The Paracoccus denitrificans respiratory NO reductase (NorBC)

Field, SJ, Thorndycroft, FH, Matorin, AD, Richardson, DJ and Watmough, NJ (2008) The Paracoccus denitrificans respiratory NO reductase (NorBC). Methods in Enzymology, 437. pp. 79-101. ISSN 1557-7988

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

Abstract

The two subunit cytochrome bc complex (NorBC) isolated from membranes of the model denitrifying soil bacterium Paracoccus denitrificans is the best characterized example of the bacterial respiratory nitric oxide reductases. These are members of the superfamily of heme-copper oxidases and are characterized by the elemental composition of their active site, which contains nonheme iron rather than copper, at which the reductive coupling of two molecules of nitric oxide to form nitrous oxide is catalyzed. This chapter describes methods for the purification and characterization of both native nitric oxide reductase from P. denitrificans and a recombinant form of the enzyme expressed in Escherichia coli, which enables site-directed mutagenesis of the catalytic subunit NorB. Examples are given of electronic absorption and electron paramagnetic resonance spectra that characterize the enzyme in a number of redox states, along with a method for the routine assay of the complex using its natural electron donor pseudoazurin.

Item Type: Article
Faculty \ School: Faculty of Science > School of Biological Sciences
University of East Anglia > Faculty of Science > Research Groups > Molecular Microbiology
University of East Anglia > Faculty of Science > Research Groups > Organisms and the Environment
Related URLs:
Depositing User: EPrints Services
Date Deposited: 01 Oct 2010 14:38
Last Modified: 10 Aug 2018 17:30
URI: https://ueaeprints.uea.ac.uk/id/eprint/1601
DOI: 10.1016/S0076-6879(07)37005-5

Actions (login required)

View Item