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Q43019297-044319BD-399C-49A6-8821-075CE78FD0B9
Q43019297-044319BD-399C-49A6-8821-075CE78FD0B9
BestRank
Statement
http://www.wikidata.org/entity/statement/Q43019297-044319BD-399C-49A6-8821-075CE78FD0B9
Structure and reactivity of a thermostable prokaryotic nitric-oxide synthase that forms a long-lived oxy-heme complex.
P2860
Q43019297-044319BD-399C-49A6-8821-075CE78FD0B9
BestRank
Statement
http://www.wikidata.org/entity/statement/Q43019297-044319BD-399C-49A6-8821-075CE78FD0B9
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wasDerivedFrom
4a8b444121c409da746fe03c62970ef548a8eb72
P2860
Catalytic mechanism of heme oxygenase through EPR and ENDOR of cryoreduced oxy-heme oxygenase and its Asp 140 mutants.