about
Crystal structure of the dioxygen-bound heme oxygenase from Corynebacterium diphtheriae: implications for heme oxygenase functionEnzymatic ring-opening mechanism of verdoheme by the heme oxygenase: a combined X-ray crystallography and QM/MM studyDistinct reaction pathways followed upon reduction of oxy-heme oxygenase and oxy-myoglobin as characterized by Mössbauer spectroscopy.Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexesA new way to degrade heme: the Mycobacterium tuberculosis enzyme MhuD catalyzes heme degradation without generating CO.Unique coupling of mono- and dioxygenase chemistries in a single active site promotes heme degradation.Structure and catalytic mechanism of heme oxygenase.Heme degradation by Staphylococcus aureus IsdG and IsdI liberates formaldehyde rather than carbon monoxide.Bach1, a heme-dependent transcription factor, reveals presence of multiple heme binding sites with distinct coordination structure.Crystallographic studies of heme oxygenase complexed with an unstable reaction intermediate, verdoheme.Heme regulates B-cell differentiation, antibody class switch, and heme oxygenase-1 expression in B cells as a ligand of Bach2.Heme binds to an intrinsically disordered region of Bach2 and alters its conformation.Characterization of a direct oxygen sensor heme protein from Escherichia coli. Effects of the heme redox states and mutations at the heme-binding site on catalysis and structure.Binding of oxygen and carbon monoxide to a heme-regulated phosphodiesterase from Escherichia coli. Kinetics and infrared spectra of the full-length wild-type enzyme, isolated PAS domain, and Met-95 mutants.Characterization of Met95 mutants of a heme-regulated phosphodiesterase from Escherichia coli. Optical absorption, magnetic circular dichroism, circular dichroism, and redox potentials.Mechanistic studies of the isomerization of peroxynitrite to nitrate catalyzed by distal histidine metmyoglobin mutants.Roles of distal Asp in heme oxygenase from Corynebacterium diphtheriae, HmuO: A water-driven oxygen activation mechanism.Proton transfer at helium temperatures during dioxygen activation by heme monooxygenases.O(2)- and H(2)O(2)-dependent verdoheme degradation by heme oxygenase: reaction mechanisms and potential physiological roles of the dual pathway degradation.Charge-state-distribution analysis of Bach2 intrinsically disordered heme binding region.Time-resolved small-angle X-ray scattering investigation of the folding dynamics of heme oxygenase: implication of the scaling relationship for the submillisecond intermediates of protein folding.Hydrogen sulfide bypasses the rate-limiting oxygen activation of heme oxygenaseKinetic isotope effects on the rate-limiting step of heme oxygenase catalysis indicate concerted proton transfer/heme hydroxylationLigand design for the improvement of stability of metal complex.protein hybridsA heme degradation enzyme, HutZ, from Vibrio choleraeLight-Wavelength-Based Quantitative Control of Dihydrofolate Reductase Activity by Using a Photochromic Isostere of an Inhibitor
P50
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P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Toshitaka Matsui
@ast
Toshitaka Matsui
@en
Toshitaka Matsui
@es
Toshitaka Matsui
@nl
Toshitaka Matsui
@sl
type
label
Toshitaka Matsui
@ast
Toshitaka Matsui
@en
Toshitaka Matsui
@es
Toshitaka Matsui
@nl
Toshitaka Matsui
@sl
prefLabel
Toshitaka Matsui
@ast
Toshitaka Matsui
@en
Toshitaka Matsui
@es
Toshitaka Matsui
@nl
Toshitaka Matsui
@sl
P106
P31
P496
0000-0003-3865-8468