A novel conformer of oxidized Paracoccus pantotrophus cytochrome cd(1) observed by freeze-quench NIR-MCD spectroscopy

Allen, James W. A., Cheesman, Myles R., Higham, Christopher W., Ferguson, Stuart J. and Watmough, Nicholas J. (2000) A novel conformer of oxidized Paracoccus pantotrophus cytochrome cd(1) observed by freeze-quench NIR-MCD spectroscopy. Biochemical and Biophysical Research Communications, 279 (2). pp. 674-677. ISSN 0006-291X

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

Abstract

Paracoccus pantotrophus cytochrome cd(1) is a physiological nitrite reductase and an in vitro hydroxylamine reductase. The oxidised "as isolated" form of the enzyme has bis-histidinyl coordinated c-heme and upon reduction its coordination changes to histidine/ methionine. Following treatment of reduced enzyme with hydroxylamine, a novel, oxidised, conformer of the enzyme is obtained. We have devised protocols for freeze-quench near-ir-MCD spectroscopy that have allowed us to establish unequivocally the c-heme coordination of this species as His/Met. Thus it is shown that the catalytically competent, hydroxylamine reoxidised, form of P. pantotrophus cytochrome cd(1) has different axial ligands to the c-heme than "as isolated" enzyme. (C) 2000 Academic Press.

Item Type: Article
Faculty \ School: Faculty of Science > School of Chemistry
Faculty of Science > School of Biological Sciences
Depositing User: Rachel Smith
Date Deposited: 10 May 2011 10:17
Last Modified: 21 Apr 2020 21:12
URI: https://ueaeprints.uea.ac.uk/id/eprint/30097
DOI: 10.1006/bbrc.2000.4009

Actions (login required)

View Item View Item