Profiling the Active Site of a Copper Enzyme through Its Far-Infrared Fingerprint |
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| Authors: | Marboutin Laure Petitjean Hugo Xerri Bertrand Vita Nicolas Dupeyrat François Flament Jean-Pierre Berthomieu Dorothée Berthomieu Catherine |
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| Affiliation: | CEA, DSV, IBEB, Lab Interact Protein Metal, CNRS, UMR 6191 Biol Veget and Microbiol Environ, Aix-Marseille Université, 13108 Saint-Paul-lez-Durance (France). |
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| 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. |
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| Keywords: | density functional calculations histidine IR spectroscopy proteins terahertz |
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