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Q30754996-8328CCAC-07BE-4E1F-A3C5-A11DA38D8598
Q30754996-8328CCAC-07BE-4E1F-A3C5-A11DA38D8598
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http://www.wikidata.org/entity/statement/Q30754996-8328CCAC-07BE-4E1F-A3C5-A11DA38D8598
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
Q30754996-8328CCAC-07BE-4E1F-A3C5-A11DA38D8598
BestRank
Statement
http://www.wikidata.org/entity/statement/Q30754996-8328CCAC-07BE-4E1F-A3C5-A11DA38D8598
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wasDerivedFrom
56a65b81f7ebab9d7c6dc969e1f278ed2cc4ef23
P2860
Utilization of host iron sources by Corynebacterium diphtheriae: identification of a gene whose product is homologous to eukaryotic heme oxygenases and is required for acquisition of iron from heme and hemoglobin.