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Structure and chemistry of cytochrome P450.
This review will concentrate on findings with P-450cam of the Pseudomonas putida camphor-5-exo-hydroxylase, and attention will be drawn to parallel and contrasting examples from other P- 450s as appropriate.
Hydroxylation of camphor by reduced oxy-cytochrome P450cam: mechanistic implications of EPR and ENDOR studies of catalytic intermediates in native and mutant enzymes.
- R. Davydov, T. Makris, V. Kofman, D. Werst, S. Sligar, B. Hoffman
- ChemistryJournal of the American Chemical Society
- 30 January 2001
Chemical and EPR quantitations indicate the reaction pathway involving 5B yields 5-exo-hydroxycamphor quantitatively, and gamma-irradiation at cryogenic temperatures of the ternary complexes of camphor, dioxygen, and ferro-cytochrome P450cam uses EPR and ENDOR spectroscopies to characterize the primary product of reduction as well as subsequent states created by annealing reduced oxyP450.
Thirty years of microbial P450 monooxygenase research: peroxo-heme intermediates--the central bus station in heme oxygenase catalysis.
Resonance Raman characterization of the peroxo and hydroperoxo intermediates in cytochrome P450.
- I. Denisov, P. Mak, T. Makris, S. Sligar, J. Kincaid
- ChemistryThe journal of physical chemistry. A
- 18 December 2008
Experimental Resonance Raman studies of intermediates generated by cryoreduction of the oxyferrous complex of the D251N mutant of cytochrome P450(cam) (CYP101) are reported, showing that the nu(O-O) mode decreases from a superoxo-like frequency near approximately 1130 cm(-1) to 792 cm (-1) upon reduction.
Cytochrome p450 compound I.
Formation of the Compound I derivative of a P450 enzyme is reported by laser flash photolysis oxidation of the corresponding Compound II species, an iron(IV)-oxo neutral porphyrin intermediate.
MECHANISTIC ENZYMOLOGY OF OXYGEN ACTIVATION BY THE CYTOCHROMES P450
- T. Makris, R. Davydov, I. Denisov, B. Hoffman, S. Sligar
- Chemistry, BiologyDrug metabolism reviews
- 1 January 2002
The detailed mechanism of P450 dioxygen scission is discussed utilizing the CYP101 hydroxylation of camphor as a model system and a structural and spectroscopic analysis of the nature of critical intermediate states in the reaction is discussed.
Cyanobacterial aldehyde deformylase oxygenation of aldehydes yields n-1 aldehydes and alcohols in addition to alkanes.
It is shown that ADO also catalyzes incorporation of an oxygen atom from O2 into the alkane product to yield alcohol and aldehyde products, and the nature of the diiron cluster and the newly recognized products from ADO catalysis hold implications for the mechanism of C-C bond cleavage.
EPR and ENDOR of catalytic intermediates in cryoreduced native and mutant oxy-cytochromes P450cam: Mutation-induced changes in the proton delivery system 
Decarboxylation of fatty acids to terminal alkenes by cytochrome P450 compound I.
- Job L. Grant, Chun H. Hsieh, T. Makris
- Chemistry, BiologyJournal of the American Chemical Society
- 10 April 2015
Results indicate that the initial mechanism for alkene formation, which does not result from oxygen rebound, is similar to that widely suggested for P450 monooxygenation reactions.
Structural and Molecular Characterization of Iron-sensing Hemerythrin-like Domain within F-box and Leucine-rich Repeat Protein 5 (FBXL5)♦
The atomic structure of the FBXL5 N terminus is presented, a hemerythrin-like α-helical bundle fold not previously observed in mammalian proteins, which provides insights into the mechanisms by whichFBXL5 serves as a unique mammalian metabolic sensor.