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

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1995
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Schläfli, Hans R.
Baker, Darren P.
Leisinger, Thomas
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Journal of Bacteriology ; 177 (1995), 3. - S. 831-834
Zusammenfassung
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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570 Biowissenschaften, Biologie
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ISO 690SCHLÄFLI, Hans R., Darren P. BAKER, Thomas LEISINGER, Alasdair M. COOK, 1995. Stereospecificity of hydride removal from NADH by reductases of multicomponent nonheme iron oxygenase systems. In: Journal of Bacteriology. 177(3), pp. 831-834
BibTex
@article{Schlafli1995Stere-8715,
  year={1995},
  title={Stereospecificity of hydride removal from NADH by reductases of multicomponent nonheme iron oxygenase systems},
  number={3},
  volume={177},
  journal={Journal of Bacteriology},
  pages={831--834},
  author={Schläfli, Hans R. and Baker, Darren P. and Leisinger, Thomas and Cook, Alasdair M.}
}
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