Active intermediates in heme monooxygenase reactions as revealed by cryoreduction/annealing, EPR/ENDOR studies.
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1H-ENDOR evidence for a hydrogen-bonding interaction that modulates the reactivity of a nonheme Fe(IV)═O unit.Compound I is the reactive intermediate in the first monooxygenation step during conversion of cholesterol to pregnenolone by cytochrome P450scc: EPR/ENDOR/cryoreduction/annealing studies.Unveiling the crucial intermediates in androgen production.Evidence That Compound I Is the Active Species in Both the Hydroxylase and Lyase Steps by Which P450scc Converts Cholesterol to Pregnenolone: EPR/ENDOR/Cryoreduction/Annealing StudiesComparison of the Mechanisms of Heme Hydroxylation by Heme Oxygenases-1 and -2: Kinetic and Cryoreduction StudiesSpectroscopic and Crystallographic Evidence for the Role of a Water-Containing H-Bond Network in Oxidase Activity of an Engineered Myoglobin.The use of deuterated camphor as a substrate in (1)H ENDOR studies of hydroxylation by cryoreduced oxy P450cam provides new evidence of the involvement of compound IUsing Biosynthetic Models of Heme-Copper Oxidase and Nitric Oxide Reductase in Myoglobin to Elucidate Structural Features Responsible for Enzymatic Activities.Nanodiscs in Membrane Biochemistry and Biophysics.Heteroatom-Heteroatom Bond Formation in Natural Product Biosynthesis.Spectroscopic studies of the cytochrome P450 reaction mechanisms.Role of the Proximal Cysteine Hydrogen Bonding Interaction in Cytochrome P450 2B4 Studied by Cryoreduction, Electron Paramagnetic Resonance, and Electron-Nuclear Double Resonance Spectroscopy.Spectroscopic and Kinetic Evidence for the Crucial Role of Compound 0 in the P450cam -Catalyzed Hydroxylation of Camphor by Hydrogen Peroxide.Organometallic Complex Formed by an Unconventional Radical S-Adenosylmethionine Enzyme.Exploring Electron/Proton Transfer and Conformational Changes in the Nitrogenase MoFe Protein and FeMo-cofactor Through Cryoreduction/EPR Measurements.Exploiting the Symmetry of the Resonator Mode to Enhance PELDOR SensitivityElectron paramagnetic resonance and electron-nuclear double resonance studies of the reactions of cryogenerated hydroperoxoferric-hemoprotein intermediates.Identification of a key catalytic intermediate demonstrates that nitrogenase is activated by the reversible exchange of N₂ for H₂.Enzymatic and cryoreduction EPR studies of the hydroxylation of methylated N(ω)-hydroxy-L-arginine analogues by nitric oxide synthase from Geobacillus stearothermophilus.Oxygen Activation and Radical Transformations in Heme Proteins and Metalloporphyrins.EPR/ENDOR and Theoretical Study of the Jahn-Teller-Active [HIPTN3N]MoVL Complexes (L = N-, NH).
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Active intermediates in heme monooxygenase reactions as revealed by cryoreduction/annealing, EPR/ENDOR studies.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 18 September 2010
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Active intermediates in heme m ...... /annealing, EPR/ENDOR studies.
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Active intermediates in heme m ...... /annealing, EPR/ENDOR studies.
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type
label
Active intermediates in heme m ...... /annealing, EPR/ENDOR studies.
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Active intermediates in heme m ...... /annealing, EPR/ENDOR studies.
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prefLabel
Active intermediates in heme m ...... /annealing, EPR/ENDOR studies.
@en
Active intermediates in heme m ...... /annealing, EPR/ENDOR studies.
@nl
P2860
P1476
Active intermediates in heme m ...... /annealing, EPR/ENDOR studies.
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P2093
Brian M Hoffman
Roman Davydov
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P356
10.1016/J.ABB.2010.09.013
P407
P577
2010-09-18T00:00:00Z