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A Self-Assembled Respiratory Chain that Catalyzes NADH Oxidation by Ubiquinone-10 Cycling between Complex I and the Alternative Oxidase

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Author(s)

  • Andrew J Y Jones
  • James N Blaza
  • Hannah R Bridges
  • Benjamin May
  • Anthony L Moore
  • Judy Hirst

Department/unit(s)

Publication details

JournalAngewandte Chemie International Edition
DateE-pub ahead of print - 23 Nov 2015
DatePublished (current) - 11 Jan 2016
Issue number2
Volume55
Number of pages4
Pages (from-to)728-31
Early online date23/11/15
Original languageEnglish

Abstract

Complex I is a crucial respiratory enzyme that conserves the energy from NADH oxidation by ubiquinone-10 (Q10) in proton transport across a membrane. Studies of its energy transduction mechanism are hindered by the extreme hydrophobicity of Q10, and they have so far relied on native membranes with many components or on hydrophilic Q10 analogues that partition into membranes and undergo side reactions. Herein, we present a self-assembled system without these limitations: proteoliposomes containing mammalian complex I, Q10, and a quinol oxidase (the alternative oxidase, AOX) to recycle Q10H2 to Q10. AOX is present in excess, so complex I is completely rate determining and the Q10 pool is kept oxidized under steady-state catalysis. The system was used to measure a fully-defined K(M) value for Q10. The strategy is suitable for any enzyme with a hydrophobic quinone/quinol substrate, and could be used to characterize hydrophobic inhibitors with potential applications as pharmaceuticals, pesticides, or fungicides.

Bibliographical note

© 2016 The Authors.

    Research areas

  • Catalysis, Electron Transport, Electron Transport Complex I/chemistry, Mitochondrial Proteins/chemistry, NAD/chemistry, Oxidation-Reduction, Oxidoreductases/chemistry, Plant Proteins/chemistry, Ubiquinone/chemistry

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