Alternative NAD(P)H dehydrogenases in plant mitochondria - localisation, catalytic functions and physiological roles

Agnieszka Michalecka

Research output: ThesisDoctoral Thesis (compilation)


In addition to complex I, the plant mitochondrial electron transport chain possesses several alternative NAD(P)H dehydrogenases, not present in animals. These enzymes allow nonenergy-conserving electron transfer from cytoplasmic and matrix NAD(P)H to ubiquinone.

The mitochondrial inner membrane was permeabilised with a channel-forming antibiotic, alamethicin, and the activity of internal NADH dehydrogenases was studied in the matrix. This technique revealed that changes occur in substrate specificity of complex I upon isolation of submitochondrial particles. Alamethicin permeabilisation was shown to be a reliable method for measurements of internal NADH dehydrogenases and soluble matrix proteins in their native environment of plant mitochondria.

Three gene families encoding alternative NAD(P)H dehydrogenases were detected in Arabidopsis genome. There are two At-nda genes, four At-ndb genes and one At-ndc gene. The nda and ndb families are more closely related to fungal homologues, while the ndc family has its origin in cyanobacteria. Representative genes of all three families were all shown to encode proteins targeted to mitochondria. Expression of nda1 but not nda2 was shown to be light-dependent. Based on the sequence similarity between NDA proteins it is possible that they have the same submitochondrial localisation and enzymatic function. Most likely, NDA proteins are internal alternative NADH dehydrogenases.

Expression of the St-ndb1 gene in transgenic Nicotiana sylvestris plants imposed specifically increased and decreased external NADPH oxidation in mitochondria isolated from different transgenic lines. A strict correlation to transcript and protein amounts allowed the assignment of St-NDB1 as an external NADPH dehydrogenase. As a consequence the St-ndb1 overexpressing transgenic plants had specifically increased protein levels for alternative oxidase and uncoupling protein, indicating crosstalk in regulation of the protein amount for the enzymes involved in non-energy-conserving pathways.
Original languageEnglish
Awarding Institution
  • Department of Biology
  • [unknown], [unknown], Supervisor, External person
Award date2004 Jun 11
ISBN (Print)91-85067-13-X
Publication statusPublished - 2004

Bibliographical note

Defence details

Date: 2004-06-11
Time: 10:00
Place: Lecture Hall Biology Building

External reviewer(s)

Name: Newton, Kathleen J.
Title: [unknown]
Affiliation: [unknown]


Article: I. Johansson, F.I., Michalecka, A.M., Møller, I.M., and Rasmusson, A.G. (2004) Oxidation and reduction of pyridine nucleotides in alamethicin-permeabilised plant mitochondria. Biochem. J. 380, 193-202

Article: II. Michalecka, A.M., Svensson, Å.S., Johansson, F.I., Agius, S.C., Johansson, U., Brennicke, A., Binder, S., and Rasmusson, A.G. (2003) Arabidopsis genes for mitochondrial type II NAD(P)H dehydrogenases show different evolutionary origin and show distinct responses to light. Plant Physiol. 133, 642-652

Article: III. Michalecka, A.M., Agius, S.C., Møller, I.M., and Rasmusson, A.G. (2004) Identification of a mitochondrial external NADPH dehydrogenase by overexpression in transgenic Nicotiana sylvestris. Plant J. 37, 415-425

The information about affiliations in this record was updated in December 2015.
The record was previously connected to the following departments: Department of Cell and Organism Biology (Closed 2011.) (011002100), Biology building (Closed 2011) (011008000)

Subject classification (UKÄ)

  • Biological Sciences

Free keywords

  • Kärlväxters fysiologi
  • Physiology of vascular plants
  • NAD(P)H dehydrogenase
  • light-dependence
  • electron transport chain
  • alamethicin
  • alternative oxidase


Dive into the research topics of 'Alternative NAD(P)H dehydrogenases in plant mitochondria - localisation, catalytic functions and physiological roles'. Together they form a unique fingerprint.

Cite this