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![Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase](/_next/image?url=https%3A%2F%2Fcloudfront.jove.com%2FCDNSource%2Fteasers%2F55858.jpg&w=3840&q=50)
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Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
Published on: December 4, 2017
Profiling the active site of a copper enzyme through its far-infrared fingerprint
Laure Marboutin1, Hugo Petitjean, Bertrand Xerri
1CEA, DSV, IBEB, Lab Interact Protein Metal, CNRS, UMR Biol Veget and Microbiol Environ, Aix-Marseille Université, Saint-Paul-lez-Durance, France.
Angewandte Chemie (International Ed. in English)
|July 14, 2011
Abstract:
Vibrations of the metal active site of the Cu,Zn-superoxide dismutase enzyme were analyzed by far-infrared difference spectroscopy and theoretical normal mode calculation. Both electrochemically triggered Cu(I) and Cu(II) redox states show well-defined infrared vibrational modes, notably modes of the histidine ligands, the Cu(II)-His(61)-Zn(II) bridge and of the water pseudo-ligand.

