Electrocatalytic reduction of nitrate and selenate by NapAB

Gates, Andrew J. ORCID: https://orcid.org/0000-0002-4594-5038, Butler, Clive S., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Butt, Julea N. ORCID: https://orcid.org/0000-0002-9624-5226 (2011) Electrocatalytic reduction of nitrate and selenate by NapAB. Biochemical Society Transactions, 39 (1). pp. 236-242. ISSN 0300-5127

Full text not available from this repository. (Request a copy)

Abstract

Bacterial cellular metabolism is renowned for its metabolic diversity and adaptability. However, certain environments present particular challenges. Aerobic metabolism of highly reduced carbon substrates by soil bacteria such as Paracoccus pantotrophus presents one such challenge since it may result in excessive electron delivery to the respiratory redox chain when compared with the availability of terminal oxidant, O2. The level of a periplasmic ubiquinol-dependent nitrate reductase, NAP, is up-regulated in the presence of highly reduced carbon substrates. NAP oxidizes ubiquinol at the periplasmic face of the cytoplasmic membrane and reduces nitrate in the periplasm. Thus its activity counteracts the accumulation of excess reducing equivalents in ubiquinol, thereby maintaining the redox poise of the ubiquinone/ubiquinol pool without contributing to the protonmotive force across the cytoplasmic membrane. Although P. pantotrophus NapAB shows a high level of substrate specificity towards nitrate, the enzyme has also been reported to reduce selenate in spectrophotometric solution assays. This transaction draws on our current knowledge concerning the bacterial respiratory nitrate reductases and extends the application of PFE (protein film electrochemistry) to resolve and quantify the selenate reductase activity of NapAB.

Item Type:	Article
Faculty \ School:	Faculty of Science > School of Biological Sciences Faculty of Science > School of Chemistry
Depositing User:	Rachel Smith
Date Deposited:	17 Feb 2011 16:45
Last Modified:	15 May 2023 00:06
URI:	https://ueaeprints.uea.ac.uk/id/eprint/21392
DOI:	10.1042/BST0390236

Actions (login required)

View Item