The same domain motif for ubiquinone reduction in mitochondrial or chloroplast NADH dehydrogenase and bacterial glucose dehydrogenase

FEBS Lett. 1990 Jun 4;265(1-2):37-40. doi: 10.1016/0014-5793(90)80878-m.

Abstract

The respiratory chain NADH:ubiquinone oxidoreductase (NADH dehydrogenase or Complex I) of mitochondria comprises some 30 different subunits, and one FMN and 4 or 5 iron-sulfur clusters as internal redox groups. The bacterial glucose dehydrogenase, which oxidizes glucose to gluconolactone in the periplasmatic space and transfers the electrons to ubiquinone, is a single polypeptide chain with pyrolloquinoline quinone as the only redox group. We report here that the two different enzymes have the same ubiquinone binding domain motif and we discuss the predicted membrane folding of this domain with regard to its role in the proton translocating function of the two enzymes.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacteria / enzymology*
  • Bacteria / genetics
  • Carbohydrate Dehydrogenases / genetics*
  • Chlamydomonas / enzymology
  • Chlamydomonas / genetics
  • Chloroplasts / enzymology*
  • Cytochrome Reductases / genetics*
  • Genes
  • Glucose 1-Dehydrogenase
  • Glucose Dehydrogenases / genetics*
  • Humans
  • Mitochondria / enzymology*
  • Models, Structural
  • Molecular Sequence Data
  • NADH Dehydrogenase / genetics*
  • Neurospora crassa / enzymology
  • Neurospora crassa / genetics
  • Oxidation-Reduction
  • Protein Conformation
  • Sequence Homology, Nucleic Acid
  • Ubiquinone / metabolism*

Substances

  • Ubiquinone
  • Carbohydrate Dehydrogenases
  • Glucose Dehydrogenases
  • Glucose 1-Dehydrogenase
  • Cytochrome Reductases
  • NADH Dehydrogenase