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Results 1 - 10 of 23 > >>
EC Number
Cofactor
Commentary
Reference
FAD
1 mol FAD per mol enzyme
FAD
1 mol FAD per mol of recombinant enzyme
FAD
calculated results suggest that the electron and/or hydride ion transfer reaction from NADH to FAD can be accelerated in the presence of heme(Fe3+)
FAD
cytochrome b5 reductase is composed of one FAD and one NADH binding domain linked by a hinge region
FAD
flavoprotein, the FAD domain has a large cleft in which the FAD prosthetic group is located. The N-terminus of the NADH domain plays a hinge-connecting role between the two domains, the FAD and the NADH domains
FAD
non-covalentely bound prosthetic group
FAD
non-covalently bound in a large cleft between the two major domains
FAD
redox state of FAD during the b5R catalytic cycle and crystal structures comparion of the fully reduced form and the oxidized form, overview
FAD
tightly bound prosthetic group
Results 1 - 10 of 23 > >>