Zhang Rui, Nagraj Nandini, Lansakara-P Dharmika S P, Hager Lowell P, Newcomb Martin
Department of Chemistry, University of Illinois at Chicago, 60607, USA.
Org Lett. 2006 Jun 22;8(13):2731-4. doi: 10.1021/ol060762k.
[structure: see text] Rate constants for two-electron oxidation reactions of Compound I from chloroperoxidase (CPO) with a variety of substrates were measured by stopped-flow kinetic techniques. The thiolate ligand of CPO Compound I activates the iron-oxo species with the result that oxidation reactions are 2 to 3 orders of magnitude faster than oxidations by model iron(IV)-oxo porphyrin radical cations containing weaker binding counterions.
[结构:见正文] 采用停流动力学技术测定了氯过氧化物酶(CPO)中化合物I与多种底物的双电子氧化反应的速率常数。CPO化合物I的硫醇盐配体激活了铁-氧物种,结果是氧化反应比含有较弱结合抗衡离子的模型铁(IV)-氧卟啉自由基阳离子的氧化反应快2至3个数量级。