Two binding sites for naturally occurring inhibitors in mitochondrial and bacterial NADH:ubiquinone oxidoreductase (complex I).
نویسندگان
چکیده
226 Two binding sites for naturally occurring inhibitors in mitochondrial and bacterial NADH : ubiquinone oxidoreductase (Complex I) Thorsten Friedrich,*$ Tomoko Ohnishi,t Edgar Forche,$ Brigitte Kunze,+ Rolf Jansen,t Wolfram Trowitzsch,+ Gerhard Hofle,$ Hans Reichenbacht and Hanns Weiss* *Institut fur Biochemie, Heinrich-Heine Universitat Dusseldorf, Universitatsstrasse I, W-4OOO Dusseldorf I , Germany; +Department of Biochemistry and Biophysics, School of Medicine, University of Pennsylvania, Philadelphia, PA 19 104-6089, U.S.A. and SGesellschaft fur Biotechnologische Forschung mbH, Mascheroder Weg I , W-3300 Braunschweig, Germany
منابع مشابه
External alternative NADH:ubiquinone oxidoreductase redirected to the internal face of the mitochondrial inner membrane rescues complex I deficiency in Yarrowia lipolytica.
Alternative NADH:ubiquinone oxidoreductases are single subunit enzymes capable of transferring electrons from NADH to ubiquinone without contributing to the proton gradient across the respiratory membrane. The obligately aerobic yeast Yarrowia lipolytica has only one such enzyme, encoded by the NDH2 gene and located on the external face of the mitochondrial inner membrane. In sharp contrast to ...
متن کاملNN'-dicyclohexylcarbodi-imide-sensitivity of bovine heart mitochondrial NADH: ubiquinone oxidoreductase. Inhibition of activity and binding to subunits.
Dicyclohexylcarbodi-imide (DCCD) inhibition of NADH: ubiquinone oxidoreductase was studied in submitochondrial particles and in the isolated form, together with the binding of the reagent to the enzyme. DCCD inhibited the isolated enzyme in a time- and concentration-dependent manner. Over the concentration range studied, a maximum inhibition of 85% was attained within 60 min. The time course fo...
متن کاملComplexes I in the Green Lineage
L. Sazanov (ed.), A Structural Perspective on Respiratory Complex I: Structure and Function of NADH:ubiquinone oxidoreductase, DOI 10.1007/978-94-007-4138-6_11, © Springer Science+Business Media Dordrecht 2012 Abstract In land plants and green algae, mitochondria and chloroplasts were acquired sequentially through primary endosymbiotic events with a a -proteobacterium and a cyanobacterium, resp...
متن کاملThe mitochondrial-encoded subunits of respiratory complex I (NADH:ubiquinone oxidoreductase): identifying residues important in mechanism and disease.
Complex I (NADH:ubiquinone oxidoreductase) is crucial to respiration in many aerobic organisms. The hydrophilic domain of complex I, containing nine or more redox cofactors, and comprising seven conserved core subunits, protrudes into the mitochondrial matrix or bacterial cytoplasm. The α-helical membrane-bound hydrophobic domain contains a further seven core subunits that are mitochondrial-enc...
متن کاملThe transition between active and de-activated forms of NADH:ubiquinone oxidoreductase (Complex I) in the mitochondrial membrane of Neurospora crassa.
The mammalian mitochondrial NADH:ubiquinone oxidoreductase (Complex I) has been shown to exist in two kinetically and structurally distinct slowly interconvertible forms, active (A) and de-activated (D) [Vinogradov and Grivennikova (2001) IUBMB Life 52, 129-134]. This work was undertaken to investigate the putative Complex I A-D transition in the mitochondrial membrane of the lower eukaryote Ne...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- Biochemical Society transactions
دوره 22 1 شماره
صفحات -
تاریخ انتشار 1994