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Reduction of Dioxygen Catalyzed by Pyrene-Wired Heme Domain Cytochrome P450 BM3 Electrodes
 

Summary: Reduction of Dioxygen Catalyzed by Pyrene-Wired Heme Domain Cytochrome
P450 BM3 Electrodes
Andrew K. Udit, Michael G. Hill, V. Garrett Bittner, Frances H. Arnold, and Harry B. Gray*,
DiVision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California 91125,
and Department of Chemistry, Occidental College, Los Angeles, California 90041
Received June 7, 2004; E-mail: hbgray@caltech.edu
Cytochromes P450 (P450s) catalyze oxygenations of inert
substrates under physiological conditions.1 Exploiting this activity
in vitro would be greatly facilitated if reductants other than NADPH
could be found. While an electrode is perhaps the most attractive
source of electrons, direct electrochemistry of P450 has been
elusive, owing to poor electronic coupling to the deeply buried heme
and inactivation through surface adsorption. Investigations of
electrochemical reduction of P450 have led to clever techniques
for effecting electron transfer (ET). These methods include confin-
ing the protein within surfactant2,3 or polyelectrolyte4,5 films,
modifying the electrode surface covalently (mercaptans on gold6)
or through adsorption (clay on carbon7) and modifying the enzyme
with molecular electronic relays.8
We are working on electrochemical methods for reduction of

  

Source: Arnold, Frances H. - Division of Chemistry and Chemical Engineering, California Institute of Technology

 

Collections: Chemistry; Biology and Medicine