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NAD(P)H-ubiquinone oxidoreductases in plant mitochondria

Møller, Ian M.; Rasmusson, Allan G. LU and Fredlund, Kenneth M. (1993) In Journal of Bioenergetics and Biomembranes 25(4). p.377-384
Abstract

Plant (and fungal) mitochondria contain multiple NAD(P)H dehydrogenases in the inner membrane all of which are connected to the respiratory chain via ubiquinone. On the outer surface, facing the intermembrane space and the cytoplasm, NADH and NADPH are oxidized by what is probably a single low-molecular-weight, nonproton-pumping, unspecific rotenone-insensitive NAD(P)H dehydrogenase. Exogenous NADH oxidation is completely dependent on the presence of free Ca2+ with a K0.5 of about 1 μM. On the inner surface facing the matrix there are two dehydrogenases: (1) the proton-pumping rotenone-sensitive multisubunit Complex I with properties similar to those of Complex I in mammalian and fungal mitochondria. (2) a... (More)

Plant (and fungal) mitochondria contain multiple NAD(P)H dehydrogenases in the inner membrane all of which are connected to the respiratory chain via ubiquinone. On the outer surface, facing the intermembrane space and the cytoplasm, NADH and NADPH are oxidized by what is probably a single low-molecular-weight, nonproton-pumping, unspecific rotenone-insensitive NAD(P)H dehydrogenase. Exogenous NADH oxidation is completely dependent on the presence of free Ca2+ with a K0.5 of about 1 μM. On the inner surface facing the matrix there are two dehydrogenases: (1) the proton-pumping rotenone-sensitive multisubunit Complex I with properties similar to those of Complex I in mammalian and fungal mitochondria. (2) a rotenone-insensitive NAD(P)H dehydrogenase with equal activity with NADH and NADPH and no proton-pumping activity. The NADPH-oxidizing activity of this enzyme is completely dependent on Ca2+ with a K0.5 of 3 μM. The enzyme consists of a single subunit of 26 kDa and has a native size of 76 kDa, which means that it may form a trimer. © 1993 Plenum Publishing Corporation.

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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
(Plant) mitochondria, calcium, Complex I, electrostatic interactions, NAD(P)H dehydrogenase, NAD(P)H-ubiquinone oxidoreductase, rotenone
in
Journal of Bioenergetics and Biomembranes
volume
25
issue
4
pages
8 pages
publisher
Kluwer
external identifiers
  • Scopus:0027323955
ISSN
0145-479X
DOI
10.1007/BF00762463
language
English
LU publication?
yes
id
444ba892-8003-4d4e-b6b1-40717b201221
date added to LUP
2016-05-31 21:38:37
date last changed
2016-08-10 14:36:52
@misc{444ba892-8003-4d4e-b6b1-40717b201221,
  abstract     = {<p>Plant (and fungal) mitochondria contain multiple NAD(P)H dehydrogenases in the inner membrane all of which are connected to the respiratory chain via ubiquinone. On the outer surface, facing the intermembrane space and the cytoplasm, NADH and NADPH are oxidized by what is probably a single low-molecular-weight, nonproton-pumping, unspecific rotenone-insensitive NAD(P)H dehydrogenase. Exogenous NADH oxidation is completely dependent on the presence of free Ca<sup>2+</sup> with a K<sub>0.5</sub> of about 1 μM. On the inner surface facing the matrix there are two dehydrogenases: (1) the proton-pumping rotenone-sensitive multisubunit Complex I with properties similar to those of Complex I in mammalian and fungal mitochondria. (2) a rotenone-insensitive NAD(P)H dehydrogenase with equal activity with NADH and NADPH and no proton-pumping activity. The NADPH-oxidizing activity of this enzyme is completely dependent on Ca<sup>2+</sup> with a K<sub>0.5</sub> of 3 μM. The enzyme consists of a single subunit of 26 kDa and has a native size of 76 kDa, which means that it may form a trimer. © 1993 Plenum Publishing Corporation.</p>},
  author       = {Møller, Ian M. and Rasmusson, Allan G. and Fredlund, Kenneth M.},
  issn         = {0145-479X},
  keyword      = {(Plant) mitochondria,calcium,Complex I,electrostatic interactions,NAD(P)H dehydrogenase,NAD(P)H-ubiquinone oxidoreductase,rotenone},
  language     = {eng},
  number       = {4},
  pages        = {377--384},
  publisher    = {ARRAY(0x8839c88)},
  series       = {Journal of Bioenergetics and Biomembranes},
  title        = {NAD(P)H-ubiquinone oxidoreductases in plant mitochondria},
  url          = {http://dx.doi.org/10.1007/BF00762463},
  volume       = {25},
  year         = {1993},
}