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Q30754996-E0698B5D-AC1A-4344-9964-67BC7DF0CEC6
Q30754996-E0698B5D-AC1A-4344-9964-67BC7DF0CEC6
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http://www.wikidata.org/entity/statement/Q30754996-E0698B5D-AC1A-4344-9964-67BC7DF0CEC6
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.
P2860
Q30754996-E0698B5D-AC1A-4344-9964-67BC7DF0CEC6
BestRank
Statement
http://www.wikidata.org/entity/statement/Q30754996-E0698B5D-AC1A-4344-9964-67BC7DF0CEC6
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wasDerivedFrom
56a65b81f7ebab9d7c6dc969e1f278ed2cc4ef23
P2860
Heme degradation as catalyzed by a recombinant bacterial heme oxygenase (Hmu O) from Corynebacterium diphtheriae.