1H NMR study of the effect of variable ligand on heme oxygenase electronic and molecular structure.
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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.Role of propionates in substrate binding to heme oxygenase from Neisseria meningitidis: a nuclear magnetic resonance studyThe orbital ground state of the azide-substrate complex of human heme oxygenase is an indicator of distal H-bonding: implications for the enzyme mechanism.
P2860
1H NMR study of the effect of variable ligand on heme oxygenase electronic and molecular structure.
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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 05 September 2008
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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
1H NMR study of the effect of ...... ronic and molecular structure.
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1H NMR study of the effect of ...... ronic and molecular structure.
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label
1H NMR study of the effect of ...... ronic and molecular structure.
@en
1H NMR study of the effect of ...... ronic and molecular structure.
@nl
prefLabel
1H NMR study of the effect of ...... ronic and molecular structure.
@en
1H NMR study of the effect of ...... ronic and molecular structure.
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P2093
P2860
P1476
1H NMR study of the effect of ...... ronic and molecular structure.
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P2093
Gerd N La Mar
Tadashi Yoshida
Xuhong Zhang
Yangzhong Liu
P2860
P356
10.1016/J.JINORGBIO.2008.08.012
P577
2008-09-05T00:00:00Z