Conformational changes of cytochromes P-450cam and P-450lin induced by high pressure.
Absorbance and fluorescence spectra of bacterial cytochrome P-450cam and cytochrome P-450lin have been studied as a function of pressure. These pressure-induced spectral perturbations fall into two categories, which are interpreted as resulting from denaturation domains and are discussed in terms of protein structural dynamics. The results presented herein support a view that these two bacterial cytochromes have large structural differences and suggest a picture in which the gellike cortex of each protein may play an essential role in stability and function.
Hui Bon Hoa
G
G
INSERM-INRA, U310, Institut de Biologie Physico-Chimique, Paris, France.
Di Primo
C
C
Dondaine
I
I
Sligar
S G
SG
Gunsalus
I C
IC
Douzou
P
P
D002164:Camphor / Q000378:metabolism; D019475:Camphor 5-Monooxygenase; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D006874:Hydrostatic Pressure; D006899:Mixed Function Oxygenases / Q000378:metabolism*; D010088:Oxidoreductases / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D011489:Protein Denaturation; D011549:Pseudomonas / Q000378:metabolism; D013050:Spectrometry, Fluorescence; D013053:Spectrophotometry; D014364:Tryptophan
D002164:Camphor; D014364:Tryptophan; D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases; D010088:Oxidoreductases; C059620:linalool 8-monooxygenase; D019475:Camphor 5-Monooxygenase