Structural Changes in Cytochrome P-450cam Effected by the Binding of the Enantiomers (1R)-Camphor and (1S)-Camphor-Reference-Cited by-同舟云学术

Structural Changes in Cytochrome P-450cam Effected by the Binding of the Enantiomers (1R)-Camphor and (1S)-Camphor

Published:1996-01-01 Issue:45 Volume:35 Page:14127-14138
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Schulze Heike¹,Hui Bon Hoa Gaston¹,Helms Volkhard¹,Wade Rebecca C.¹,Jung Christiane¹

Affiliation:

1. MDC, Max-Delbrück-Centrum für Molekulare Medizin Berlin-Buch, Robert-Rössle-Strasse 10, 13122 Berlin, Germany, INSERM-U310, Institut de Biologie Physico-Chimique, 13 rue P. et M. Curie, 75005 Paris, France, and European Molecular Biology Laboratory Heidelberg, Meyerhofstrasse 1, 69012 Heidelberg, Germany

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi9527303

Reference74 articles.

1. The roles of active site hydrogen bonding in cytochrome P-450cam as revealed by site-directed mutagenesis.

2. Molecular recognition in cytochrome P-450: alteration of regioselective alkane hydroxylation via protein engineering

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

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