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Metalloproteins/metalloenzymes for the synthesis of acetyl-CoA in the Wood-Ljungdahl pathway

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Abstract

This paper focuses on the group of metalloproteins/metalloenzymes in the acetyl-coenzyme A synthesis pathway of anaerobic microbes called Wood-Ljungdahl pathway, including formate dehydrogenase (FDH), corrinoid iron sulfur protein (CoFeSP), acetyl-CoA synthase (ACS) and CO dehydrogenase (CODH). FDH, a key metalloenzyme involved in the conversion of carbon dioxide to methyltetrahydrofolate, catalyzes the reversible oxidation of formate to carbon dioxide. CoFeSP, as a methyl group transformer, accepts the methyl group from CH3-H4 folate and then transfers it to ACS. CODH reversibly catalyzes the reduction of CO2 to CO and ACS functions for acetyl-coenzyme A synthesis through condensation of the methyl group, CO and coenzyme A, to finish the whole pathway. This paper introduces the structure, function and reaction mechanisms of these enzymes.

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  1. Department of Chemistry, Fudan University, Shanghai, 200433, China

    XiaoFei Zhu & XiangShi Tan

  2. Institutes of Biomedical Sciences, Fudan University, Shanghai, 200433, China

    XiangShi Tan

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  1. XiaoFei Zhu
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Correspondence to XiangShi Tan.

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Supported by the National Natural Science Foundation of China (Grant No. 20771029), Shanghai Pujiang Talent Project (Grant No. 08PJ14017) and Shanghai Leading Academic Discipline Project (Grant No. B108)

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Zhu, X., Tan, X. Metalloproteins/metalloenzymes for the synthesis of acetyl-CoA in the Wood-Ljungdahl pathway. Sci. China Ser. B-Chem. 52, 2071–2082 (2009). https://doi.org/10.1007/s11426-009-0082-3

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