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Wiertz, Frank G. M., Richter, Oliver-Matthias H., Cherepanov, Alexey V., MacMillan, Fraser 
ORCID: https://orcid.org/0000-0002-2410-4790, Ludwig, Bernd and de Vries, Simon
(2004)
An oxo-ferryl tryptophan radical catalytic intermediate in cytochrome c and quinol oxidases trapped by microsecond freeze-hyperquenching (MHQ).
FEBS Letters, 575 (1-3).
pp. 127-130.
ISSN 0014-5793
Abstract
The pre-steady state reaction kinetics of the reduction of molecular oxygen catalyzed by fully reduced cytochrome oxidase from Escherichia coli and Paracoccus denitrificans were studied using the newly developed microsecond freeze-hyperquenching mixing-and-sampling technique. Reaction samples are prepared 60 and 200 μs after direct mixing of dioxygen with enzyme. Analysis of the reaction samples by low temperature UV-Vis spectroscopy indicates that both enzymes are trapped in the P state. EPR spectroscopy revealed the formation of a mixture of two radicals in both enzymes. Based on its apparent g-value and lineshape, one of these radicals is assigned to a weakly magnetically coupled oxo-ferryl tryptophan cation radical. Implications for the catalytic mechanism of cytochrome oxidases are discussed.
| Item Type: | Article |
|---|---|
| Faculty \ School: | Faculty of Science > School of Chemistry (former - to 2024) |
| UEA Research Groups: | Faculty of Science > Research Groups > Biophysical Chemistry (former - to 2017) 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 |
| Related URLs: | |
| Depositing User: | Pure Connector |
| Date Deposited: | 21 Jan 2015 11:44 |
| Last Modified: | 25 Sep 2024 11:40 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/51846 |
| DOI: | 10.1016/j.febslet.2004.08.048 |
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