波谱学杂志 ›› 2011, Vol. 28 ›› Issue (4): 490-501.

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乙酰辅酶A合成酶/一氧化碳脱氢酶的EPR研究

刘奕,谭相石*   

  1. 复旦大学 化学系,  生物医学研究院,上海 200433
  • 收稿日期:2011-09-30 出版日期:2011-12-05 发布日期:2011-12-05
  • 基金资助:

    国家自然科学基金资助项目(20771029,  91013001).

EPR Studies on Acetyl-CoA Synthase/Carbon Monoxide Dehydrogenase

 LIU Yi, TAN Xiang-Shi*   

  1. Department of Chemistry and Institute of Biomedical Science, Fudan Univeristy, Shanghai 200433, China
  • Received:2011-09-30 Online:2011-12-05 Published:2011-12-05
  • Supported by:

    国家自然科学基金资助项目(20771029,  91013001).

摘要:

来源于厌氧微生物的乙酰辅酶A合成酶/一氧化碳脱氢酶(ACS/CODH)含有金属Ni和Fe所组成的多达7个金属簇中心,能够催化CO和CO2的可逆氧化还原,并利用CO/CO2和H2作为碳源和能源合成乙酰辅酶A. 近年来,随着全球能源危机和温室效应等环境问题的加重,这类金属蛋白酶的研究日益成为人们关注的热点. 电子顺磁共振光谱(EPR)作为一种研究金属价态和配位结构的有效技术,从20世纪80年代开始便被广泛地应用到该酶的研究中. 该文将从ACS/CODH的各个金属簇中心入手,介绍每个金属中心的结构、功能和EPR研究.

关键词: 电子顺磁共振光谱 (EPR), 乙酰辅酶A合成酶/一氧化碳脱氢酶(ACS/CODH), 金属酶, 金属蛋白, 酶催化反应机理

Abstract:

Actyl-CoA synthase/carbon monoxide dehydogenase (ACS/CODH) from anaerobic microbes is a Ni, Fe-containing metalloenzyme, which contains up to seven metal clusters. It catalyses the reversible conversion of CO2 and CO, and utilizes CO and/or CO as carbon source and H2 as energy to synthesize actyl-CoA. Interests in these enzymes have been increased in recent years due to energy crisis and environmental issues such as greenhouse effects. As one of the most effective techniques to detect the valence state and coordination of metals, EPR has been used to study the enzyme since 1980s. In this paper, the structures of metal clusters, function and catalytic mechanism of ACS/CODH studied by EPR were summarized and reviewed.

Key words: EPR,  , actyl-CoA synthase/carbon monoxide dehydogenase, metalloenzyme, metalloprotein, enzymology

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