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Active‐Site Structure and Dynamics of Cytochrome c Immobilized on Self‐Assembled Monolayers—A Time‐Resolved Surface Enhanced Resonance Raman Spectroscopic Study
Author(s) -
Murgida Daniel H.,
Hildebrandt Peter
Publication year - 2001
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/1521-3773(20010216)40:4<728::aid-anie7280>3.0.co;2-p
Subject(s) - monolayer , raman spectroscopy , resonance raman spectroscopy , electron transfer , cytochrome c , chemistry , resonance (particle physics) , self assembled monolayer , redox , surface enhanced raman spectroscopy , active site , raman scattering , molecular dynamics , chemical physics , photochemistry , analytical chemistry (journal) , computational chemistry , inorganic chemistry , catalysis , organic chemistry , optics , atomic physics , physics , biochemistry , mitochondrion
Time‐resolved surface‐enhanced resonance Raman spectroscopy can selectively probe the molecular structure and dynamics of the active sites of redox proteins that are immobilized on self‐assembled monolayers on Ag electrodes (see picture). As shown for the protein cytochrome c , this method is capable of analyzing complex interfacial processes in terms of electron transfer and non‐Faradaic reactions.