In Azotobacter vinelandii Hydrogenase, Substitution of Serine for the Cysteine Residues at Positions 62, 65, 294, and 297 in the Small (HoxK) Subunit Affects H2 Oxidation
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=206646Documentos Relacionados
- In Azotobacter vinelandii hydrogenase, substitution of serine for the cysteine residues at positions 62, 65, 294, and 297 in the small (HoxK) subunit affects H2 oxidation [corrected]
- Substitution of Azotobacter vinelandii hydrogenase small-subunit cysteines by serines can create insensitivity to inhibition by O2 and preferentially damages H2 oxidation over H2 evolution.
- The Hydrogenase Cytochrome b Heme Ligands of Azotobacter vinelandii Are Required for Full H2 Oxidation Capability
- The hoxZ gene of the Azotobacter vinelandii hydrogenase operon is required for activation of hydrogenase.
- Nucleotide sequences and genetic analysis of hydrogen oxidation (hox) genes in Azotobacter vinelandii.