通过远红外指纹对铜酶的活性位点进行分析。
Profiling the active site of a copper enzyme through its far-infrared fingerprint.
机构信息
CEA, DSV, IBEB, Lab Interact Protein Metal, CNRS, UMR Biol Veget and Microbiol Environ, Aix-Marseille Université, Saint-Paul-lez-Durance, France.
出版信息
Angew Chem Int Ed Engl. 2011 Aug 22;50(35):8062-6. doi: 10.1002/anie.201102014. Epub 2011 Jul 12.
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.
通过远红外差光谱和理论正则模式计算分析了 Cu、Zn-超氧化物歧化酶酶的金属活性部位的振动。电化学触发的 Cu(I)和 Cu(II)氧化还原态都显示出明确的红外振动模式，特别是组氨酸配体、Cu(II)-His(61)-Zn(II)桥和水拟配体的模式。
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