New insights into the mechanism of electron transfer within flavohemoglobins: tunnelling pathways, packing density, thermodynamic and kinetic analyses

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F12%3A00384206" target="_blank" >RIV/61388963:_____/12:00384206 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1039/c2cp41261f" target="_blank" >http://dx.doi.org/10.1039/c2cp41261f</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1039/c2cp41261f" target="_blank" >10.1039/c2cp41261f</a>

Jazyk výsledku

angličtina

Název v původním jazyce

New insights into the mechanism of electron transfer within flavohemoglobins: tunnelling pathways, packing density, thermodynamic and kinetic analyses

Popis výsledku v původním jazyce

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 aflavin 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 andcomputational 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 ofcomputational 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 functio

Název v anglickém jazyce

New insights into the mechanism of electron transfer within flavohemoglobins: tunnelling pathways, packing density, thermodynamic and kinetic analyses

Popis výsledku anglicky

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 aflavin 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 andcomputational 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 ofcomputational 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 functio

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CF - Fyzikální chemie a teoretická chemie

OECD FORD obor

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Projekt

—

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2012

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Physical Chemistry Chemical Physics

ISSN

1463-9076

e-ISSN

—

Svazek periodika

14

Číslo periodika v rámci svazku

40

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

9

Strana od-do

13872-13880

Kód UT WoS článku

000309140400018

EID výsledku v databázi Scopus

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