J. Biol. Chem., Vol. 255, Issue 19, 9025-9027, 10, 1980

Stereochemical studies of 8-hydroxy-5-deazaflavin-dependent NADP+ reductase from Methanococcus vannielii

S Yamazaki, L Tsai, TC Stadtman, FS Jacobson and C Walsh

The purified 8-hydroxy-5-deazaflavin-dependent NADP+ reductase from Methanococcus vannielii catalyzes an oxidation-reduction reaction between a novel 8-hydroxy-5-deazaflavin cofactor and nicotinamide adenine dinucleotide phosphate. The reaction was shown to be a direct hydride transfer process. Using stereospecifically 3H-labeled substrates, the steric course of this process was established to be S- specific with respect to the nicotinamide nucleotide. The 8-hydroxy-5- deazaflavin-dependent NADP+ reductase from M. vannielii and the hydrogenase system in the cell-free extracts of Methanobacterium thermoautotrophicum recognize the same side, designated as A side, with respect to the prochiral center at C-5 of the dihydro-8-hydroxy-5- deazaflavin cofactor.
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