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[铁]氢化酶的有机金属活性位点:模型与内环境稳定态

The organometallic active site of [Fe]hydrogenase: models and entatic states.

作者信息

Darensbourg Marcetta Y, Lyon Erica J, Zhao Xuan, Georgakaki Irene P

机构信息

Texas A&M University, Department of Chemistry, College Station, TX 77843, USA.

出版信息

Proc Natl Acad Sci U S A. 2003 Apr 1;100(7):3683-8. doi: 10.1073/pnas.0536955100. Epub 2003 Mar 17.

DOI:10.1073/pnas.0536955100
PMID:12642671
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC152982/
Abstract

The simple organometallic, (mu-S(2))Fe(2)(CO)(6), serves as a precursor to synthetic analogues of the chemically rudimentary iron-only hydrogenase enzyme active site. The fundamental properties of the (mu-SCH(2)CH(2)CH(2)S)Fe(CO)(3) compound, including structural mobility and regioselectivity in cyanidecarbon monoxide substitution reactions, relate to the enzyme active site in the form of transition-state structures along reaction paths rather than ground-state structures. Even in the absence of protein-based active-site organization, the ground-state structural model complexes are shown to serve as hydrogenase enzyme reaction models, H(2) uptake and H(2) production, with the input of photo- or electrochemical energy, respectively.

摘要

简单的有机金属化合物(μ-S₂)Fe₂(CO)₆可作为化学上基本的仅含铁氢化酶酶活性位点的合成类似物的前体。(μ-SCH₂CH₂CH₂S)[Fe(CO)₃]₂化合物的基本性质,包括氰化物-一氧化碳取代反应中的结构迁移率和区域选择性,是以反应路径上的过渡态结构而非基态结构的形式与酶活性位点相关。即使在没有基于蛋白质的活性位点组织的情况下,基态结构模型配合物也被证明可分别在光或电化学能量输入下作为氢化酶酶反应模型,用于氢气吸收和氢气产生。

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本文引用的文献

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Hydrogenase: a bacterial enzyme activating molecular hydrogen: The properties of the enzyme.氢化酶:一种激活分子氢的细菌酶:该酶的特性
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