Abstract
Clostridium autoethanogenum is an industrial microbe used for the commercial-scale production of ethanol from carbon monoxide. While significant progress has been made in the attempted diversification of this bioprocess, further improvements are desirable, particularly in the formation of the high-value platform chemicals such as 2,3-butanediol (2,3-BD). A new, experimentally parameterised genome-scale model of C. autoethanogenum predicts dramatically increased 2,3-BD production under non-carbon-limited conditions when thermodynamic constraints on hydrogen production are considered.
Highlights
The adverse environmental and societal consequences of continued fossil-fuel dependence represent arguably the defining challenge for scientific research in the 21st century [1, 2]
Autoethanogenum to grow on carbon monoxide (CO) is the Wood–Ljungdahl pathway (WLP) [7, 8]
Results obtained through the application of flux balance analysis (FBA) provide insight into the capabilities of a metabolic network, helping to investigate the steady-state behaviour of an organism
Summary
The adverse environmental and societal consequences of continued fossil-fuel dependence represent arguably the defining challenge for scientific research in the 21st century [1, 2]. The fundamental metabolic pathway enabling C. autoethanogenum to grow on CO is the Wood–Ljungdahl pathway (WLP) [7, 8]. Autoethanogenum to grow on CO is the Wood–Ljungdahl pathway (WLP) [7, 8] This ancient biochemical pathway is split into two ‘branches’: the methyl branch and the carbonyl branch [9]. The methyl branch proceeds by constructing a methyl group from carbon dioxide (CO2) via a series of biochemical conversions including an adenosine triphosphate (ATP)-consuming reaction [catalysed by formyl-tetrahydrofolate (THF) ligase, FtfL] and three redox reactions collectively requiring nicotinamide adenine dinucleotide (NADH), NAD phosphate (NADPH) and reduced ferredoxin (Fdred). The carbonyl branch is the reduction of CO2 to an enzyme-bound carbonyl group as catalysed by the acetyl-CoA synthase/CO dehydrogenase complex (ACS/CODH)
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