Biological H production has potential to address energy security and environmental concerns if produced from renewable or waste sources. The purple non-sulfur photosynthetic bacterium Rubrivivax gelatinosus CBS produces H while oxidizing CO, a component of synthesis gas (Syngas). CO-linked H production is facilitated by an energy-converting hydrogenase (Ech), while a subsequent H oxidation reaction is catalyzed by a membrane-bound hydrogenase (MBH). Both hydrogenases contain [NiFe] active sites requiring 6 maturation factors (HypA-F) for assembly, but it is unclear which of the two annotated sets of hyp genes are required for each in R. gelatinosus CBS. Herein, we report correlated expression of hyp1 genes with Ech genes and hyp2 expression with MBH genes. Moreover, we find that while Ech H evolving activity is only delayed when hyp1 is deleted, hyp2 deletion completely disrupts MBH H uptake, providing a platform for a biologically driven water-gas shift reaction to produce H from CO.
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Inactivation of the uptake hydrogenase in the purple non-sulfur photosynthetic bacterium Rubrivivax gelatinosus CBS enables a biological water-gas shift platform for H production.
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Biosciences Center, National Renewable Energy Laboratory, Golden, CO, USA.
Biological H production has potential to address energy security and environmental concerns if produced from renewable or waste sources. The purple non-sulfur photosynthetic bacterium Rubrivivax gelatinosus CBS produces H while oxidizing CO, a component of synthesis gas (Syngas). CO-linked H production is facilitated by an energy-converting hydrogenase (Ech), while a subsequent H oxidation reaction is catalyzed by a membrane-bound hydrogenase (MBH).
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We report here the sequencing and analysis of the genome of the purple non-sulfur photosynthetic bacterium Rubrivivax gelatinosus CBS. This microbe is a model for studies of its carboxydotrophic life style under anaerobic condition, based on its ability to utilize carbon monoxide (CO) as the sole carbon substrate and water as the electron acceptor, yielding CO2 and H2 as the end products. The CO-oxidation reaction is known to be catalyzed by two enzyme complexes, the CO dehydrogenase and hydrogenase.
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