Title : Oxygen activation by the noncoupled binuclear copper site in peptidylglycine alpha-hydroxylating monooxygenase. Spectroscopic definition of the resting sites and the putative CuIIM-OOH intermediate.

Pub. Date : 2004 May 18

PMID : 15134448






2 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Azide binding to PHM is used as a spectroscopic and electronic structure analogue to OOH(-) binding to provide a starting point for developing a geometric and electronic structural model for the putative Cu(II)(M)-OOH intermediate in the H-atom abstraction reaction of PHM. Azides peptidylglycine alpha-amidating monooxygenase Homo sapiens
2 Azide binding to PHM is used as a spectroscopic and electronic structure analogue to OOH(-) binding to provide a starting point for developing a geometric and electronic structural model for the putative Cu(II)(M)-OOH intermediate in the H-atom abstraction reaction of PHM. Azides peptidylglycine alpha-amidating monooxygenase Homo sapiens