Effect of redox potential of the heme on the peroxidase activity of cytochrome b562.
Measurements of peroxidase activities of two site-specific mutants and wild type cytochrome b562 suggest that the enzymatic activity correlates with the redox potential of the metal center. A lower value of the Fe(3+)/Fe(2+) redox potential seems to be important for promoting peroxidase activity of the hemeprotein possibly by stabilization of the high-valent redox intermediate involved in the catalytic function. The results provide an approach towards rational tuning of enzyme function when 'grafted' into a new protein environment.
D002384:Catalysis; D003573:Cytochrome b Group / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004563:Electrochemistry; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006418:Heme / Q000737:chemistry*; D006420:Hemeproteins / Q000737:chemistry / Q000378:metabolism; D016297:Mutagenesis, Site-Directed; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000378:metabolism; D013329:Structure-Activity Relationship
D003573:Cytochrome b Group; D029968:Escherichia coli Proteins; D006420:Hemeproteins; D006418:Heme; C017850:cytochrome b562, E coli; D010544:Peroxidases