Tris(2,2'-bipyridyl)ruthenium(II)-mediated photoinduced electron transfer of engineered cytochrome P450 1A2.
In this study, it is shown that an electron from photoreduced tris(2,2'-bipyridyl)Ru2+ ion reaches the haem iron of engineered wild-type cytochrome P450 1A2 (P450 1A2) with an electron transfer rate of 6.04 x 10(-3) min(-1). The electron transfer rate, 4.05 x 10(-2) min(-1), of a His163Glu mutant, which has a redox potential 40 mV lower than that of the wild type, is more than sixfold faster than that of the wild type. The photoinduced electron transfer rates of the present system are strongly influenced by detergents, cholic acid and Emulgen 913. We discuss the intermolecular and intramolecular electron transfer mechanism of the P450 1A2 system based on the kinetic data.
Nakano
R
R
Institute for Chemical Reaction Science, Tohoku University, Sendai, Japan.
Sato
H
H
Shimizu
T
T
D015082:2,2'-Dipyridyl / Q000031:analogs & derivatives* / Q000494:pharmacology; D056831:Coordination Complexes; D019388:Cytochrome P-450 CYP1A2; D003577:Cytochrome P-450 Enzyme System / Q000187:drug effects / Q000378:metabolism* / Q000528:radiation effects; D004579:Electron Transport / Q000187:drug effects / Q000528:radiation effects; D018698:Glutamic Acid; D006639:Histidine; D007700:Kinetics; D008027:Light; D016297:Mutagenesis, Site-Directed; D010088:Oxidoreductases / Q000187:drug effects / Q000378:metabolism* / Q000528:radiation effects; D017319:Photosensitizing Agents / Q000494:pharmacology*; D015202:Protein Engineering; D011994:Recombinant Proteins / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D013053:Spectrophotometry; D017975:Ruthenium Compounds
D015082:2,2'-Dipyridyl; D056831:Coordination Complexes; D019388:Cytochrome P-450 CYP1A2; D003577:Cytochrome P-450 Enzyme System; D018698:Glutamic Acid; D006639:Histidine; D010088:Oxidoreductases; D017319:Photosensitizing Agents; D011994:Recombinant Proteins; C547232:tris(2,2-bipyridine)-ruthenium(II); D017975:Ruthenium Compounds