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Q35648424-2D5646A0-E731-47EF-8798-C2A2EE4EDF09
Q35648424-2D5646A0-E731-47EF-8798-C2A2EE4EDF09
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http://www.wikidata.org/entity/statement/Q35648424-2D5646A0-E731-47EF-8798-C2A2EE4EDF09
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.
P2860
Q35648424-2D5646A0-E731-47EF-8798-C2A2EE4EDF09
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http://www.wikidata.org/entity/statement/Q35648424-2D5646A0-E731-47EF-8798-C2A2EE4EDF09
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69e54e48813ea03765d2def53d1bf4afada817a6
P2860
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.