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Contzen,J., Ristau O., and C. Jung (1996)
Time-resolved
Fourier-transform infrared studies of the cytochrome P-450cam
carbonmonoxide complex bound with (1R)-camphor and (1S)-camphor
substrate.
FEBS Letters 383, 13-17.
The CO binding reaction of cytochrome P 450(cam) bound with (1R) camphor and (1S) camphor are compared in the temperature region of 210-260 K using time resolved Fourier transform infrared spectroscopy with the CO stretch vibration as spectroscopic probe. For (1S) camphor as substrate the association of CO is slowed down by a factor of 2, while the dissociation is accelerated by a factor of 3. The CO complex for the (1S)camphor bound P-450 is less stabilized (Delta G= 22 kJ/mol) compared to the natural substrate (1R) camphor (Delta G= 30 kJ/mol). The data are interpreted by a smaller change of the mobility of the (1S) camphor due to CO binding as compared to (1R) camphor, which would indicate a higher mobility of (1S)camphor already in the CO free reduced form of P 450(cam). The higher mobility of (1S) camphor in the heme pocket might explain the increased uncoupling rate (hydrogen peroxide formation) of 11% [Maryniak et al, (1993) Tetrahedron 49, 9373 9384] during the P 450(cam) catalyzed hydroxylation compared to 3% for the conversion of (1R) camphor.
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Wade et al. (1996) Fundamentals of Enzyme-Ligand Interactions in
Cytochrome P450cam
POPE5 Conference Proceedings
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