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ToolsAllen, 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.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 (former - to 2024) Faculty of Science > School of Biological Sciences |
| UEA Research Groups: | Faculty of Science > Research Groups > Biophysical Chemistry (former - to 2017) Faculty of Science > Research Groups > Molecular Microbiology 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 > Chemistry of Light and Energy |
| Depositing User: | Rachel Smith |
| Date Deposited: | 10 May 2011 10:17 |
| Last Modified: | 24 Sep 2024 10:26 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/30097 |
| DOI: | 10.1006/bbrc.2000.4009 |
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