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

Article

DOI: 10.1007/s11426-009-0082-3

Cite this article as:
Zhu, X. & Tan, X. Sci. China Ser. B-Chem. (2009) 52: 2071. doi:10.1007/s11426-009-0082-3

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.

Keywords

Wood-Ljungdahl pathway formate dehydrogenase corrinoid iron sulfur protein acetyl-CoA synthase CO dehydrogenase 

Copyright information

© Science in China Press and Springer-Verlag GmbH 2009

Authors and Affiliations

  1. 1.Department of ChemistryFudan UniversityShanghaiChina
  2. 2.Institutes of Biomedical SciencesFudan UniversityShanghaiChina

Personalised recommendations