Tryptophan-Accelerated Electron Flow Across a ProteinProtein Interface
The result's identifiers
Result code in 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>
Result on the web
<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>
Alternative languages
Result language
angličtina
Original language name
Tryptophan-Accelerated Electron Flow Across a ProteinProtein Interface
Original language description
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
Czech name
—
Czech description
—
Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CF - Physical chemistry and theoretical chemistry
OECD FORD branch
—
Result continuities
Project
<a href="/en/project/LH13015" target="_blank" >LH13015: Metalloprotein photoactivation: Structural dynamics and electron transfer</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2013
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Journal of the American Chemical Society
ISSN
0002-7863
e-ISSN
—
Volume of the periodical
135
Issue of the periodical within the volume
41
Country of publishing house
US - UNITED STATES
Number of pages
11
Pages from-to
15515-15525
UT code for WoS article
000326125200038
EID of the result in the Scopus database
—