4.7 Review

Towards Characterization of the Chloroplast NAD(P)H Dehydrogenase Complex

Journal

MOLECULAR PLANT
Volume 2, Issue 6, Pages 1127-1140

Publisher

CELL PRESS
DOI: 10.1093/mp/ssp052

Keywords

Arabidopsis; maize; tobacco; NAD(P)H dehydrogenese; chloroplast; thylakoid membrane; cyclic electron transfer; photosystem I

Funding

  1. Academy of Finland
  2. European FP7 SOLAR-H2 Program [212508]
  3. Emil Aaltonen Foundation
  4. Maj and Tor Nessling Foundation

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The NAD(P)H dehydrogenase (NDH) complex in chloroplast thylakoid membranes functions in cyclic electron transfer, and in chlororespiration. NDH is composed of at least 15 subunits, including both chloroplast- and nuclear-encoded proteins. During the past few years, extensive proteomic and genetic research on the higher plant NDH complex has been carried out, resulting in identification of several novel nuclear-encoded subunits. In addition, a number of auxiliary proteins, which mainly regulate the expression of chloroplast-encoded ndh genes as well as the assembly and stabilization of the NDH complex, have been discovered and characterized. In the absence of detailed crystallographic data, the structure of the NDH complex has remained obscure, and therefore the role of several NDH-associated nuclear-encoded proteins either as auxiliary proteins or structural subunits remains uncertain. In this review, we summarize the current knowledge on the subunit composition and assembly process of the chloroplast NDH complex. In addition, a novel oligomeric structure of NDH, the PSI/NDH supercomplex, is discussed.

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