Open AccessProton Magnetic Resonance Reveals High-Spin Iron (II) in Ferrous Cytochrome P450 cam from Pseudomonas putida
Author(s) -
Regula M. Keller,
Kurt Wüthrich,
Peter G. Debrunner
Publication year - 1972
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.69.8.2073
Subject(s) - ferrous , ferric , pseudomonas putida , chemistry , hemeprotein , heme , resonance (particle physics) , carbon monoxide , nuclear magnetic resonance , cyanide , inorganic chemistry , crystallography , biochemistry , organic chemistry , atomic physics , physics , enzyme , catalysis
High-resolution proton nuclear magnetic resonance spectra were studied in D(+)-camphor-saturated solutions of ferric and ferrous cytochrome P450cam fromPseudomonas putida , and of the cyanide complex of ferric P450cam . In all these compounds several hyperfineshifted resonances of the heme group could be detected. In the ferrous protein, these resonance lines, which exhibit a Curie-type temperature dependence in the range of 5-28°, indicate the presence of high-spin iron (II). It is suggested that the iron (II) in ferrous P450cam might be pentacoordinated, as in other hemoproteins that can reversibly bind molecular oxygen and carbon monoxide.