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ToolsJepson, B. J. N., Marietou, A., Mohan, S., Cole, J. A., Butler, C. S. and Richardson, D. J. (2006) Evolution of the soluble nitrate reductase: defining the monomeric periplasmic nitrate reductase subgroup. Biochemical Society Transactions, 34 (1). pp. 122-126. ISSN 1470-8752
Full text not available from this repository. (Request a copy)Abstract
Bacterial nitrate reductases can be classified into at least three groups according to their localization and function, namely membrane-bound (NAR) or periplasmic (NAP) respiratory and cytoplasmic assimilatory (NAS) enzymes. Monomeric NASs are the simplest of the soluble nitrate reductases, although heterodimeric NASs exist, and a common structural arrangement of NAP is that of a NapAB heterodimer. Using bioinformatic analysis of published genomes, we have identified more representatives of a monomeric class of NAP, which is the evolutionary link between the monomeric NASs and the heterodimeric NAPs. This has further established the monomeric structural clade of NAP. The operons of the monomeric NAP do not contain NapB and suggest that other redox partners are employed by these enzymes, including NapM or NapG predicted proteins. A structural alignment and comparison of the monomeric and heterodimeric NAPs suggests that a difference in surface polarity is related to the interaction of the respective catalytic subunit and redox partner.
| Item Type: | Article |
|---|---|
| Faculty \ School: | Faculty of Science > School of Biological Sciences |
| 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 |
| Depositing User: | EPrints Services |
| Date Deposited: | 01 Oct 2010 13:37 |
| Last Modified: | 28 Mar 2025 04:02 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/1160 |
| DOI: | 10.1042/BST0340122 |
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