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. 1995 Feb;177(3):831-4.
doi: 10.1128/jb.177.3.831-834.1995.

Stereospecificity of hydride removal from NADH by reductases of multicomponent nonheme iron oxygenase systems

H R Schläfli  1 , D P Baker, T Leisinger, A M Cook
Affiliations

Stereospecificity of hydride removal from NADH by reductases of multicomponent nonheme iron oxygenase systems

H R Schläfli et al. J Bacteriol. 1995 Feb.

Abstract

The stereospecificity of hydride removal from the 4 position of the pyridine ring of NADH by reductases from all three classes of multicomponent nonheme iron oxygenases was examined. The class I and II reductases, modules of which show significant sequence similarity with and which belong to the ferredoxin-NADP+ reductase family of flavin-dependent oxidoreductases, transferred the pro-R hydrogen. By contrast, the class II enzymes, which do not show significant sequence similarity to the class I and III enzymes but modules of which belong to the glutathione reductase family of flavoenzymes, transferred the pro-S hydrogen.

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