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Respiratory electron transfer pathways in plant mitochondria

Peter Schertl, Hans-Peter Braun

Frontiers in Plant Science · 2014 · Review

doi:10.3389/fpls.2014.00163

Abstract

The respiratory electron transport chain (ETC) couples electron transfer from organic substrates onto molecular oxygen with proton translocation across the inner mitochondrial membrane. The resulting proton gradient is used by the ATP synthase complex for ATP formation. In plants, the ETC is especially intricate. Besides the "classical" oxidoreductase complexes (complex I-IV) and the mobile electron transporters cytochrome c and ubiquinone, it comprises numerous "alternative oxidoreductases." Furthermore, several dehydrogenases localized in the mitochondrial matrix and the mitochondrial intermembrane space directly or indirectly provide electrons for the ETC. Entry of electrons into the system occurs via numerous pathways which are dynamically regulated in response to the metabolic state of a plant cell as well as environmental factors. This mini review aims to summarize recent findings on respiratory electron transfer pathways in plants and on the involved components and supramolecular assemblies.

Full text

From PubMed Central, U.S. National Library of Medicine, as current on Oct 21, 2026. Paragraph numbers are ours, so an answer can point at one.

Introduction

During cellular respiration, organic compounds are oxidized to generate usable chemical energy in the form of ATP. The respiratory electron transport chain (ETC) of mitochondria is at the center of this process. Its core consists of four oxidoreductase complexes, the NADH dehydrogenase (complex I), the succinate dehydrogenase (complex II), the cytochrome c reductase (complex III) and the cytochrome c oxidase (complex IV), as well as of two mobile electron transporters, cytochrome c, and the lipid ubiquinone. Overall, electrons are transferred from the coenzymes NADH or FADH2 onto molecular oxygen which is reduced to water. Three of the four oxidoreductase complexes (complexes I, III and IV) couple their electron transfer reactions with proton translocation across the inner mitochondrial membrane. As a result, a proton gradient is formed which can be used by the ATP synthase complex (complex V) for the phosphorylation of ADP. In its classically described form, cellular respiration is based on a linear ETC (from NADH via complexes I, III, and IV to molecular oxygen). However, electrons can enter and leave the ETC at several alternative points. This is especially true for the plant ETC system, which is highly branched. In this review we aim to integrate current knowledge on the ETC system in plants with respect to its components, electron transport pathways and supramolecular structure.

Components of the plant ETC system

The “classical” oxidoreductase complexes of the respiratory chain (given in dark blue in Figure 1) resemble their homologues in animal mitochondria but at the same time have some clear distinctive features (reviewed in Millar et al.,,; Rasmusson and Moller,; van Dongen et al.,; Jacoby et al., ). Complex I is especially large in plant mitochondria and includes nearly 50 different subunits (Braun et al., ). Compared to its homologs from bacteria and other eukaryotic lineages it has an extra domain which includes carbonic anhydrase-like proteins. The function of this additional domain is currently unclear but it has been suggested to be important in the context of an inner-cellular CO2 transfer mechanism to provide mitochondrial CO2 for carbon fixation in chloroplasts (Braun and Zabaleta,; Zabaleta et al., ). Complex II is composed of four subunits in bacteria and mitochondria of animals and fungi. In plants complex II includes homologs of these subunits but additionally four extra proteins of unknown function (Millar et al.,; Huang and Millar, ). In contrast, the subunit composition of complex III from plants is highly similar to the ones in yeast and bovine mitochondria (Braun and Schmitz, ). The two largest subunits of this protein complex, termed “core proteins” in animals and fungi, are homologous to the two subunits of the mitochondrial processing peptidase (MPP) which removes pre-sequences of nuclear-encoded mitochondrial proteins after their import into mitochondria. In animal mitochondria, the core proteins are proteolytically inactive. Instead, an active MPP is present within the mitochondrial matrix. In contrast, the core subunits of complex III from plants have intact active sites (Braun et al.,; Glaser et al., ). Indeed, complex III isolated from plant mitochondria efficiently removes pre-sequences of mitochondrial pre-proteins. The differing functional states of complex III in diverse eukaryotic lineages might reflect different evolutionary stages of this protein complex (Braun and Schmitz, ). Also complex IV has some extra subunits in mitochondria of plants (Millar et al., ). Eight subunits are homologous to complex IV subunits from other groups of eukaryotes and another six putative subunits represent proteins of unknown functions.

