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Q46342369-214E669B-4195-492C-9746-A843A3C46B45
Q46342369-214E669B-4195-492C-9746-A843A3C46B45
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http://www.wikidata.org/entity/statement/Q46342369-214E669B-4195-492C-9746-A843A3C46B45
Critical Aspects of Heme-Peroxo-Cu Complex Structure and Nature of Proton Source Dictate Metal-O(peroxo) Breakage versus Reductive O-O Cleavage Chemistry.
P2860
Q46342369-214E669B-4195-492C-9746-A843A3C46B45
BestRank
Statement
http://www.wikidata.org/entity/statement/Q46342369-214E669B-4195-492C-9746-A843A3C46B45
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wasDerivedFrom
8d49c3544d683f953dc6387991707b0378a27454
P2860
Using Biosynthetic Models of Heme-Copper Oxidase and Nitric Oxide Reductase in Myoglobin to Elucidate Structural Features Responsible for Enzymatic Activities.