Journal
CHEMICAL COMMUNICATIONS
Volume 52, Issue 58, Pages 9133-9136Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c6cc00515b
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Funding
- Wellcome Trust through Combating Infectious Disease: Computational Approaches in Translational Science CDT program [CIDCATS WT095024MA]
- Royal Society Research Grant Award [RG2014R2]
- [EP/M024393/1]
- [EP/M506394/1]
- EPSRC [EP/M024393/1] Funding Source: UKRI
- Engineering and Physical Sciences Research Council [1499224, EP/M024393/1] Funding Source: researchfish
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Naturally occurring oxygen tolerant NiFe membrane bound hydrogenases have a conserved catalytic bias towards hydrogen oxidation which limits their technological value. We present an Escherichia coli Hyd-1 amino acid exchange that apparently causes the catalytic rate of H-2 production to double but does not impact the O-2 tolerance.
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