Reduction of dioxygen catalyzed by pyrene-wired heme domain cytochrome P450 BM3 electrodes.
We have electronically wired the cytochrome P450 BM3 heme domain to a graphite electrode with the use of a pyrene-terminated tether. AFM images clearly reveal that pyrene-wired enzyme molecules are adsorbed to the electrode surface. The enzyme-electrode system undergoes rapid and reversible electron transfer, displaying a standard rate constant higher than that of any other P450-electrode system. We also show that the graphite-pyrene-BM3 system catalyzes the four-electron reduction of dioxygen to water.
Udit
Andrew K
AK
Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA.
Hill
Michael G
MG
Bittner
V Garrett
VG
Arnold
Frances H
FH
Gray
Harry B
HB
D001426:Bacterial Proteins / Q000737:chemistry*; D015374:Biosensing Techniques / Q000379:methods; D002384:Catalysis; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry*; D004563:Electrochemistry / Q000379:methods; D006418:Heme / Q000737:chemistry*; D018625:Microscopy, Atomic Force; D006899:Mixed Function Oxygenases / Q000737:chemistry*; D009251:NADPH-Ferrihemoprotein Reductase; D010084:Oxidation-Reduction; D010100:Oxygen / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D011721:Pyrenes / Q000737:chemistry*
D001426:Bacterial Proteins; D011721:Pyrenes; D006418:Heme; D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases; D009251:NADPH-Ferrihemoprotein Reductase; C052423:flavocytochrome P450 BM3 monoxygenases; D010100:Oxygen