Institut für Biochemie I (Molekulare Bioenergetik)

Komm. Direktor: Prof. Dr. Ulrich Brandt

Publikationen 2000

Originalpublikationen und Reviews

  1.    Ahlers,P., Garofano,A., Kerscher,S. and Brandt,U. Application of the Obligate Aerobic Yeast Yarrowia lipolytica as a Eucaryotic Model to Analyze Leigh Syndrome Mutations in the Complex I Core Subunits PSST and TYKY . Biochim. Biophys. Acta 1459, 258-265 (2000).

  2.    Ahlers,P., Zwicker,K., Kerscher,S. and Brandt,U. Function of conserved acidic residues in the PSST-homologue of complex I (NADH:ubiquinone oxidoreductase) from Yarrowia lipolytica. J. Biol. Chem. 275, 23577-23582 (2000).

  3.    Aufurth,S., Schägger,H. & Müller,V. Identification of subunits a, b, and c1 from Acetobacterium woodii Na+-F1F0 ATPase: Subunits c1,c2, and c3 constitute a mixed c-oligomer. J. Biol. Chem. 275, 33297-33301 (2000) 

  4.    Averbeck,N.B., Jensen,O.N., Mann,M., Schägger,H. & Osiewacz,H.D. Identification and characterization of PaMTH1, a putative O-methyltransferase accumulating during senescence of Podospora anserina cultures. Curr. Genet. 37, 200-208 (2000) .

  5.    Djafarzadeh,R. Kerscher, S., Zwicker, K., Lindahl, M., Radermacher, M. und Brandt, U. Biophysical and structural characterization of proton-translocating NADH-dehydrogenase (complex I) from the strictly aerobic yeast Yarrowia lipolytica. Biochim. Biophys. Acta 1459, 230-238 (2000). 

  6.      Kerscher,S. Diversity and origin of alternative NADH:ubiquinone oxidoreductases Biochim. Biophys. Acta 1459, 274-283 (2000).  

  7.     Kurki,S., Zickermann,V., Kervinen,M., Hassinen,I. and Finel,M. Mutagenesis of three conserved glu residues in a bacterial homologue of the ND1 subunit of complex I affects ubiquinone reduction kinetics but not inhibition by dicyclohexylcarbodiimide. Biochemistry 39, 13496-13502 (2000).

  8.    Okun,J.G., Zickermann,V., Zwicker,K., Schägger,H. and Brandt,U. Binding of Detergents and Inhibitors to Bovine Complex I - A Novel Purification Procedure of Bovine Complex I Retaining Full Inhibitor Sensitivity. Biochim. Biophys. Acta 1459, 77-87 (2000).

  9.      Poetsch,A., Neff,D., Seelert,H., Schägger,H. and Dencher,N.A. Dye removal, catalytic activity and 2D crystallization of chloroplast H+-ATP synthase purified by blue native electrophoresis. Biochim. Biophys. Acta 1466, 339-349 (2000).

  10.      Schägger,H. and Pfeiffer,K. Supercomplexes in the respiratory chains of yeast and mammalian mitochondria. EMBO J. 19, 1777-1783 (2000).

  11.     Zickermann,V., Kurki,S., Kervinen,M., Hassinen,I., and Finel,M. The NADH oxidation domain of Complex I: do bacterial and mitochondrial enzymes catalyze ferricyanide reduction similarly? Biochim. Biophys. Acta 1459, 61-68 (2000).

Lehr- und Handbuchbeiträge, Monografien

  1. Zubay,G.L. Biochemie; U. Brandt und H. Schägger, Hrsg., McGraw-Hill, London, Frankfurt (2000).

Dissertationen

  1. Ahlers, P.M.
    Funktion von konservierten sauren Resten in der PSST-homologen Untereinheit von Komplex I (NADH:Ubichinon Oxidoreduktase) aus Yarrowia lipolytica´

  2. T. Merbitz-Zahradnik
    Untersuchungen an Mutanten des "Rieske"-Eisen-Schwefel-Proteins des mitochondrialen bc1-Komplexes in Saccharomyces cerevisiae.

  3. Djafarzadeh Andabili, R.
    Isolierung und Charakterisierung von Komplex I (NADH:Ubichinon Oxidoreduktase) aus Hefe Yarrowia lipolytica

  4. Kashani-Poor, N.
    Identifizierung des katalytischen Zentrums im Komplex I  (NADH:Ubichinon Oxidoreduktase)