The ETC of plant mitochondria additionally includes several so-called “alternative oxidoreductases”: the alternative oxidase (AOX; light blue in Figure 1) and several functionally distinguishable alternative NAD(P)H dehydrogenases (alternative NDs, light green in Figure 1). Findings on their functional roles have been reviewed recently (Rasmusson et al.,; Rasmusson and Moller,; Moore et al., ). AOX directly transfers electrons from ubiquinol to molecular oxygen and therefore constitutes an alternative electron exit point of the ETC. As a result, complexes III and IV are excluded from respiratory electron transport. The alternative NAD(P)H dehydrogenases serve as alternative electron entry points of the plant ETC and may substitute complex I. They differ with respect to co-factor requirement and localization at the outer or inner surface of the inner mitochondrial membrane (external alternative NDs, internal alternative NDs). Some of the genes encoding alternative NDs are activated by light (Rasmusson et al.,; Rasmusson and Moller, ). The latter enzymes are considered to be important during photorespiration and all alternative enzymes during various stress conditions. Since none of the alternative oxidoreductases couple electron transfer with proton translocation across the inner mitochondrial membrane, their enzymatic function is believed to be important in the context of an overflow protection mechanism for the ETC which is especially relevant during high-light conditions.

Finally, dehydrogenases (dark green in Figure 1; Table 1) can directly or indirectly insert electrons into the respiratory chain (Rasmusson et al.,; Rasmusson and Moller, ). Numerous dehydrogenases of the mitochondrial matrix generate NADH which is re-oxidized by complex I and the internal alternative NDs. However, some dehydrogenases directly transfer electrons onto ubiquinone [dihydroorotate dehydrogenase (DHODH), glyceraldehyde 3-phosphate dehydrogenase (G3-PDH) and possibly proline dehydrogenase (ProDH)] or onto cytochrome c [L-galactone-1,4-lactone dehydrogenase (GLDH) and D-lactate dehydrogenase (DLDH)]. Furthermore, at least two dehydrogenases [isovaleryl-coenzyme A dehydrogenase (IVDH) and D-2-hydroxyglutarate dehydrogenase (D-2HGDH)] transfer electrons onto ubiquinone via a short electron transfer chain composed of the “electron transfer flavoprotein” and the “electron transfer flavoprotein-ubiquinone oxidoreductase” (ETF and ETFQ-OR, purple in Figure 1) (Ishizaki et al.,,; Araújo et al., ). IVDH is involved in the branched chain amino acid catabolism and D-2HGDH in the catabolism of lysine. In plants, degradation of amino acids for respiration was shown to be especially important during carbon starvation conditions, e.g., extended darkness (Araújo et al., ). In contrast to animal mitochondria, fatty acid oxidation does not take place in plant mitochondria and the involved dehydrogenases consequently are absent. Instead, additional metabolic pathways occur in plants, e.g., the final step of an ascorbic acid biosynthesis pathway, which is catalyzed by GLDH. Electrons of L-galactono-1,4-lactone (GL) oxidation are inserted into the ETC via cytochrome c (Bartoli et al., ). Proline, besides being a building block for protein biosynthesis, is used as an osmolyte in plant cells. Proline is catabolized in mitochondria by a two-step process involving pyrroline-5-carboxylate dehydrogenase (P5CDH) and ProDH (Szabados and Savouré, ). P5CDH produces NADH, whereas ProDH represents a flavoenzyme which is assumed to transfer electrons directly or indirectly onto ubiquinone. Some additional dehydrogenases occur in plant mitochondria in the mitochondrial matrix and the intermembrane space which also contribute electrons to the ETC (Figure 1, Table 1). However, in some cases their mitochondrial localization is not entirely certain and should be further investigated by future research.

Electron entry pathways into the ETC

All electrons enter the ETC via NAD(P)H (generated by a variety of dehydrogenases in the mitochondrial matrix or the intermembrane space/the cytoplasm) or via flavine nucleotides (FADH2, FMNH2), which generally are bound to proteins termed flavoproteins. Consequently, the following electron entry pathways into the ETC can be defined: (i) the Matrix NAD(P)H pathway, (ii) the Matrix-FADH2 pathway, (iii) the Intermembrane-space-NAD(P)H pathway, and (iv) the Intermembrane-space-FADH2/FMDH2 pathway (Figure 2).

