A long-lived, substrate-hydroxylating peroxodiiron(III/III) intermediate in the amine oxygenase, AurF, from Streptomyces thioluteus.
A long-lived, substrate-hydroxylating peroxodiiron(III/III) intermediate in the amine oxygenase, AurF, from Streptomyces thioluteus.
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DOI：
10.1021/ja9064969
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发表时间：
2009-09-30
影响因子：
15
通讯作者：
Krebs, Carsten
中科院分区：
文献类型：
--
作者：
Korboukh, Victoria Korneeva;Li, Ning;Barr, Eric W.;Bollinger, J. Martin, Jr.;Krebs, Carsten
硫解链霉菌（Streptomyces thioluteus）的胺加氧酶AuRF催化对氨基苯甲酸酯（pABA）的六电子氧化为对硝基苯甲酸酯（pNBA）。在这项工作中，我们已经研究了其还原的Fe 2（II/II）辅因子与O2的反应，这导致生成的过氧-Fe 2（III/III）中间体。在不存在底物的情况下，该中间体异常稳定（t1/2 = 7 min，20°C），允许其积累到几乎化学计量的量。它的衰变被底物pABA加速约105倍，这意味着它是影响胺到羟胺的双电子氧化的复合物。通过含有过量中间体的溶液将pABA几乎定量地转化为pNBA，这表明它也可能胜任随后的两个双电子氧化，从而产生产物。
The amine oxygenase AurF from Streptomyces thioluteus catalyzes the six-electron oxidation of p-aminobenzoate (pABA) to p-nitrobenzoate (pNBA). In this work, we have studied the reaction of its reduced Fe2(II/II) cofactor with O2, which results in generation of a peroxo-Fe2(III/III) intermediate. In the absence of substrate, this intermediate is unusually stable (t1/2 = 7 min at 20°C), allowing for its accumulation to almost stoichiometric amounts. Its decay is accelerated ~105-fold by the substrate, pABA, implying that it is the complex that effects the two-electron oxidation of the amine to the hydroxylamine. The nearly quantitative conversion of pABA to pNBA by solutions containing an excess of the intermediate suggests that it may also be competent for the two subsequent two-electron oxidations leading to the product.
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影响因子：
5.6
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通讯作者：
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