观察到一个前所未有的铜双组氨酸位点：亚硝酸还原酶H129V突变体的晶体结构。
Observation of an unprecedented Cu Bis-His site: crystal structure of the H129V mutant of nitrite reductase.
作者信息
Ellis Mark J, Antonyuk Svetlana V, Strange Richard W, Sawers Gary, Eady Robert R, Hasnain S Samar
机构信息
Molecular Biophysics Group, CCLRC Daresbury Laboratory, Warrington, Cheshire, UK.
出版信息
Inorg Chem. 2004 Nov 29;43(24):7591-3. doi: 10.1021/ic048966p.
PMID:15554622
Abstract
Copper nitrite reductases contain both an electron-transfer type 1 Cu site and a catalytic type 2 Cu site. We have mutated one of the type 2 copper ligating histidines to observe the effect on catalytic turnover. This mutation has created a unique site where Cu is ligated by 2 His Nepsilon2 atoms alone.
摘要
亚硝酸铜还原酶同时含有一个电子传递型1铜位点和一个催化型2铜位点。我们将其中一个与2型铜配位的组氨酸进行了突变，以观察其对催化周转的影响。这种突变产生了一个独特的位点，在该位点上铜仅由两个组氨酸的Nε2原子配位。
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