title: Yeast mitochondrial dehydrogenases are associated in a supramolecular complex.
abstract: Separation of yeast mitochondrial complexes by colorless native polyacrylamide gel electrophoresis led to the identification of a supramolecular structure exhibiting NADH-dehydrogenase activity. Components of this complex were identified by N-terminal Edman degradation and matrix-assisted laser desorption ionization mass spectrometry. The complex was found to contain the five known intermembrane space-facing dehydrogenases, namely two external NADH-dehydrogenases Nde1p and Nde2p, glycerol-3-phosphate dehydrogenase Gut2p, D- and L-lactate-dehydrogenases Dld1p and Cyb2p, the matrix-facing NADH-dehydrogenase Ndi1p, two probable flavoproteins YOR356Wp and YPR004Cp, four tricarboxylic acids cycle enzymes (malate dehydrogenase Mdh1p, citrate synthase Cit1p, succinate dehydrogenase Sdh1p, and fumarate hydratase Fum1p), and the acetaldehyde dehydrogenase Ald4p. The association of these proteins is discussed in terms of NADH-channeling.
authors.affiliation: UMR5095 C.N.R.S./Université de Bordeaux 2, 1 rue Camille Saint-Saëns, 33077 Bordeaux Cedex, France. x.grandier-vazeilles@ibgc.u-bordeaux2.fr
authors.forename: X
authors.initials: X
authors.lastname: Grandier-Vazeille
authors.forename: K
authors.initials: K
authors.lastname: Bathany
authors.forename: S
authors.initials: S
authors.lastname: Chaignepain
authors.forename: N
authors.initials: N
authors.lastname: Camougrand
authors.forename: S
authors.initials: S
authors.lastname: Manon
authors.forename: J M
authors.initials: JM
authors.lastname: Schmitter
mesh_terms: D050842:1-Pyrroline-5-Carboxylate Dehydrogenase; D000445:Aldehyde Oxidoreductases / Q000737:chemistry; D002462:Cell Membrane / Q000201:enzymology; D002851:Chromatography, High Pressure Liquid; D002950:Citrate (si)-Synthase / Q000737:chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D005420:Flavoproteins / Q000737:chemistry; D005649:Fumarate Hydratase / Q000737:chemistry; D005993:Glycerolphosphate Dehydrogenase / Q000737:chemistry; D007770:L-Lactate Dehydrogenase / Q000737:chemistry; D008291:Malate Dehydrogenase / Q000737:chemistry; D008928:Mitochondria / Q000201:enzymology*; D008954:Models, Biological; D009245:NADH Dehydrogenase / Q000737:chemistry / Q000378:metabolism; D010088:Oxidoreductases / Q000737:chemistry*; D010100:Oxygen / Q000378:metabolism; D010766:Phosphorylation; D011485:Protein Binding; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D029701:Saccharomyces cerevisiae Proteins; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013385:Succinate Dehydrogenase / Q000737:chemistry; D013997:Time Factors
chemical_list: D005420:Flavoproteins; D029701:Saccharomyces cerevisiae Proteins; D010088:Oxidoreductases; D005993:Glycerolphosphate Dehydrogenase; D007770:L-Lactate Dehydrogenase; D008291:Malate Dehydrogenase; D000445:Aldehyde Oxidoreductases; C018699:aldehyde dehydrogenase (NAD(P)+); D050842:1-Pyrroline-5-Carboxylate Dehydrogenase; C494242:PUT2 protein, S cerevisiae; D013385:Succinate Dehydrogenase; D009245:NADH Dehydrogenase; D002950:Citrate (si)-Synthase; D005649:Fumarate Hydratase; D010100:Oxygen