Crystal structure of the dioxygen-bound heme oxygenase from Corynebacterium diphtheriae: implications for heme oxygenase function
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Involvement of NADPH in the interaction between heme oxygenase-1 and cytochrome P450 reductaseMolecular insights into substrate recognition and catalysis by tryptophan 2,3-dioxygenaseRuffling of Metalloporphyrins Bound to IsdG and IsdI, Two Heme-degrading Enzymes in Staphylococcus aureusThe IsdG-family of haem oxygenases degrades haem to a novel chromophoreDiscrimination between CO and O 2 in Heme Oxygenase: Comparison of Static Structures and Dynamic Conformation Changes following CO PhotolysisStaphylococcus aureus IsdG and IsdI, heme-degrading enzymes with structural similarity to monooxygenases.Distinct reaction pathways followed upon reduction of oxy-heme oxygenase and oxy-myoglobin as characterized by Mössbauer spectroscopy.Modulation of the axial water hydrogen-bonding properties by chemical modification of the substrate in resting state, substrate-bound heme oxygenase from Neisseria meningitidis; coupling to the distal H-bond network via ordered water molecules.Characterization of the spontaneous "aging" of the heme oxygenase from the pathological bacterium Neisseria meningitidis via cleavage of the C-terminus in contact with the substrate. Implications for functional studies and the crystal structure.1H NMR study of the magnetic properties and electronic structure of the hydroxide complex of substrate-bound heme oxygenase from Neisseria meningitidis: influence of the axial water deprotonation on the distal H-bond network.Diatomic ligand discrimination by the heme oxygenases from Neisseria meningitidis and Pseudomonas aeruginosa.The effects of hydrogen bonds on metal-mediated O2 activation and related processesInteractions of multiple gas-transducing systems: hallmarks and uncertainties of CO, NO, and H2S gas biology.Formation of the iron-oxo hydroxylating species in the catalytic cycle of aromatic amino acid hydroxylases.Overcoming the heme paradox: heme toxicity and tolerance in bacterial pathogens.Heme enzyme structure and function.Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexesStaphylococcus lugdunensis IsdG liberates iron from host heme.Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis. A 1H NMR study.Carbon monoxide: impact on remethylation/transsulfuration metabolism and its pathophysiologic implicationsRole of propionates in substrate binding to heme oxygenase from Neisseria meningitidis: a nuclear magnetic resonance studyAlteration of the regiospecificity of human heme oxygenase-1 by unseating of the heme but not disruption of the distal hydrogen bonding networkThe orbital ground state of the azide-substrate complex of human heme oxygenase is an indicator of distal H-bonding: implications for the enzyme mechanism.1H NMR study of the effect of variable ligand on heme oxygenase electronic and molecular structure.Structures of the substrate-free and product-bound forms of HmuO, a heme oxygenase from corynebacterium diphtheriae: x-ray crystallography and molecular dynamics investigation.A selective stepwise heme oxygenase model system: an iron(IV)-oxo porphyrin π-cation radical leads to a verdoheme-type compound via an isoporphyrin intermediate.Direct visualization of a Fe(IV)-OH intermediate in a heme enzyme.Apo-bacteriophytochromes modulate bacterial photosynthesis in response to low lightSpectroscopic features of cytochrome P450 reaction intermediatesSpectroscopic studies of the cytochrome P450 reaction mechanisms.Heme utilization by pathogenic bacteria: not all pathways lead to biliverdin.Substrate-protein interaction in human tryptophan dioxygenase: the critical role of H76.Cryoradiolytic reduction of heme proteins: Maximizing dose dependent yield.Regiospecificity determinants of human heme oxygenase: differential NADPH- and ascorbate-dependent heme cleavage by the R183E mutant.Roles of distal Asp in heme oxygenase from Corynebacterium diphtheriae, HmuO: A water-driven oxygen activation mechanism.O(2)- and H(2)O(2)-dependent verdoheme degradation by heme oxygenase: reaction mechanisms and potential physiological roles of the dual pathway degradation.Cryoradiolysis as a Method for Mechanistic Studies in Inorganic BiochemistryWhat can molecular modelling bring to the design of artificial inorganic cofactors?
P2860
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P2860
Crystal structure of the dioxygen-bound heme oxygenase from Corynebacterium diphtheriae: implications for heme oxygenase function
description
2004 nî lūn-bûn
@nan
2004 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Crystal structure of the dioxy ...... ns for heme oxygenase function
@ast
Crystal structure of the dioxy ...... ns for heme oxygenase function
@en
Crystal structure of the dioxy ...... ns for heme oxygenase function
@nl
type
label
Crystal structure of the dioxy ...... ns for heme oxygenase function
@ast
Crystal structure of the dioxy ...... ns for heme oxygenase function
@en
Crystal structure of the dioxy ...... ns for heme oxygenase function
@nl
prefLabel
Crystal structure of the dioxy ...... ns for heme oxygenase function
@ast
Crystal structure of the dioxy ...... ns for heme oxygenase function
@en
Crystal structure of the dioxy ...... ns for heme oxygenase function
@nl
P2093
P2860
P50
P356
P1476
Crystal structure of the dioxy ...... ns for heme oxygenase function
@en
P2093
Denis L Rousseau
Grace C Chu
Masaki Unno
Masao Ikeda-Saito
Tadashi Yoshida
P2860
P304
P356
10.1074/JBC.M400491200
P407
P577
2004-05-14T00:00:00Z