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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

Publikationstyp: Zeitschriftenartikel
Publikationsstatus: Published
Autor/innen: Farver, Ole; Kroneck, Peter M. H.; Pecht, Israel; Zumft, Walter G.
Erscheinungsjahr: 2006
Erschienen in: Rendiconti Lincei ; 17 (2006), 1. - S. 213-220. - ISSN 2037-4631. - eISSN 1720-0776
DOI (zitierfähiger Link): https://dx.doi.org/10.1007/BF02904510
Zusammenfassung:
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.
Fachgebiet (DDC): 570 Biowissenschaften, Biologie
Schlagwörter: Metalloenzymes, Electron transfer, Conformational control
Universitätsbibliographie: Ja

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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

@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. Kroneck, Peter M. H. Pecht, Israel Zumft, Walter G. Allosteric control of internal electron transfer in cytochromecd<sub>1</sub> nitrite reductase Pecht, Israel

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