Different metabolic processes, which vary depending on the physiological state of the plant cell, contribute to the four electron entry pathways. During stable carbohydrate conditions, electrons for the respiratory chain can be supplied by NADH and FADH2 provided by the tricarboxylic acid (TCA) cycle. This is believed to be the standard mode of cellular respiration in non-green plant tissues or green tissues at night and resembles the basic situation in animal cells. However, during photosynthesis, NADH generation of the TCA cycle is reduced because some of its intermediates are used for anabolic reactions (reviewed in Sweetlove et al., ). Furthermore, the pyruvate dehydrogenase (PDH) complex is deactivated in plant mitochondria in the light by phosphorylation (Budde and Randall, ). At the same time photorespiration leads to an increase in NADH formation in the mitochondrial matrix by the activity of the glycine dehydrogenase complex (GDC). Indeed, at high-light conditions, NADH formed by GDC is believed to be the main substrate of the ETC, and not the NADH formed by the enzymes of the TCA cycle. At the same time, plant cells might become over-reduced in the presence of high-light. In this situation alternative oxidoreductases can insert excess electrons into the respiratory chain without contributing to the proton gradient. Upon carbon starvation conditions (e.g., extended darkness) electrons from the breakdown of amino acids are provided to the ETC (Araújo et al., ). Especially after release of salt stress the amino acid proline is used as an electron source (Szabados and Savouré, ). In summary, electron entry into the ETC is a highly flexible process in plants which much depends on light, the metabolic state of the cell as well as environmental stress factors.

Supramolecular structure of the ETC system

The ETC is based on defined protein-protein interactions. Most stable interactions occur within the four “classical” oxidoreductase complexes of the respiratory chain. Indeed, complexes I to IV can be isolated in intact form by various biochemical and electrophoretic procedures. Furthermore, several lines of evidence indicate that complexes I, III and IV interact within the inner mitochondrial membrane forming respiratory supercomplexes (reviewed in Dudkina et al., ). Complex I as well as complex IV associate with dimeric complex III (I + III2 and IV2 + III2 supercomplexes). An even larger supercomplex includes complexes I, III2, and IV and was proposed to be called “respirasome” because it can autonomously catalyzes the overall ETC reaction in the presence of ubiquinone and cytochrome c. The alternative oxidoreductases of the plant ETC seem not to be part of the respiratory supercomplexes. However, alternative NDs were found to be part of other protein complexes of about 160 kDa (Klodmann et al., ) or 150–700 kDa (Rasmusson and Agius, ).

Experimental data also indicate that several of the mitochondrial dehydrogenases form protein complexes. TCA cycle enzymes can assemble forming multienzyme clusters (Barnes and Weitzman, ). In addition, some of the mitochondrial dehydrogenases interact with ETC complexes, e.g., malate dehydrogenase has been reported to interact with complex I in animal mitochondria (Fukushima et al.,; see Braun et al., for review). Information on the native state of mitochondrial dehydrogenases furthermore comes from the GelMap project (Klodmann et al., ). Using 2D Blue native/SDS PAGE and systematic protein identifications, various dehydrogenases were described (Figure 3, Table 1). Native molecular mass of the dehydrogenases in many cases much exceeds the molecular mass of the monomeric proteins (Table 1, column 3). This indicates that probably most mitochondrial dehydrogenases form part of defined higher order structures.

Conclusion and outlook

Cellular respiration in plants is an especially dynamic system. The classical protein complexes of the ETC have extra functions and several alternative oxidoreductases occur. A network of mitochondrial dehydrogenases directly or indirectly supplies electrons for the respiratory chain. Insertion of electrons via various pathways is highly dependent on the metabolic state of the plant cell. The regulation of electron entry pathways into the respiratory chain is only partially understood and might, besides others, depend on the formation of supramolecular structures. Non-invasive experimental procedures will be necessary to physiologically investigate the function of these structures by future research.

