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Q31039839-2FD3306A-C8FB-4E40-A2F9-24E83F089AAD
Q31039839-2FD3306A-C8FB-4E40-A2F9-24E83F089AAD
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http://www.wikidata.org/entity/statement/Q31039839-2FD3306A-C8FB-4E40-A2F9-24E83F089AAD
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.
P2860
Q31039839-2FD3306A-C8FB-4E40-A2F9-24E83F089AAD
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http://www.wikidata.org/entity/statement/Q31039839-2FD3306A-C8FB-4E40-A2F9-24E83F089AAD
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7e7d9355b79367ced1c60095f0ac122b82a0af02
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.