| Literature DB >> 24477517 |
Jae-Hun Jeoung, Sebastian Goetzl, Sandra Elisabeth Hennig, Jochen Fesseler, Christina Wörmann, Julia Dendra, Holger Dobbek.
Abstract
The reductive acetyl-coenzyme A (acetyl-CoA) pathway, also known as the Wood-Ljungdahl pathway, allows reduction and condensation of two molecules of carbon dioxide (CO2) to build the acetyl-group of acetyl-CoA. Productive utilization of CO2 relies on a set of oxygen sensitive metalloenzymes exploiting the metal organic chemistry of nickel and cobalt to synthesize acetyl-CoA from activated one-carbon compounds. In addition to the central catalysts, CO dehydrogenase and acetyl-CoA synthase, ATPases are needed in the pathway. This allows the coupling of ATP binding and hydrolysis to electron transfer against a redox potential gradient and metal incorporation to (re)activate one of the central players of the pathway. This review gives an overview about our current knowledge on how these ATPases achieve their tasks of maturation and reductive activation.Entities:
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Year: 2014 PMID: 24477517 DOI: 10.1515/hsz-2013-0290
Source DB: PubMed Journal: Biol Chem ISSN: 1431-6730 Impact factor: 3.915