Conflict of interest statement

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

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    Kiyosue T. Yoshiba Y. Yamaguchi-Shinozaki K. Shinozaki K. (1996 ). A nuclear gene encoding mitochondrial proline dehydrogenase, an enzyme involved in proline metabolism, is upregulated by proline but downregulated by dehydration in Arabidopsis. Plant Cell 8, 1323–1335

    Not in our library10.1105/tpc.8.8.1323

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    Klodmann J. Senkler M. Rode C. Braun H.-P. (2011 ). Defining the protein complex proteome of plant mitochondria. Plant Physiol. 157, 587–598

    Not in our library10.1104/pp.111.182352

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    Krömer S. (1995 ) Respiration during photosynthesis. Annu. Rev. Plant Physiol. Plant Mol. Biol. 46, 47–70

    Not in our library10.1146/annurev.pp.46.060195.000401

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    Lancien M. Gadal P. Hodges M. (1998 ). Molecular characterization of higher plant NAD-dependent isocitrate dehydrogenase: evidence for a heteromeric structure by the complementation of yeast mutants. Plant J. 16, 325–333

    Not in our library10.1046/j.1365-313x.1998.00305.x

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    Lee C. P. Eubel H. O'Toole N. Millar A. H. (2008 ). Heterogeneity of the mitochondrial proteome for photosynthetic and non-photosynthetic Arabidopsis metabolism. Mol. Cell Proteomics 7, 1297–1316

    Not in our library10.1074/mcp.m700535-mcp200

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    Leferink N. G. H. van den Berg W. A. M. van Berkel W. J. H. (2008 ). l-Galactono-gamma-lactone dehydrogenase from Arabidopsis thaliana, a flavoprotein involved in vitamin C biosynthesis. FEBS J. 275, 713–726

    Not in our library10.1111/j.1742-4658.2007.06233.x

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    Leferink N. G. H. van Duijn E. Barendregt A. Heck A. J. R. van Berkel W. J. H. (2009 ). Galactonolactone dehydrogenase requires a redox-sensitive thiol for optimal production of vitamin C. Plant Physiol. 150, 596–605

    Not in our library10.1104/pp.109.136929

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    Lemaitre T. Hodges M. (2006 ). Expression analysis of Arabidopsis thaliana NAD-dependent isocitrate dehydrogenase genes shows the presence of a functional subunit that is mainly expressed in the pollen and absent from vegetative organs. Plant Cell Physiol. 47, 634–643

    Not in our library10.1093/pcp/pcj030

  69. 69.

    Lemaitre T. Urbanczyk-Wochniak E. Flesch V. Bismuth E. Fernie A. R. Hodges M. (2007 ). NAD-dependent isocitrate dehydrogenase mutants of Arabidopsis suggest the enzyme is not limiting for nitrogen assimilation. Plant Physiol. 144, 1546–1558

    Not in our library10.1104/pp.107.100677

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    Lin M. Behal R. H. Oliver D. J. (2004 ) Characterization of a mutation in the IDH-II subunit of the NAD1-dependent isocitrate dehydrogenase from Arabidopsis thaliana. Plant Sci. 166, 983–988

    Not in our library10.1016/j.plantsci.2003.12.012

  71. 71.

    Luethy M. H. Miernyk J. A. Randall D. D. (1994 ). The nucleotide and deduced amino acid sequences of a cDNA encoding the E1 beta-subunit of the Arabidopsis thaliana mitochondrial pyruvate dehydrogenase complex. Biochim. Biophys. Acta 1187, 95–98

    Not in our library10.1016/0005-2728(94)90171-6

  72. 72.

    Mani S. van de Cotte B. van Montagu M. Verbruggen N. (2002 ). Altered levels of proline dehydrogenase cause hypersensitivity to proline and its analogs in Arabidopsis. Plant Physiol. 128, 73–83

    Not in our library10.1104/pp.010572

  73. 73.

    Mapson L. W. Breslow E. (1958 ). Biological synthesis of ascorbic acid: L-galactono-gamma-lactone dehydrogenase. Biochem. J. 68, 395–406

    Not in our library10.1042/bj0680395

  74. 74.

    Miersch J. Grancharov K. Krauss G. J. Spassovska N. Karamanov G. Maneva L. (1987 ). Biological activity and mode of action of some dihydroorotic and dihydroazaorotic acid derivatives. Biomed. Biochim. Acta 46, 307–315

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    Millar A. H. Eubel H. Jänsch L. Kruft V. Heazlewood J. L. Braun H.-P. (2004 ). Mitochondrial cytochrome c oxidase and succinate dehydrogenase complexes contain plant specific subunits. Plant Mol. Biol. 56, 77–90

    Not in our library10.1007/s11103-004-2316-2

  76. 76.

