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Q35648424-03D7C415-8D54-495E-8BEC-8DD715A450F8
Q35648424-03D7C415-8D54-495E-8BEC-8DD715A450F8
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http://www.wikidata.org/entity/statement/Q35648424-03D7C415-8D54-495E-8BEC-8DD715A450F8
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
Q35648424-03D7C415-8D54-495E-8BEC-8DD715A450F8
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http://www.wikidata.org/entity/statement/Q35648424-03D7C415-8D54-495E-8BEC-8DD715A450F8
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69e54e48813ea03765d2def53d1bf4afada817a6
P2860
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