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Plant Physiol, January 2003, Vol. 131, pp. 264-275
Functional Mitochondrial Complex I Is Required by Tobacco Leaves
for Optimal Photosynthetic Performance in Photorespiratory Conditions
and during Transients1
Christelle
Dutilleul,
Simon
Driscoll,
Gabriel
Cornic,
Rosine
De Paepe,
Christine H.
Foyer, and
Graham
Noctor*
Institut de Biotechnologie des Plantes (C.D., R.D.P., G.N.) and
Laboratoire d'Ecophysiologie Végétale (G.C.),
Université de Paris XI, 91405 Orsay cedex, France; and Crop
Performance and Improvement Division, Rothamsted Research, Harpenden,
Hertfordshire AL5 2JQ, United Kingdom (S.D., C.H.F.)
The importance of the mitochondrial electron transport chain
in photosynthesis was studied using the tobacco (Nicotiana
sylvestris) mutant CMSII, which lacks functional complex I. Rubisco activities and oxygen evolution at saturating CO2
showed that photosynthetic capacity in the mutant was at least as high
as in wild-type (WT) leaves. Despite this, steady-state photosynthesis
in the mutant was reduced by 20% to 30% at atmospheric
CO2 levels. The inhibition of photosynthesis was alleviated
by high CO2 or low O2. The mutant showed a
prolonged induction of photosynthesis, which was exacerbated in
conditions favoring photorespiration and which was accompanied by
increased extractable NADP-malate dehydrogenase activity. Feeding experiments with leaf discs demonstrated that CMSII had a lower capacity than the WT for glycine (Gly) oxidation in the dark. Analysis
of the postillumination burst in CO2 evolution showed that
this was not because of insufficient Gly decarboxylase capacity. Despite the lower rate of Gly metabolism in CMSII leaves in the dark,
the Gly to Ser ratio in the light displayed a similar dependence on
photosynthesis to the WT. It is concluded that: (a) Mitochondrial complex I is required for optimal photosynthetic performance, despite
the operation of alternative dehydrogenases in CMSII; and (b) complex I
is necessary to avoid redox disruption of photosynthesis in conditions
where leaf mitochondria must oxidize both respiratory and
photorespiratory substrates simultaneously.
1
This work was supported by the European Union
and by the British Council ALLIANCE/French Ministry of Education
EGIDE grant for exchange between French and UK researchers.
*
Corresponding author; e-mail noctor{at}ibp.u-psud.fr; fax
33-1-69-15-34-25.
© 2003 American Society of Plant Biologists
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