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  • 标题:Dehydrogenase and transhydrogenase properties of the soluble NADH dehydrogenase of bovine heart mitochondria
  • 本地全文:下载
  • 作者:Y Hatefi ; Y M Galante
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:1977
  • 卷号:74
  • 期号:3
  • 页码:846-850
  • DOI:10.1073/pnas.74.3.846
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:The soluble NADH dehydrogenase of low molecular weight, isolated from complex I (NADH:ubiquinone oxidoreductase, EC 1.6.5.3 ) of the respiratory chain, has been shown to have NADPH dehydrogenase and NADPH leads to NAD transhydrogenase activities. Both activities are greatly increased in the presence of added guanidine-HCl and at pH values less than 6.5. The chromophores of the soluble enzyme (flavin and iron--sulfur centers) are reduced by NADH and NADPH to the same extent. The latter reduction is extremely slow, and is considerably stimulated in the presence of guanidine-HCl. The soluble dehydrogenase has little or no NADH leads to NADP and NADPH leads to NADP transhydrogenase activity. The former reaction is known to be energy-linked in submitochondrial particles; the latter was shown in the present studies also to be energy-linked. In view of the above and earlier results, possible mechanisms for dehydrogenation and transhydrogenation (nonenergy-linked and energy-linked) involving reduced and oxidized NAD and NADP are proposed.
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