Proximal cysteine residue is essential for the enzymatic activities of cytochrome P450cam.
about
Probing the role of the proximal heme ligand in cytochrome P450cam by recombinant incorporation of selenocysteineVariations on a (t)heme--novel mechanisms, redox partners and catalytic functions in the cytochrome P450 superfamilyRedox and chemical activities of the hemes in the sulfur oxidation pathway enzyme SoxAXStructural Adaptability Facilitates Histidine Heme Ligation in a Cytochrome P450.Monooxygenation of an aromatic ring by F43W/H64D/V68I myoglobin mutant and hydrogen peroxide. Myoglobin mutants as a model for P450 hydroxylation chemistry.Calculated and experimental spin state of seleno cytochrome P450.Elucidating the role of the proximal cysteine hydrogen-bonding network in ferric cytochrome P450cam and corresponding mutants using magnetic circular dichroism spectroscopy.A novel intermediate in the reaction of seleno CYP119 with m-chloroperbenzoic acidNon-natural olefin cyclopropanation catalyzed by diverse cytochrome P450s and other hemoproteins.Probing the origins of aromatase inhibitory activity of disubstituted coumarins via QSAR and molecular dockingRapid kinetic methods to dissect steroidogenic cytochrome P450 reaction mechanisms.Molecular basis for the inability of an oxygen atom donor ligand to replace the natural sulfur donor heme axial ligand in cytochrome P450 catalysis. Spectroscopic characterization of the Cys436Ser CYP2B4 mutantSolution NMR structure of putidaredoxin-cytochrome P450cam complex via a combined residual dipolar coupling-spin labeling approach suggests a role for Trp106 of putidaredoxin in complex formation.NMR study on the structural changes of cytochrome P450cam upon the complex formation with putidaredoxin. Functional significance of the putidaredoxin-induced structural changes.PpoC from Aspergillus nidulans is a fusion protein with only one active haem.Identification of crucial histidines for heme binding in the N-terminal domain of the heme-regulated eIF2alpha kinase.Refolding processes of cytochrome P450cam from ferric and ferrous acid forms to the native conformation. Formations of folding intermediates with non-native heme coordination state.L358P mutation on cytochrome P450cam simulates structural changes upon putidaredoxin binding: the structural changes trigger electron transfer to oxy-P450cam from electron donors.Structure and redox properties of the haem centre in the C357M mutant of cytochrome P450cam.Characterization of a selenocysteine-ligated P450 compound I reveals direct link between electron donation and reactivity.
P2860
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P2860
Proximal cysteine residue is essential for the enzymatic activities of cytochrome P450cam.
description
2001 nî lūn-bûn
@nan
2001 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Proximal cysteine residue is e ...... ivities of cytochrome P450cam.
@ast
Proximal cysteine residue is e ...... ivities of cytochrome P450cam.
@en
type
label
Proximal cysteine residue is e ...... ivities of cytochrome P450cam.
@ast
Proximal cysteine residue is e ...... ivities of cytochrome P450cam.
@en
prefLabel
Proximal cysteine residue is e ...... ivities of cytochrome P450cam.
@ast
Proximal cysteine residue is e ...... ivities of cytochrome P450cam.
@en
P2093
P2860
P1433
P1476
Proximal cysteine residue is essential for the enzymatic activities of cytochrome P450cam
@en
P2093
P2860
P304
P356
10.1046/J.1432-1033.2001.01872.X
P407
P577
2001-01-01T00:00:00Z