Proton-coupled electron transfer and adduct configuration are important for C4a-hydroperoxyflavin formation and stabilization in a flavoenzyme.
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The substrate tolerance of alcohol oxidasesKinetic Mechanism of the Dechlorinating Flavin-dependent Monooxygenase HadA.Kinetic mechanism of L-α-glycerophosphate oxidase from Mycoplasma pneumoniae.Magnetic field effects as a result of the radical pair mechanism are unlikely in redox enzymes.Oxidative dehalogenation and denitration by a flavin-dependent monooxygenase is controlled by substrate deprotonation
P2860
Proton-coupled electron transfer and adduct configuration are important for C4a-hydroperoxyflavin formation and stabilization in a flavoenzyme.
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Proton-coupled electron transf ...... tabilization in a flavoenzyme.
@en
Proton-coupled electron transf ...... tabilization in a flavoenzyme.
@nl
type
label
Proton-coupled electron transf ...... tabilization in a flavoenzyme.
@en
Proton-coupled electron transf ...... tabilization in a flavoenzyme.
@nl
prefLabel
Proton-coupled electron transf ...... tabilization in a flavoenzyme.
@en
Proton-coupled electron transf ...... tabilization in a flavoenzyme.
@nl
P2093
P356
P1476
Proton-coupled electron transf ...... tabilization in a flavoenzyme.
@en
P2093
Jeerus Sucharitakul
Panida Surawatanawong
Surawit Visitsatthawong
Thanyaporn Wongnate
P304
P356
10.1021/JA4088055
P407
P577
2013-12-24T00:00:00Z