Počet záznamů: 1
New insights into the mechanism of electron transfer within flavohemoglobins: tunnelling pathways, packing density, thermodynamic and kinetic analyses
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SYSNO ASEP 0384206 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název New insights into the mechanism of electron transfer within flavohemoglobins: tunnelling pathways, packing density, thermodynamic and kinetic analyses Tvůrce(i) El Hammi, E. (FR)
Houée-Lévin, Ch. (FR)
Řezáč, Jan (UOCHB-X) RID, ORCID
Lévy, B. (FR)
Demachy, I. (FR)
Baciou, L. (FR)
de la Lande, A. (FR)Celkový počet autorů 7 Zdroj.dok. Physical Chemistry Chemical Physics. - : Royal Society of Chemistry - ISSN 1463-9076
Roč. 14, č. 40 (2012), s. 13872-13880Poč.str. 9 s. Jazyk dok. eng - angličtina Země vyd. GB - Velká Británie Klíč. slova metalloenzymes ; flavohemoglobin ; electron transfer ; monooxygenase Vědní obor RIV CF - Fyzikální chemie a teoretická chemie CEZ AV0Z40550506 - UOCHB-X (2005-2011) UT WOS 000309140400018 DOI https://doi.org/10.1039/c2cp41261f Anotace Flavohemoglobins (FlavoHb) are metalloenzymes catalyzing the reaction of nitric oxide dioxygenation. The iron cation of the heme group needs to be preliminarily reduced to the ferrous state to be catalytically competent. This reduction is triggered by a flavin adenine dinucleotide (FAD) prosthetic group which is localized in a distinct domain of the protein. In this paper we obtain new insights into the internal long range electron transfer (over ca. 12 angstrom) using a combination of experimental and computational approaches. Employing a time-resolved pulse radiolysis technique we report the first direct measurement of the FADH(center dot) -> HemeFe(III) electron transfer rate. A rate constant of (6.8 +/- 0.5) x 10(3) s(-1) is found. A large panel of computational approaches are used to provide the first estimation of the thermodynamic characteristics of the internal electron transfer step within flavoHb: both the driving force and the reorganization energy are estimated as a function of the protonated state of the flavin semi-quinone. We also report an analysis of the electron pathways involved in the tunnelling of the electron through the aqueous interface between the globin and the flavin domains. Pracoviště Ústav organické chemie a biochemie Kontakt asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Jana Procházková, Tel.: 220 183 418 Rok sběru 2013
Počet záznamů: 1