Composition and Enzymatic Properties of the Mitochondrial NADH- and NADPH-Ubiquinone Reductase (Complex I)

  • Youssef Hatefi
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 74)


Complex I is one of the five component enzyme complexes of the mitochondrial electron transport-oxidative phosphorylation system (Fig. 1) (1–3). The enzymatic reactions catalyzed by complex I are summarized in Table I and the composition of the preparation in terms of flavin, nonheme iron (Fe), acid-labile sulfide (S*), ubi quinone, and phospholipids is given in Table II. The resolution of complex I by chaotropic agents (4–6) results in solubilization of ~ 20% protein containing flavin and approximately 50% of the Fe and S* content of complex I. The remainder of Fe and S* plus lipids are associated with the water-insoluble fraction (Fig. 2). Upon fractionation with ammonium sulfate, the soluble fraction yields an iron-sulfur protein with epr characteristics of FeS* center 2 of complex I (see below), plus a flavoprotein containing approximately 4 g atoms of Fe and 4 moles of S* per mole of FMN. The latter catalyzes the oxidation of NADH by various quinones and ferric compounds, including cytochrome c (Table III).


Electron Paramagnetic Resonance Enzymatic Property Nonheme Iron Submitochondrial Particle Chaotropic Agent 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.



electron paramagnetic resonance




2-methylnaphthoquinone (menadione)




reduced 3-acetylpyridine adenine dinucleotide


iron-sulfur centers 1,2,3 and 4, respectively




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Copyright information

© Plenum Press, New York 1976

Authors and Affiliations

  • Youssef Hatefi
    • 1
  1. 1.Scripps Clinic and Research FoundationDepartment of BiochemistryLa JollaUSA

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