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Two separate transhydrogenase activities are present in plant mitochondria

Author:
  • Natalia V. Bykova
  • Allan G. Rasmusson
  • Abir U. Igamberdiev
  • Per Gardeström
  • Ian M Møller
Publishing year: 1999-11-11
Language: English
Pages: 106-111
Publication/Series: Biochemical and Biophysical Research Communications
Volume: 265
Issue: 1
Document type: Journal article
Publisher: Elsevier

Abstract english

Inside-out submitochondrial particles from both potato tubers and pea leaves catalyze the transfer of hydride equivalents from NADPH to NAD+ as monitored with a substrate-regenerating system. The NAD+ analogue acetylpyridine adenine dinucleotide is also reduced by NADPH and incomplete inhibition by the complex I inhibitor diphenyleneiodonium (DPI) indicates that two enzymes are involved in this reaction. Gel-filtration chromatography of solubilized mitochondrial membrane complexes confirms that the DPI-sensitive TH activity is due to NADH-ubiquinone oxidoreductase (EC 1.6.5.3, complex I), whereas the DPI-insensitive activity is due to a separate enzyme eluting around 220 kDa. The DPI-insensitive TH activity is specific for the 4B proton on NADH, whereas there is no indication of a 4A-specific activity characteristic of a mammalian-type energy-linked TH. The DPI-insensitive TH may be similar to the soluble type of transhydrogenase found in, e.g., Pseudomonas. The presence of non-energy-linked TH activities directly coupling the matrix NAD(H) and NADP(H) pools will have important consequences for the regulation of NADP-linked processes in plant mitochondria.

Keywords

  • Botany
  • Biochemistry and Molecular Biology

Other

Published
  • ISSN: 0006-291X
Allan Rasmusson
E-mail: allan [dot] rasmusson [at] biol [dot] lu [dot] se

Professor

Molecular Cell Biology

+46 46 222 93 81

B-A329A

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