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1
The mechanism of olefin epoxidation by oxo-iron porphyrins. Direct observation of an intermediate.氧代铁卟啉催化烯烃环氧化反应的机理。中间体的直接观测。
J Am Chem Soc. 1986 Feb 1;108(3):507-8. doi: 10.1021/ja00263a026.
2
Rapid freeze-quench ENDOR study of chloroperoxidase compound I: the site of the radical.氯过氧化物酶化合物I的快速冷冻淬灭电子核双共振研究：自由基位点
J Am Chem Soc. 2006 May 3;128(17):5598-9. doi: 10.1021/ja060776l.
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Cytochrome p450 compound I.细胞色素P450复合酶I
J Am Chem Soc. 2006 Apr 12;128(14):4580-1. doi: 10.1021/ja060048y.
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Kinetic studies of reactions of iron(IV)-oxo porphyrin radical cations with organic reductants.铁（IV）-氧代卟啉自由基阳离子与有机还原剂反应的动力学研究。
J Inorg Biochem. 2006 Apr;100(4):524-32. doi: 10.1016/j.jinorgbio.2005.12.022. Epub 2006 Feb 28.
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X-ray absorption spectroscopy of chloroperoxidase compound I: Insight into the reactive intermediate of P450 chemistry.氯过氧化物酶化合物I的X射线吸收光谱：深入了解细胞色素P450化学的反应中间体
Proc Natl Acad Sci U S A. 2005 Nov 15;102(46):16563-5. doi: 10.1073/pnas.0507069102. Epub 2005 Nov 7.
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Photochemical generation of a highly reactive iron-oxo intermediate. A true iron(V)-oxo species?高活性铁氧中间体的光化学生成。一种真正的五价铁氧物种？
J Am Chem Soc. 2005 Oct 12;127(40):13776-7. doi: 10.1021/ja0542439.
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Highly reactive electrophilic oxidants in cytochrome P450 catalysis.细胞色素P450催化作用中的高反应活性亲电氧化剂。
Biochem Biophys Res Commun. 2005 Dec 9;338(1):394-403. doi: 10.1016/j.bbrc.2005.08.208. Epub 2005 Sep 6.
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Structure and chemistry of cytochrome P450.细胞色素P450的结构与化学性质
Chem Rev. 2005 Jun;105(6):2253-77. doi: 10.1021/cr0307143.
9
Oxoiron(IV) porphyrin pi-cation radical complexes with a chameleon behavior in cytochrome P450 model reactions.在细胞色素P450模型反应中具有变色龙行为的氧代铁（IV）卟啉π-阳离子自由基配合物。
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Formation of compound I by photo-oxidation of compound II.通过化合物II的光氧化形成化合物I。
Org Lett. 2005 Mar 17;7(6):1193-5. doi: 10.1021/ol050296j.

氯过氧化物酶的化合物I衍生物（一种细胞色素P450氧化剂模型）催化的双电子氧化动力学。

Kinetics of two-electron oxidations by the compound I derivative of chloroperoxidase, a model for cytochrome P450 oxidants.

作者信息

Zhang Rui, Nagraj Nandini, Lansakara-P Dharmika S P, Hager Lowell P, Newcomb Martin

机构信息

Department of Chemistry, University of Illinois at Chicago, 60607, USA.

出版信息

Org Lett. 2006 Jun 22;8(13):2731-4. doi: 10.1021/ol060762k.

DOI:10.1021/ol060762k
PMID:16774243
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2535770/
Abstract

[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.

摘要

[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。