Literature DB >> 8226717

The proton-translocating NADH: ubiquinone oxidoreductase: a discussion of selected topics.

M Finel1.   

Abstract

The proton-translocating NADH:ubiquinone oxidoreductase (complex I) is a large, multi-subunit and multi-redox centre enzyme which is found in the mitochondrial inner membrane and plasma membrane of some bacteria. In this minireview an attempt has been made to critically discuss selected topics in the structure and function of this enzyme. A special emphasis is given to the iron-sulphur cluster and to the proteins that may bind them. Previous suggestions for the mechanism of proton-translocation by complex I are discussed. Subcomplexes that contain several but not all of the subunits of the intact mitochondrial enzyme are described and analysed in order to identify the functional core of the enzyme. The data on the trans-membrane organisation of several subunits is examined. It is hoped that most of the suggestions as well as the questions raised here could be experimentally tested in the near future.

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Year:  1993        PMID: 8226717     DOI: 10.1007/bf00762461

Source DB:  PubMed          Journal:  J Bioenerg Biomembr        ISSN: 0145-479X            Impact factor:   2.945


  52 in total

1.  Accumulation of the pre-assembled membrane arm of NADH:ubiquinone oxidoreductase in mitochondria of manganese-limited grown Neurospora crassa.

Authors:  M Schmidt; T Friedrich; J Wallrath; T Ohnishi; H Weiss
Journal:  FEBS Lett       Date:  1992-11-16       Impact factor: 4.124

2.  Proton/electron stoichiometry of mitochondrial complex I estimated from the equilibrium thermodynamic force ratio.

Authors:  G C Brown; M D Brand
Journal:  Biochem J       Date:  1988-06-01       Impact factor: 3.857

3.  EPR studies of iron-sulfur clusters in isolated subunits and subfractions of NADH-ubiquinone oxidoreductase.

Authors:  T Ohnishi; C I Ragan; Y Hatefi
Journal:  J Biol Chem       Date:  1985-03-10       Impact factor: 5.157

4.  Purification and molecular and enzymic properties of mitochondrial NADH dehydrogenase.

Authors:  Y M Galante; Y Hatefi
Journal:  Arch Biochem Biophys       Date:  1979-02       Impact factor: 4.013

5.  A comparison of the respiratory chain in particles from Paracoccus denitrificans and bovine heart mitochondria by EPR spectroscopy.

Authors:  S P Albracht; H W van Verseveld; W R Hagen; M L Kalkman
Journal:  Biochim Biophys Acta       Date:  1980-12-03

6.  New insights, ideas and unanswered questions concerning iron-sulfur clusters in mitochondria.

Authors:  H Beinert; S P Albracht
Journal:  Biochim Biophys Acta       Date:  1982-12-31

7.  Studies on the electron transfer pathway, topography of iron-sulfur centers, and site of coupling in NADH-Q oxidoreductase.

Authors:  G Krishnamoorthy; P C Hinkle
Journal:  J Biol Chem       Date:  1988-11-25       Impact factor: 5.157

8.  Resolution of NADH:ubiquinone oxidoreductase from bovine heart mitochondria into two subcomplexes, one of which contains the redox centers of the enzyme.

Authors:  M Finel; J M Skehel; S P Albracht; I M Fearnley; J E Walker
Journal:  Biochemistry       Date:  1992-11-24       Impact factor: 3.162

9.  The 30-kilodalton subunit of bovine mitochondrial complex I is homologous to a protein coded in chloroplast DNA.

Authors:  S J Pilkington; J M Skehel; J E Walker
Journal:  Biochemistry       Date:  1991-02-19       Impact factor: 3.162

10.  Three-dimensional structure of NADH: ubiquinone reductase (complex I) from Neurospora mitochondria determined by electron microscopy of membrane crystals.

Authors:  K Leonard; H Haiker; H Weiss
Journal:  J Mol Biol       Date:  1987-03-20       Impact factor: 5.469

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  1 in total

1.  Proton pumping of mitochondrial complex I: differential activation by analogs of ubiquinone.

Authors:  L Helfenbaum; A Ngo; A Ghelli; A W Linnane; M Degli Esposti
Journal:  J Bioenerg Biomembr       Date:  1997-02       Impact factor: 2.945

  1 in total

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