    Millar A. H. Hill S. A. Leaver C. J. (1999 ). Plant mitochondrial 2-oxoglutarate dehydrogenase complex: purification and characterization in potato. Biochem. J. 343(Pt 2), 327–334

    Not in our library10.1042/0264-6021:3430327

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    Millar A. H. Small I. D. Day D. A. Whelan J. (2008 ). Mitochondrial biogenesis and function in Arabidopsis. Arabidopsis Book 6, e0111

    Not in our library10.1199/tab.0111

  78. 78.

    Millar A. H. Whelan J. Soole K. L. Day D. A. (2011 ). Organization and regulation of 1822 mitochondrial respiration in plants. Annu. Rev. Plant Biol. 62, 79–104

    Not in our library10.1146/annurev-arplant-042110-103857

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    Miller G. Honig A. Stein H. Suzuki N. Mittler R. Zilberstein A. (2009 ). Unraveling delta1-pyrroline-5-carboxylate-proline cycle in plants by uncoupled expression of proline oxidation enzymes. J. Biol. Chem. 284, 26482–26492

    Not in our library10.1074/jbc.m109.009340

  80. 80.

    Miyashita Y. Good A. G. (2008a ). Glutamate deamination by glutamate dehydrogenase plays a central role in amino acid catabolism in plants. Plant Signal. Behav. 3, 842–843

    Not in our library10.4161/psb.3.10.5936

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    Miyashita Y. Good A. G. (2008b ). NAD(H)-dependent glutamate dehydrogenase is essential for the survival of Arabidopsis thaliana during dark-induced carbon starvation. J. Exp. Bot. 59, 667–680

    Not in our library10.1093/jxb/erm340

  82. 82.

    Mooney B. P. Henzl M. T. Miernyk J. A. Randall D. D. (2000 ). The dihydrolipoyl acyltransferase (BCE2) subunit of the plant branched-chain alpha-ketoacid dehydrogenase complex forms a 24-mer core with octagonal symmetry. Protein Sci. 9, 1334–1339

    Not in our library10.1110/ps.9.7.1334

  83. 83.

    Moore A. L. Shiba T. Young L. Harada S. Kita K. Ito K. (2013 ). Unraveling the heater: new insights into the structure of the alternative oxidase. Annu. Rev. Plant Biol. 64, 637–663

    Not in our library10.1146/annurev-arplant-042811-105432

  84. 84.

    Nagai A. Scheidegger A. (1991 ). Purification and characterization of histidinol dehydrogenase from cabbage. Arch. Biochem. Biophys. 284, 127–132

    Not in our library10.1016/0003-9861(91)90274-m

  85. 85.

    Nunes-Nesi A. Carrari F. Lytovchenko A. Smith A. M. O. Loureiro M. E. Ratcliffe R. G. (2005 ). Enhanced photosynthetic performance and growth as a consequence of decreasing mitochondrial malate dehydrogenase activity in transgenic tomato plants. Plant Physiol. 137, 611–622

    Not in our library10.1104/pp.104.055566

  86. 86.

    Oguchi K. Tanaka N. Komatsu S. Akao S. (2004 ). Methylmalonate-semialdehyde dehydrogenase is induced in auxin-stimulated and zinc-stimulated root formation in rice. Plant Cell Rep. 22, 848–858

    Not in our library10.1007/s00299-004-0778-y

  87. 87.

    Oliver D. J. (1994 ) The glycine decarboxylase complex from plant mitochondria. Annu. Rev.Plant Physiol. Plant Mol. Biol. 45, 323–338

    Not in our library10.1146/annurev.pp.45.060194.001543

  88. 88.

    Oliver D. J. Neuburger M. Bourguignon J. Douce R. (1990 ). Interaction between the component enzymes of the glycine decarboxylase multienzyme complex. Plant Physiol. 94, 833–839

    Not in our library10.1104/pp.94.2.833

  89. 89.

    Olson B. J. Skavdahl M. Ramberg H. Osterman J. C. Markwell J. (2000 ). Formate dehydrogenase in Arabidopsis thaliana: characterization and possible targeting to the chloroplast. Plant Sci. 159, 205–212

    Not in our library10.1016/s0168-9452(00)00337-x

  90. 90.

    Pineau B. Layoune O. Danon A. de Paepe R. (2008 ). L-galactono-1,4-lactone dehydrogenase is required for the accumulation of plant respiratory complex I. J. Biol. Chem. 283, 32500–32505

    Not in our library10.1074/jbc.m805320200

  91. 91.

