PMID: 2296Jan 20, 1976

Cytochrome P450cam and its complexes. Mössbauer parameters of the heme iron

Biochimica Et Biophysica Acta
M SharrockI C Gunsalus

Abstract

Mössbauer spectroscopy has been used to study the heme iron in various states of cytochrome P450cam from the camphor-hydroxylating system of the bacterium Pseudomonas putida. Native, camphor-free P450cam contains low-spin ferric iron, part of which (approx. 50-70%) is converted to the high-spin ferric state upon addition of camphor. The Mössbauer spectra of the camphor-free enzyme (S equals 1/2) and of the high-spin component (S equals 5/2) of the camphor complex have been successfully simulated using a model based on crystal-field theory and simple convalency considerations. The native low-spin ferric state of P450cam forms a complex with 2-phenylimidazole, with small changes in the g values and Mössbauer spectra. These changes can be accounted for consistently in the crystal-field model referred to above. The addition of putidaredoxin to the camphor-complexed, oxidized P450cam decreases the intensity of the high-spin component and changes its quadrupole splitting. The reduced form of P450cam contrins high-spin ferrous iron, both in the presence and absence of camphor. The complex of reduced P450cam with molecular oxygen is diamagnetic and has a combination of quadrupole splitting and isomer shift that is unusual for a ferrous...Continue Reading

References

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Citations

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Related Concepts

Cytochrome P-450 Oxygenase
Heme
Hydrogen-Ion Concentration
Iron
Mathematics
Oxidation-Reduction
Plasma Protein Binding Capacity
Protein Conformation
Pseudomonas
Spectrometry

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