Construction and characterization of bioelectrocatalytic sensors based on cytochromes P450.
Semisynthetic flavocytochromes RfP450 1A2, RfP450 2B4 and RfP450scc--molecular conjugates of protein with riboflavin--could be reduced on rhodium-graphite screen-printed thick film electrodes as was confirmed by cyclic voltammograms of immobilized enzymes. Amperometric enzyme electrodes for direct measurement of organic pollutants were developed. The efficiency of controlled potential electrolysis for the reduction of flavocytochromes P450 was comparable with traditional reduction by pyridine nucleotides. The rate constants for substrates conversion obtained by electrochemical methods were close to those obtained using NAD(P)H as an electron source.
Shumyantseva
V V
VV
Institute of Biomedical Chemistry, Pogodinskaya St. 10, 119992, Moscow, Russia. victoria@ibmh.msk.su
Bulko
T V
TV
Usanov
S A
SA
Schmid
R D
RD
Nicolini
C
C
Archakov
A I
AI
D000632:Aminopyrine / Q000032:analysis; D001426:Bacterial Proteins; D015374:Biosensing Techniques / Q000295:instrumentation*; D002784:Cholesterol / Q000032:analysis; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry*; D004566:Electrodes; D004800:Enzymes, Immobilized; D007527:Isoenzymes / Q000737:chemistry; D006899:Mixed Function Oxygenases / Q000737:chemistry; D009251:NADPH-Ferrihemoprotein Reductase; D010084:Oxidation-Reduction
D001426:Bacterial Proteins; D004800:Enzymes, Immobilized; D007527:Isoenzymes; D000632:Aminopyrine; D003577:Cytochrome P-450 Enzyme System; D002784:Cholesterol; D006899:Mixed Function Oxygenases; D009251:NADPH-Ferrihemoprotein Reductase; C052423:flavocytochrome P450 BM3 monoxygenases