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Journal of Cell Science, Vol 112, Issue 14 2347-2354, Copyright © 1999 by Company of Biologists
JOURNAL ARTICLES |
SJ Kerscher, JG Okun and U Brandt
Institut fur Biochemie I, Zentrum der Biologischen Chemie, Universitatsklinikum Frankfurt, D-60590 Frankfurt am Main, Germany.
NADH:ubiquinone oxidoreductases catalyse the first step within the diverse pathways of mitochondrial NADH oxidation. In addition to the energy-conserving form commonly called complex I, fungi and plants contain much simpler alternative NADH:ubiquinone oxido-reductases that catalyze the same reaction but do not translocate protons across the inner mitochondrial membrane. Little is known about the distribution and function of these enzymes. We have identified YLNDH2 as the only gene encoding an alternative NADH:ubiquinone oxidoreductase (NDH2) in the obligate aerobic yeast Yarrowia lipolytica. Cells carrying a deletion of YLNDH2 were fully viable; full inhibition by piericidin A indicated that complex I activity was the sole NADH:ubiquinone oxidoreductase activity left in the deletion strains. Studies with intact mitochondria revealed that NDH2 in Y. lipolytica is oriented towards the external face of the mitochondrial inner membrane. This is in contrast to the situation seen in Saccharomyces cerevisiae, Neurospora crassa and in green plants, where internal alternative NADH:ubiquinone oxidoreductases have been reported. Phylogenetic analysis of known NADH:ubiquinone oxidoreductases suggests that during evolution conversion of an ancestral external alternative NADH:ubiquinone oxidoreductase to an internal enzyme may have paved the way for the loss of complex I in fermenting yeasts like S. cerevisiae.
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T. Yamashita, E. Nakamaru-Ogiso, H. Miyoshi, A. Matsuno-Yagi, and T. Yagi Roles of Bound Quinone in the Single Subunit NADH-Quinone Oxidoreductase (Ndi1) from Saccharomyces cerevisiae J. Biol. Chem., March 2, 2007; 282(9): 6012 - 6020. [Abstract] [Full Text] [PDF]
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K. Zwicker, A. Galkin, S. Drose, L. Grgic, S. Kerscher, and U. Brandt The Redox-Bohr Group Associated with Iron-Sulfur Cluster N2 of Complex I J. Biol. Chem., August 11, 2006; 281(32): 23013 - 23017. [Abstract] [Full Text] [PDF]
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A. Galkin and U. Brandt Superoxide Radical Formation by Pure Complex I (NADH:Ubiquinone Oxidoreductase) from Yarrowia lipolytica J. Biol. Chem., August 26, 2005; 280(34): 30129 - 30135. [Abstract] [Full Text] [PDF]
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A. Eschemann, A. Galkin, W. Oettmeier, U. Brandt, and S. Kerscher HDQ (1-Hydroxy-2-dodecyl-4(1H)quinolone), a High Affinity Inhibitor for Mitochondrial Alternative NADH Dehydrogenase: EVIDENCE FOR A PING-PONG MECHANISM J. Biol. Chem., February 4, 2005; 280(5): 3138 - 3142. [Abstract] [Full Text] [PDF]
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 A. M. P. Melo, T. M. Bandeiras, and M. Teixeira New Insights into Type II NAD(P)H:Quinone Oxidoreductases Microbiol. Mol. Biol. Rev., December 1, 2004; 68(4): 603 - 616. [Abstract] [Full Text] [PDF]
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L. Grgic, K. Zwicker, N. Kashani-Poor, S. Kerscher, and U. Brandt Functional Significance of Conserved Histidines and Arginines in the 49-kDa Subunit of Mitochondrial Complex I J. Biol. Chem., May 14, 2004; 279(20): 21193 - 21199. [Abstract] [Full Text] [PDF]
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 S. J. Kerscher, A. Eschemann, P. M. Okun, and U. Brandt External alternative NADH:ubiquinone oxidoreductase redirected to the internal face of the mitochondrial inner membrane rescues complex I deficiency in Yarrowia lipolytica J. Cell Sci., January 11, 2001; 114(21): 3915 - 3921. [Abstract] [Full Text] [PDF]
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P. M. Ahlers, K. Zwicker, S. Kerscher, and U. Brandt Function of Conserved Acidic Residues in the PSST Homologue of Complex I (NADH:Ubiquinone Oxidoreductase) from Yarrowia lipolytica J. Biol. Chem., July 28, 2000; 275(31): 23577 - 23582. [Abstract] [Full Text] [PDF]
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A. M. P. Melo, M. Duarte, I. M. Moller, H. Prokisch, P. L. Dolan, L. Pinto, M. A. Nelson, and A. Videira The External Calcium-dependent NADPH Dehydrogenase from Neurospora crassa Mitochondria J. Biol. Chem., February 2, 2001; 276(6): 3947 - 3951. [Abstract] [Full Text] [PDF]
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N. Kashani-Poor, K. Zwicker, S. Kerscher, and U. Brandt A Central Functional Role for the 49-kDa Subunit within the Catalytic Core of Mitochondrial Complex I J. Biol. Chem., June 22, 2001; 276(26): 24082 - 24087. [Abstract] [Full Text] [PDF]
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