Functional differences between peroxidase compound I and the cytochrome P-450 reactive oxygen intermediate.
Open Access
- 1 August 1983
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 258 (15) , 9153-9158
- https://doi.org/10.1016/s0021-9258(17)44644-8
Abstract
No abstract availableThis publication has 15 references indexed in Scilit:
- The detection of two electron paramagnetic resonance radical signals associated with chloroperoxidase compound I.Journal of Biological Chemistry, 1982
- Spectroscopic investigations of ferric cytochrome P-450-CAM ligand complexes. Identification of the ligand trans to cysteinate in the native enzyme.Journal of Biological Chemistry, 1982
- Stereochemistry and deuterium isotope effects in camphor hydroxylation by the cytochrome P450cam monooxygenase systemBiochemistry, 1982
- Oxygen-17 ENDOR of horseradish peroxidase compound IJournal of the American Chemical Society, 1981
- Oxygen Activation by Cytochrome P-4501Annual Review of Biochemistry, 1980
- Properties of NADPH-cytochrome P-450 reductase purified from rabbit liver microsomesArchives of Biochemistry and Biophysics, 1979
- Studies of the ferric forms of cytochrome P-450 and chloroperoxidase by extended x-ray absotption fine structure. Characterization of the iron-nitrogen and iron-sulfur distancesJournal of the American Chemical Society, 1978
- [10] Two forms of liver microsomal cytochrome P-450, P-450lm2 and P-450lm4 (rabbit liver)Published by Elsevier ,1978
- Effect of mixed solvents on the formation of horseradish peroxidase compound I. The importance of diffusion-controlled reactionsBiochemistry, 1977
- Spectral evidence for the structure of three flavanotropolones related to theaflavin, an orange-red pigment of black teaCanadian Journal of Chemistry, 1967