Multiple forms of the catalytic centre, Cu-z, in the enzyme nitrous oxide reductase from Paracoccus pantotrophus

Rasmussen, Tim, Berks, Ben C., Butt, Julea N. ORCID: https://orcid.org/0000-0002-9624-5226 and Thomson, Andrew J. (2002) Multiple forms of the catalytic centre, Cu-z, in the enzyme nitrous oxide reductase from Paracoccus pantotrophus. Biochemical Journal, 364 (3). pp. 807-815. ISSN 1470-8728

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

Abstract

Nitrous oxide reductase catalyses the reduction of nitrous oxide to dinitrogen at a unique tetranuclear copper site, called CuZ, which has a central inorganic sulphide ligand. Limited incubation with oxygen during the preparation of nitrous oxide reductase from Paracoccus pantotrophus results in changed redox properties of the catalytic centre by comparison with anaerobic preparations. While the anaerobically purified enzyme has a catalytic centre which performs a single electron step at a midpoint potential of Em =+60mV versus the standard hydrogen electrode (n = 1), the altered centre shows no redox change under similar experimental conditions. Spectroscopic properties of this ‘redox fixed’ centre are similar to spectra of the reduced ‘redox active’ form of CuZ, although the positions and intensities of a number of transitions are changed in the optical spectrum. These observations are interpreted in terms of two forms of the catalytic centre, called CuZ and CuZ∗. The structural relationship between these forms is unclear. EPR and magnetic circular dichroism spectra suggest that the basic Cu4S structure is common to both. Curiously, steady-state activity of the aerobic enzyme preparation is slightly increased despite the fact the catalytic centre does not undergo detectable redox changes.

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 Groups > Chemistry of Light and Energy Faculty of Science > Research Groups > Chemistry of Life Processes Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry Faculty of Science > Research Groups > Biophysical Chemistry (former - to 2017)
Depositing User:	EPrints Services
Date Deposited:	01 Oct 2010 13:37
Last Modified:	24 Sep 2024 10:19
URI:	https://ueaeprints.uea.ac.uk/id/eprint/663
DOI:	10.1042/BJ20020055

Actions (login required)

View Item