Tryptophan-Accelerated Electron Flow Across a ProteinProtein Interface

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388955%3A_____%2F13%3A00397877" target="_blank" >RIV/61388955:_____/13:00397877 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1021/ja406830d" target="_blank" >http://dx.doi.org/10.1021/ja406830d</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1021/ja406830d" target="_blank" >10.1021/ja406830d</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Tryptophan-Accelerated Electron Flow Across a ProteinProtein Interface

Popis výsledku v původním jazyce

We report a new metallolabeled blue copper protein, Re126W122CuI Pseudomonas aeruginosa azurin, which has three redox sites at well-defined distances in the protein fold: ReI(CO)3(4,7-dimethyl- 1,10-phenanthroline) covalently bound at H126, a Cu center,and an indole side chain W122 situated between the Re and Cu sites (Re- W122(indole) = 13.1 ?, dmp-W122(indole) = 10.0 ?, Re-Cu = 25.6 ?). Near-UV excitation of the Re chromophore leads to prompt CuI oxidation (<50 ns), followed by slow back ET to regenerate CuI and ground-state ReI with biexponential kinetics, 220 ns and 6 ?s. From spectroscopic measurements of kinetics and relative ET yields at different concentrations, it is likely that the photoinduced ET reactions occur in protein dimers, (Re126W122CuI)2 and that the forward ET is accelerated by intermolecular electron hopping through the interfacial tryptophan: *Re//<-W122<-CuI, where // denotes a proteinprotein interface. Solution mass spectrometry confirms a broad oligomer distr

Název v anglickém jazyce

Tryptophan-Accelerated Electron Flow Across a ProteinProtein Interface

Popis výsledku anglicky

We report a new metallolabeled blue copper protein, Re126W122CuI Pseudomonas aeruginosa azurin, which has three redox sites at well-defined distances in the protein fold: ReI(CO)3(4,7-dimethyl- 1,10-phenanthroline) covalently bound at H126, a Cu center,and an indole side chain W122 situated between the Re and Cu sites (Re- W122(indole) = 13.1 ?, dmp-W122(indole) = 10.0 ?, Re-Cu = 25.6 ?). Near-UV excitation of the Re chromophore leads to prompt CuI oxidation (<50 ns), followed by slow back ET to regenerate CuI and ground-state ReI with biexponential kinetics, 220 ns and 6 ?s. From spectroscopic measurements of kinetics and relative ET yields at different concentrations, it is likely that the photoinduced ET reactions occur in protein dimers, (Re126W122CuI)2 and that the forward ET is accelerated by intermolecular electron hopping through the interfacial tryptophan: *Re//<-W122<-CuI, where // denotes a proteinprotein interface. Solution mass spectrometry confirms a broad oligomer distr

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

<a href="/cs/project/LH13015" target="_blank" >LH13015: Fotoaktivace metaloproteinů: strukturní dynamika a přenos elektronu</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2013

Kód důvěrnosti údajů

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

Název periodika

Journal of the American Chemical Society

ISSN

0002-7863

e-ISSN

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Svazek periodika

135

Číslo periodika v rámci svazku

41

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

11

Strana od-do

15515-15525

Kód UT WoS článku

000326125200038

EID výsledku v databázi Scopus

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