Mechanism of NADH transfer among dehydrogenases.
Steady-state and transient-state kinetic experiments have been performed to test the proposal that there is a direct (channelled) transfer of NADH from one dehydrogenase to another if the two enzymes exhibit distinct chiral coenzyme specificity (A-side vs. B-side). The results lend no support to this proposal, but are fully consistent with a free-diffusion mechanism of NADH transfer irrespective of the chiral specificity of the enzymes.
Arias
W M
WM
Department of Biochemistry, Chemical Center, University of Lund, Lund, Sweden.
Pettersson
H
H
Pettersson
G
G
D000426:Alcohol Dehydrogenase / Q000378:metabolism; D000818:Animals; D002021:Buffers; D002417:Cattle; D005993:Glycerolphosphate Dehydrogenase / Q000378:metabolism; D007700:Kinetics; D009243:NAD / Q000378:metabolism*; D010088:Oxidoreductases / Q000378:metabolism*; D011817:Rabbits; D013237:Stereoisomerism; D013552:Swine
D002021:Buffers; D009243:NAD; D010088:Oxidoreductases; D005993:Glycerolphosphate Dehydrogenase; D000426:Alcohol Dehydrogenase