Mechanism of hydrogen activation by [NiFe] hydrogenases

[NiFe] hydrogenases contain a conserved arginine (R509) that is suspended over the Ni and Fe atoms. Biochemical, crystallographic and electrochemical analysis of an R509K mutant reveal >100-fold lower oxidation activity despite the maintenance of structural integrity. The active site of [NiFe] hy...

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Veröffentlicht in:	Nature chemical biology 2016-01, Vol.12 (1), p.46-50
Hauptverfasser:	Evans, Rhiannon M, Brooke, Emily J, Wehlin, Sara A M, Nomerotskaia, Elena, Sargent, Frank, Carr, Stephen B, Phillips, Simon E V, Armstrong, Fraser A
Format:	Artikel
Sprache:	eng
Schlagworte:	631/1647/2258/1266 631/57 631/92/173 631/92/607 82/80 82/83 Alanine - chemistry Alanine - genetics Amino Acid Substitution Asparagine - chemistry Asparagine - genetics Biochemical Engineering Biochemistry Bioorganic Chemistry Cell Biology Chemistry Chemistry/Food Science Crystallography, X-Ray E coli Escherichia coli Proteins - chemistry Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism Guanidine - chemistry Hydrogen - metabolism Hydrogenase - chemistry Hydrogenase - genetics Hydrogenase - metabolism Iron - chemistry Lysine - chemistry Lysine - genetics Mutation Nickel Nickel - chemistry Protein Conformation
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