Production and Properties of Enzymes That Activate and Produce Carbon Monoxide

Overview

Journal Methods Enzymol

Specialty Biochemistry

Date 2018 Dec 5

PMID 30509471

Citations 1

Authors

Rodney Burton

Mehmet Can

Daniel Esckilsen

Seth Wiley

Stephen W Ragsdale

Affiliations

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Abstract

The chapter focuses on the methods involved in producing and characterizing two key nickel-iron-sulfur enzymes in the Wood-Ljungdahl pathway (WLP) of anaerobic conversion of carbon dioxide fixation into acetyl-CoA: carbon monoxide dehydrogenase (CODH) and acetyl-CoA synthase (ACS). The WLP is used for biosynthesis of cell material and energy conservation by anaerobic bacteria and archaea, and it is central to several industrial biotechnology processes aimed at using syngas and waste gases for the production of fuels and chemicals. The pathway can run in reverse to allow organisms, e. g., methanogens and sulfate reducers, to grow on acetate. The CODH and ACS intertwine to form a tenacious CODH/ACS complex that converts CO, a methyl group, and coenzyme A into acetyl-CoA. CODH also behaves as a modular unit that can function as an independent homodimer. Besides coupling to ACS, CODH can interact with hydrogenases to couple CO oxidation to H formation. These enzymes have been purified and characterized from several microbes.

Citing Articles

Batch and semi-continuous fermentation with Parageobacillus thermoglucosidasius DSM 6285 for H production.

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C Electron Nuclear Double Resonance Spectroscopy Shows Acetyl-CoA Synthase Binds Two Substrate CO in Multiple Binding Modes and Reveals the Importance of a CO-Binding "Alcove".

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