Premium
On the Origin of the Low‐Spin Character of Cytochrome P450 cam in the Resting State—Investigations of Enzyme Models with Pulse EPR and ENDOR Spectroscopy
Author(s) -
Aissaoui Hamed,
Bachmann Rainer,
Schweiger Arthur,
Woggon WolfDietrich
Publication year - 1998
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/(sici)1521-3773(19981116)37:21<2998::aid-anie2998>3.0.co;2-p
Subject(s) - electron paramagnetic resonance , chemistry , character (mathematics) , cytochrome , spin (aerodynamics) , spectroscopy , enzyme , spin states , spectral line , cytochrome p450 , crystallography , nuclear magnetic resonance , stereochemistry , physics , inorganic chemistry , biochemistry , astronomy , geometry , mathematics , quantum mechanics , thermodynamics
The P450 enzyme model 1 is a high‐spin system. EPR and ENDOR spectra reveal the coordination of water to the Fe III center. This is the first experimental proof that coordination of water is not the single determining factor in the stabilization of the low‐spin character of the cytochrome P450 resting state.