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Protein-Surfactant Film Voltammetry of Wild-Type and Mutant Cytochrome P450 BM3
 

Summary: Protein-Surfactant Film Voltammetry of Wild-Type and Mutant
Cytochrome P450 BM3
Andrew K. Udit,
Nareen Hindoyan,
Michael G. Hill,
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 November 17, 2004
We are investigating the redox chemistry of wild-type (WT) and
mutant (1-12G) cytochrome P450 BM3. Absorption spectra in
solution feature the FeIII
Soret at 418 nm for WT and a split Soret
for 1-12G at 390 and 418 nm. Voltammetry of the proteins within
DDAPSS films on the surface of carbon electrodes reveal nearly
identical FeIII/II
potentials (approximately -200 mV vs Ag/AgCl),
but significant differences in k, 250 vs 30 s-1

  

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

 

Collections: Chemistry; Biology and Medicine