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Gwyer, James D., Richardson, David J. 
ORCID: https://orcid.org/0000-0002-6847-1832 and Butt, Julea N. ORCID: https://orcid.org/0000-0002-9624-5226
(2005)
Diode or tunnel-diode characteristics? Resolving the catalytic consequences of proton coupled electron transfer in a multi-centered oxidoreductase.
Journal of the American Chemical Society, 127 (43).
pp. 14964-14965.
ISSN 0002-7863
Abstract
Protein film voltammetry has been employed to define multiple catalytic consequences of proton coupled electron transfer (PCET) in a cytochrome c nitrite reductase. Current-potential profiles reflecting the steady-state rate of nitrite-limited reduction have been defined from pH 4 to 8. Lowering the electrode potential at pH 8 causes the catalytic current to increase and then decrease before it takes a value independent of any further lowering of electrode potential. By comparison, at pH 4, catalysis is initiated at more positive electrode potentials in an approximately sigmoidal fashion with no attenuation of the catalytic rate evident at more negative electrode potentials. The results show that activity is turned on by the coupled transfer of two electrons and one proton to the enzyme. The decreased rate of catalysis at lower electrode potentials under more alkaline conditions shows that this rate attenuation occurs only when reduction is not coupled to compensating protonation(s) of the enzyme. Sites within the enzyme whose reduction and/or protonation may contribute to the definition of these activities are discussed.
| Item Type: | Article |
|---|---|
| Faculty \ School: | Faculty of Science > School of Biological Sciences Faculty of Science > School of Chemistry (former - to 2024) |
| UEA Research Groups: | Faculty of Science > Research Groups > Molecular Microbiology Faculty of Science > Research Groups > Organisms and the Environment Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry 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 Groups > Biophysical Chemistry (former - to 2017) |
| Depositing User: | Rachel Smith |
| Date Deposited: | 17 Feb 2011 14:33 |
| Last Modified: | 24 Sep 2024 09:54 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/21410 |
| DOI: | 10.1021/ja054160s |
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