    Poulsen L. L. Wedding R. T. (1970 ). Purification and properties of the alpha-ketoglutarate dehydrogenase complex of cauliflower mitochondria. J. Biol. Chem. 245, 5709–5717

    Not in our library

  92. 92.

    Rasmusson A. G. Agius S. C. (2001 ) Rotenone-insensitive NAD(P)H dehydrogenases in plants: immunodetection and distribution of native proteins in mitochondria. Plant Physiol. Biochem. 39, 1057–1066

    Not in our library10.1016/s0981-9428(01)01334-1

  93. 93.

    Rasmusson A. G. Geisler D. A. Møller I. M. (2008 ). The multiplicity of dehydrogenases in the electron transport chain of plant mitochondria. Mitochondrion 8, 47–60

    Not in our library10.1016/j.mito.2007.10.004

  94. 94.

    Rasmusson A. G. Moller I. M. (2011 ). Mitochondrial electron transport and plant stress, in Plant Mitochondria, ed Kempken F. (New York, NY: Springer), 357–381

    Not in our library

  95. 95.

    Rasmusson A. G. Soole K. L. Elthon T. E. (2004 ). Alternative NAD(P)H dehydrogenases of plant mitochondria. Annu. Rev. Plant Biol. 55, 23–39

    Not in our library10.1146/annurev.arplant.55.031903.141720

  96. 96.

    Reinard T. Janke V. Willard J. Buck F. Jacobsen H. J. Vockley J. (2000 ). Cloning of a gene for an acyl-CoA dehydrogenase from Pisum sativum L. and purification and characterization of its product as an isovaleryl-CoA dehydrogenase. J. Biol. Chem. 275, 33738–33743

    Not in our library10.1074/jbc.m004178200

  97. 97.

    Schertl P. Cabassa C. Saadallah K. Bordenave M. Savouré A. Braun H.P. (in press ). Biochemical characterization of ProDH activity in Arabidopsis mitochondria. FEBS J.

    Not in our library10.1111/febs.12821

  98. 98.

    Schertl P. Sunderhaus S. Klodmann J. Grozeff G. E. G. Bartoli C. G. Braun H.-P. (2012 ). L-galactono-1,4-lactone dehydrogenase (GLDH) forms part of three subcomplexes of mitochondrial complex I in Arabidopsis thaliana. J. Biol. Chem. 287, 14412–14419

    Not in our library10.1074/jbc.m111.305144

  99. 99.

    Sharma S. Verslues P. E. (2010 ). Mechanisms independent of abscisic acid (ABA) or proline feedback have a predominant role in transcriptional regulation of proline metabolism during low water potential and stress recovery. Plant Cell Environ. 33, 1838–1851

    Not in our library10.1111/j.1365-3040.2010.02188.x

  100. 100.

    Shen W. Wei Y. Dauk M. Tan Y. Taylor D. C. Selvaraj G. (2006 ). Involvement of a glycerol-3-phosphate dehydrogenase in modulating the NADH/NAD+ ratio provides evidence of a mitochondrial glycerol-3-phosphate shuttle in Arabidopsis. Plant Cell 18, 422–441

    Not in our library10.1105/tpc.105.039750

  101. 101.

    Shen W. Wei Y. Dauk M. Zheng Z. Zou J. (2003 ). Identification of a mitochondrial glycerol-3-phosphate dehydrogenase from Arabidopsis thaliana: evidence for a mitochondrial glycerol-3-phosphate shuttle in plants. FEBS Lett. 536, 92–96

    Not in our library10.1016/s0014-5793(03)00033-4

  102. 102.

    Siendones E. Gonzalez-Reyes J. A. Santos-Ocana C. Navas P. C rdoba F. (1999 ). Biosynthesis of ascorbic acid in kidney bean. L-galactono-gamma-lactone dehydrogenase is an intrinsic protein located at the mitochondrial inner membrane. Plant Physiol. 120, 907–912

    Not in our library10.1104/pp.120.3.907

  103. 103.

    Somerville C. R. Ogren W. L. (1982 ). Mutants of the cruciferous plant Arabidopsis thaliana lacking glycine decarboxylase activity. Biochem. J. 202, 373–380

    Not in our library10.1042/bj2020373

  104. 104.

    Srinivasan R. Oliver D. J. (1995 ). Light-dependent and tissue-specific expression of the H-protein of the glycine decarboxylase complex. Plant Physiol. 109, 161–168

    Not in our library10.1104/pp.109.1.161

  105. 105.

