Profiling the Active Site of a Copper Enzyme through Its Far-Infrared Fingerprint

Vibrations of the metal active site of the Cu,Zn‐superoxide dismutase enzyme were analyzed by far‐infrared difference spectroscopy (see picture) and theoretical normal mode calculation. Both electrochemically triggered CuI and CuII redox states show well‐defined infrared vibrational modes, notably m...

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Veröffentlicht in:	Angewandte Chemie International Edition 2011-08, Vol.50 (35), p.8062-8066
Hauptverfasser:	Marboutin, Laure, Petitjean, Hugo, Xerri, Bertrand, Vita, Nicolas, Dupeyrat, François, Flament, Jean-Pierre, Berthomieu, Dorothée, Berthomieu, Catherine
Format:	Artikel
Sprache:	eng
Schlagworte:	Catalytic Domain Chemical Sciences Copper - chemistry density functional calculations histidine Histidine - chemistry IR spectroscopy Ligands Material chemistry Oxidation-Reduction proteins Spectroscopy, Fourier Transform Infrared Superoxide Dismutase - chemistry Superoxide Dismutase - metabolism terahertz Water - chemistry
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Beschreibung
Zusammenfassung:	Vibrations of the metal active site of the Cu,Zn‐superoxide dismutase enzyme were analyzed by far‐infrared difference spectroscopy (see picture) and theoretical normal mode calculation. Both electrochemically triggered CuI and CuII redox states show well‐defined infrared vibrational modes, notably modes of the histidine ligands, the CuII‐His61‐ZnII bridge and of the water pseudo‐ligand.
ISSN:	1433-7851 1521-3773
DOI:	10.1002/anie.201102014