Inouye S, Nakamura H
Yokohama Research Center, Chisso Corporation, Japan.
Biochem Biophys Res Commun. 1994 Nov 30;205(1):275-81. doi: 10.1006/bbrc.1994.2661.
The stereospecificity of the hydride transfer in NAD(P)H-flavin reductase reaction of V. fischeri ATCC 7744 was determined by 1H-NMR spectroscopy using stereospecifically labeled reduced beta-nicotinamide adenine dinucleotide (beta-NADH). The recombinant flavoenzyme, purified from E. coli cells, selectively transferred the pro-R hydrogen at the C-4 position of the nicotinamide ring to flavin and is therefore classified as an A-side specific enzyme. Lumiflavin was used for the reductase reaction, but lumichrome and alpha-NADH were not utilized as electron acceptor and donor, respectively.
使用立体专一性标记的还原型β-烟酰胺腺嘌呤二核苷酸（β-NADH），通过1H-NMR光谱法测定了费氏弧菌ATCC 7744的NAD(P)H-黄素还原酶反应中氢化物转移的立体专一性。从大肠杆菌细胞中纯化得到的重组黄素酶，将烟酰胺环C-4位的前-R氢选择性地转移至黄素上，因此被归类为A面特异性酶。还原酶反应中使用了发光黄素，但发光色素和α-NADH分别未被用作电子受体和供体。
