Stereospecificity of hydride removal from NADH by reductases of multicomponent nonheme iron oxygenase systems.
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.
Microbiology Institute, Swiss Federal Institute of Technology, Zürich, Switzerland.
H R
HR
Schläfli
D P
DP
Baker
T
T
Leisinger
A M
AM
Cook
D049308:Dioxygenases; D005982:Glutathione Transferase / Q000502:physiology; D007501:Iron / Q000378:metabolism*; D008968:Molecular Conformation; D009097:Multienzyme Complexes / Q000502:physiology*; D009243:NAD / Q000378:metabolism*; D010088:Oxidoreductases / Q000502:physiology; D010105:Oxygenases / Q000502:physiology*
D009097:Multienzyme Complexes; D009243:NAD; D007501:Iron; D010088:Oxidoreductases; C049135:phthalate oxygenase reductase; D010105:Oxygenases; D049308:Dioxygenases; C038703:naphthalene dioxygenase; D005982:Glutathione Transferase