用一氧化氮对欧洲亚硝化单胞菌羟胺氧化还原酶进行选择性单电子还原。
Selective one-electron reduction of Nitrosomonas europaea hydroxylamine oxidoreductase with nitric oxide.
作者信息
Cabail Maria Zulema, Pacheco A Andrew
机构信息
Department of Chemistry, University of Wisconsin-Milwaukee, Milwaukee, Wisconsin 53211, USA.
出版信息
Inorg Chem. 2003 Jan 27;42(2):270-2. doi: 10.1021/ic025779n.
Hydroxylamine oxidoreductase (HAO) from the autotrophic bacterium Nitrosomonas europaea catalyzes the 4-e- oxidation of NH2-OH to NO2-. The e- are transferred from NH2OH to an unusual 5-coordinate heme known as P460, which is the active site of HAO, and from there to an array of seven c-type hemes. NO., generated by laser flash photolysis of N,N'-bis(carboxymethyl)-N,N'-dinitroso-1,4-phenylenediamine, is found to act as a 1-e- donor to HAO. Most likely NO. binds P460 to yield a [Fe(NO)]6 moiety, which then hydrolyzes to give the reduced enzyme and NO2-. The [Fe(NO)]6 moiety is also a plausible final intermediate in the oxidation of NH2OH.
自养细菌欧洲亚硝化单胞菌中的羟胺氧化还原酶（HAO）催化NH2-OH的4电子氧化生成NO2-。电子从NH2OH转移到一种不同寻常的五配位血红素，即P460，它是HAO的活性位点，然后从那里转移到一系列七个c型血红素。通过激光闪光光解N，N'-双（羧甲基）-N，N'-二亚硝基-1，4-苯二胺产生的NO·被发现可作为HAO的单电子供体。很可能NO·与P460结合生成[Fe(NO)]6部分，然后水解生成还原态酶和NO2-。[Fe(NO)]6部分也是NH2OH氧化过程中一个合理的最终中间体。
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