Binding of malate dehydrogenase and NADH channelling to complex I

Judit Ovádi, Yongwei Huang, H. Olin Spivey

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

As previously reported, mitochondrial malate dehydrogenase (MDH) binds to purified complex I of the electron transport system. With conditions used in previous reports, MDH binds even more extensively, but probably predominantly non‐specifically, to the matrix side of the inner mitochondrial membrane of submitochodrial particles (SMP). Herein we report experimental conditions for highly specific binding of malate dehydrogenase to complex I within SMP. These conditions permit us to demonstrate NADH channelling from malate dehydrogenase to complex I using the completing reaction test. This test, though not ideal for all situations, has several advantages over the enzyme buffering test previously used. These advantages should facilitate further studies elucidating NADH channeling to complex I from MDH and other dehydrogenases. Independent evidence of NADH channelling to the electron transport chain and the potential advantages of substrate channelling in general are also discussed. Substrate channelling from MDH in particular may be especially beneficial because of the unfavourable equilibrium and kinetics of this enzyme reaction.

Original languageEnglish
Pages (from-to)265-272
Number of pages8
JournalJournal of Molecular Recognition
Volume7
Issue number4
DOIs
Publication statusPublished - Dec 1994

Keywords

  • Binding
  • Complex I
  • Malate dehydrogenase
  • NADH channelling
  • Submitochondrial particles

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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