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.

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Role of propionates in substrate binding to heme oxygenase from Neisseria meningitidis: a nuclear magnetic resonance study Signaling function of heme oxygenase proteins.

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P2860

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.

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2011 nî lūn-bûn

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Influence of substrate modific ...... meningitidis. A 1H NMR study.

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Influence of substrate modific ...... meningitidis. A 1H NMR study.

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Influence of substrate modific ...... meningitidis. A 1H NMR study.

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Influence of substrate modific ...... meningitidis. A 1H NMR study.

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Influence of substrate modific ...... meningitidis. A 1H NMR study.

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Influence of substrate modific ...... meningitidis. A 1H NMR study.

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Influence of substrate modific ...... meningitidis. A 1H NMR study.

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Dungeng Peng

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Gerd N La Mar

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James D Satterlee

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Jerry L Dallas

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Li-Hua Ma

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Michihiko Sato

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Xuhong Zhang

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P2860

Crystal structure of heme oxygenase from the gram-negative pathogen Neisseria meningitidis and a comparison with mammalian heme oxygenase-1

Crystal structure of rat heme oxygenase-1 in complex with heme bound to azide. Implication for regiospecific hydroxylation of heme at the alpha-meso carbon

Crystal structures of the NO- and CO-bound heme oxygenase from Neisseriae meningitidis. Implications for O2 activation

Crystal structures of ferrous and CO-, CN(-)-, and NO-bound forms of rat heme oxygenase-1 (HO-1) in complex with heme: structural implications for discrimination between CO and O2 in HO-1

Crystal structure of the dioxygen-bound heme oxygenase from Corynebacterium diphtheriae: implications for heme oxygenase function

The binding sites on human heme oxygenase-1 for cytochrome p450 reductase and biliverdin reductase

Solution NMR characterization of an unusual distal H-bond network in the active site of the cyanide-inhibited, human heme oxygenase complex of the symmetric substrate, 2,4-dimethyldeuterohemin.

Solution 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.

1H NMR characterization of the solution active site structure of substrate-bound, cyanide-inhibited heme oxygenase from Neisseria meningitidis: comparison to crystal structures.

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10.1021/BI200978G

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Kevin M. Smith

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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.

about

P2860

P2860

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.

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