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Clarke, Thomas A. 
ORCID: https://orcid.org/0000-0002-6234-1914, Cole, Jeffrey A., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Hemmings, Andrew M. ORCID: https://orcid.org/0000-0003-3053-3134
(2007)
The crystal structure of the pentahaem c-type cytochrome NrfB and characterization of its solution-state interaction with the pentahaem nitrite reductase NrfA.
Biochemical Journal, 406 (1).
pp. 19-30.
Abstract
NrfB is a small pentahaem electron-transfer protein widely involved in the respiratory reduction of nitrite or nitric oxide to ammonia, processes that provide energy for anaerobic metabolism in many enteric bacteria and also serve to detoxify these reactive nitrogen species. The X-ray crystal structure of Escherichia coli NrfB is presented at 1.74 Å (1 Å=0.1 nm) resolution. The architecture of the protein is that of a 40 Å ‘nanowire’ in which the five haems are positioned within 6 Å of each other along a polypeptide scaffold. During nitrite reduction, the physiological role of NrfB is to mediate electron transfer to another pentahaem protein, NrfA, the enzyme that catalyses periplasmic nitrite or nitric oxide reduction. Protein–protein interaction studies suggest NrfA and NrfB can form a 20-haem NrfA2–NrfB2 heterotetrameric complex.
| Item Type: | Article |
|---|---|
| Faculty \ School: | Faculty of Science > School of Biological Sciences |
| UEA Research Groups: | Faculty of Science > Research Groups > Molecular Microbiology Faculty of Science > Research Groups > Energy Materials Laboratory Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry Faculty of Science > Research Groups > Organisms and the Environment Faculty of Science > Research Groups > Plant Sciences Faculty of Science > Research Groups > Chemistry of Life Processes Faculty of Science > Research Groups > Biophysical Chemistry (former - to 2017) |
| Depositing User: | Users 2731 not found. |
| Date Deposited: | 24 May 2011 09:50 |
| Last Modified: | 16 May 2023 00:41 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/31287 |
| DOI: | 10.1042/BJ20070321 |
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