Solution 1H NMR of the active site of substrate-bound, cyanide-inhibited human heme oxygenase. comparison to the crystal structure of the water-ligated form.

Solution 1H NMR of the active site of substrate-bound, cyanide-inhibited human heme oxygenase. comparison to the crystal structure of the water-ligated form.

Item
http://www.wikidata.org/entity/Q30647375
Comparison of the heme-free and -bound crystal structures of human heme oxygenase-1Solution 1H NMR investigation of the active site molecular and electronic structures of substrate-bound, cyanide-inhibited HmuO, a bacterial heme oxygenase from Corynebacterium diphtheriae.1H NMR investigation of the solution structure of substrate-free human heme oxygenase: comparison to the cyanide-inhibited, substrate-bound complex.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.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.Systematic comparison of crystal and NMR protein structures deposited in the protein data bank.Identification of ligand binding sites of proteins using the Gaussian Network Model.Investigations of ferric heme cyanide photodissociation in myoglobin and horseradish peroxidase.Alteration 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.Small molecule antivirulents targeting the iron-regulated heme oxygenase (HemO) of P. aeruginosa.Function Coupling Mechanism of PhuS and HemO in Heme Degradation.
P2860

Solution 1H NMR of the active site of substrate-bound, cyanide-inhibited human heme oxygenase. comparison to the crystal structure of the water-ligated form.

Item
http://www.wikidata.org/entity/Q30647375
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
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2001年学术文章
@wuu
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
name
Solution 1H NMR of the active ...... ure of the water-ligated form.
@ast
Solution 1H NMR of the active ...... ure of the water-ligated form.
@en
type
label
Solution 1H NMR of the active ...... ure of the water-ligated form.
@ast
Solution 1H NMR of the active ...... ure of the water-ligated form.
@en
prefLabel
Solution 1H NMR of the active ...... ure of the water-ligated form.
@ast
Solution 1H NMR of the active ...... ure of the water-ligated form.
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P356
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P433
P478
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P921
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P1433
P1476
Solution 1H NMR of the active ...... ure of the water-ligated form.
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P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P698
P921