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Allosteric control of internal electron transfer in cytochromecd<sub>1</sub> nitrite reductase

Allosteric control of internal electron transfer in cytochromecd1 nitrite reductase

Type of Publication: Journal article
Publication status: Published
Author: Farver, Ole; Kroneck, Peter M. H.; Pecht, Israel; Zumft, Walter G.
Year of publication: 2006
Published in: Rendiconti Lincei ; 17 (2006), 1. - pp. 213-220. - ISSN 2037-4631. - eISSN 1720-0776
DOI (citable link): https://dx.doi.org/10.1007/BF02904510
Summary:
Cytochromecd1 nitrite reductase is a bifunctional multiheme enzyme catalyzing the one-electron reduction of nitrite to nitric oxide and the four-electron reduction of dioxygen to water. Kinetics and thermodynamics of the internal electron transfer process in thePseudomonas stutzeri enzyme have been studied and found to be dominated by pronounced interactions between thec- and thed1- hemes. The interactions are expressed in both dramatic changes in the internal electron transfer rates between these sites and in marked cooperativity in their electron affinity. The results constitute a prime example of intra-protein control of the electron transfer rates by allosteric interactions.
Subject (DDC): 570 Biosciences, Biology
Keywords: Metalloenzymes, Electron transfer, Conformational control
Bibliography of Konstanz: Yes

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FARVER, Ole, Peter M. H. KRONECK, Israel PECHT, Walter G. ZUMFT, 2006. Allosteric control of internal electron transfer in cytochromecd1 nitrite reductase. In: Rendiconti Lincei. 17(1), pp. 213-220. ISSN 2037-4631. eISSN 1720-0776. Available under: doi: 10.1007/BF02904510

@article{Farver2006-03Allos-38439, title={Allosteric control of internal electron transfer in cytochromecd1 nitrite reductase}, year={2006}, doi={10.1007/BF02904510}, number={1}, volume={17}, issn={2037-4631}, journal={Rendiconti Lincei}, pages={213--220}, author={Farver, Ole and Kroneck, Peter M. H. and Pecht, Israel and Zumft, Walter G.} }

Farver, Ole Zumft, Walter G. eng Farver, Ole 2006-03 2017-04-07T13:22:14Z 2017-04-07T13:22:14Z Cytochromecd<sub>1</sub> nitrite reductase is a bifunctional multiheme enzyme catalyzing the one-electron reduction of nitrite to nitric oxide and the four-electron reduction of dioxygen to water. Kinetics and thermodynamics of the internal electron transfer process in thePseudomonas stutzeri enzyme have been studied and found to be dominated by pronounced interactions between thec- and thed<sub>1</sub>- hemes. The interactions are expressed in both dramatic changes in the internal electron transfer rates between these sites and in marked cooperativity in their electron affinity. The results constitute a prime example of intra-protein control of the electron transfer rates by allosteric interactions. Kroneck, Peter M. H. Pecht, Israel Kroneck, Peter M. H. Zumft, Walter G. Allosteric control of internal electron transfer in cytochromecd<sub>1</sub> nitrite reductase Pecht, Israel

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