Time-resolved Fourier-transform infrared studies of the cytochrome P-450cam carbonmonoxide complex bound with (1R)-camphor and (1S)-camphor substrate.

Abstract:

:The CO-binding reaction of cytochrome P-450cam 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 (deltaG=-22 kJ/mol) compared to the natural substrate (1R)-camphor (deltaG=-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-450cam. 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-450cam catalyzed hydroxylation compared to 3% for the conversion of (1R)-camphor.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Contzen J,Ristau O,Jung C

doi

10.1016/0014-5793(96)00103-2

subject

Has Abstract

pub_date

1996-03-25 00:00:00

pages

13-7

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(96)00103-2

journal_volume

383

pub_type

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