductases are phylogenetically widespread. Key words. Nitrate assimilation; nitrate respiration; nitrogen cycle; denitrification; nitrate reductase; nitrite reductase.

Item Type:	Article
Faculty \ School:	Faculty of Science > School of Biological Sciences Faculty of Science > School of Chemistry
UEA Research Groups:	Faculty of Science > Research Groups > Organisms and the Environment Faculty of Science > Research Groups > Molecular Microbiology Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry Faculty of Science > Research Groups > Physical and Analytical Chemistry (former - to 2017)
Depositing User:	Rachel Smith
Date Deposited:	21 Jan 2011 16:44
Last Modified:	16 May 2023 12:31
URI:	https://ueaeprints.uea.ac.uk/id/eprint/19743
DOI:	10.1007/PL00000845

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