| Literature DB >> 18433623 |
Thomas A Clarke1, Paul C Mills, Susie R Poock, Julea N Butt, Myles R Cheesman, Jeffrey A Cole, Jay C D Hinton, Andrew M Hemmings, Gemma Kemp, Christopher A G Söderberg, Stephen Spiro, Jessica Van Wonderen, David J Richardson.
Abstract
The periplasmic cytochrome c nitrite reductase (Nrf) system of Escherichia coli utilizes nitrite as a respiratory electron acceptor by reducing it to ammonium. Nitric oxide (NO) is a proposed intermediate in this six-electron reduction and NrfA can use exogenous NO as a substrate. This chapter describes the method used to assay Nrf-catalyzed NO reduction in whole cells of E. coli and the procedures for preparing highly purified NrfA suitable for use in kinetic, spectroscopic, voltammetric, and crystallization studies.Entities:
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Year: 2008 PMID： 18433623 DOI： 10.1016/S0076-6879(07)37004-3
Source DB: PubMed Journal: Methods Enzymol ISSN： 0076-6879 Impact factor: 1.600