    Sweetlove L. J. Beard K. F. M. Nunes-Nesi A. Fernie A. R. Ratcliffe R. G. (2010 ). Not just a circle: flux modes in the plant TCA cycle. Trends Plant Sci. 15, 462–470

    Not in our library10.1016/j.tplants.2010.05.006

  106. 106.

    Szabados L. Savouré A. (2010 ). Proline: a multifunctional amino acid. Trends Plant Sci. 15, 89–97

    Not in our library10.1016/j.tplants.2009.11.009

  107. 107.

    Szurmak B. Strokovskaya L. Mooney B. P. Randall D. D. Miernyk J. A. (2003 ). Expression and assembly of Arabidopsis thaliana pyruvate dehydrogenase in insect cell cytoplasm. Protein Expr. Purif. 28, 357–361

    Not in our library10.1016/s1046-5928(02)00712-x

  108. 108.

    Tanaka N. Takahashi H. Kitano H. Matsuoka M. Akao S. Uchimiya H. (2005 ). Proteome approach to characterize the methylmalonate-semialdehyde dehydrogenase that is regulated by gibberellin. J. Proteome Res. 4, 1575–1582

    Not in our library10.1021/pr050114f

  109. 109.

    Tarasenko V. I. Garnik E. Y. Konstantinov Y. M. (2013 ). Rate of alternative electron transport in arabidopsis mitochondria affects the expression of the glutamate dehydrogenase gene gdh2. Dokl. Biochem. Biophys. 452, 234–236

    Not in our library10.1134/s1607672913050037

  110. 110.

    Taylor N. L. Heazlewood J. L. Day D. A. Millar A. H. (2004 ). Lipoic acid-dependent oxidative catabolism of alpha-keto acids in mitochondria provides evidence for branched-chain amino acid catabolism in Arabidopsis. Plant Physiol. 134, 838–848

    Not in our library10.1104/pp.103.035675

  111. 111.

    Tomaz T. Bagard M. Pracharoenwattana I. Lindén P. Lee C. P. Carroll A. J. (2010 ). Mitochondrial malate dehydrogenase lowers leaf respiration and alters photorespiration and plant growth in Arabidopsis. Plant Physiol. 154, 1143–1157

    Not in our library10.1104/pp.110.161612

  112. 112.

    Tovar-Méndez A. Miernyk J. A. Randall D. D. (2003 ) Regulation of pyruvate dehydrogenase complex activity in plant cells. Eur. J. Biochem. 270, 1043–1049

    Not in our library10.1046/j.1432-1033.2003.03469.x

  113. 113.

    Toyokura K. Watanabe K. Oiwaka A. Kusano M. Tameshige T. Tatematsu K. (2011 ). Succinic semialdehyde dehydrogenase is involved in the robust patterning of Arabidopsis leaves along the adaxial-abaxial axis. Plant Cell Physiol. 52, 1340–1353

    Not in our library10.1093/pcp/pcr079

  114. 114.

    Tronconi M. A. Fahnenstich H. Gerrard Weehler M. C. Andreo C. S. Flügge U.-I. Drincovich M. F. (2008 ). Arabidopsis NAD-malic enzyme functions as a homodimer and heterodimer and has a major impact on nocturnal metabolism. Plant Physiol. 146, 1540–1552

    Not in our library10.1104/pp.107.114975

  115. 115.

    Tronconi M. A. Gerrard Wheeler M. C. Drincovich M. F. Andreo C. S. (2012 ). Differential fumarate binding to Arabidopsis NAD+-malic enzymes 1 and -2 produces an opposite activity modulation. Biochimie 94, 1421–1430

    Not in our library10.1016/j.biochi.2012.03.017

  116. 116.

    Tronconi M. A. Maurino V. G. Andreo C. S. Drincovich M. F. (2010 ). Three different and tissue-specific NAD-malic enzymes generated by alternative subunit association in Arabidopsis thaliana. J. Biol. Chem. 285, 11870–11879

    Not in our library10.1074/jbc.m109.097477

  117. 117.

    Turano F. J. Thakkar S. S. Fang T. Weisemann J. M. (1997 ). Characterization and expression of NAD(H)-dependent glutamate dehydrogenase genes in Arabidopsis. Plant Physiol. 113, 1329–1341

    Not in our library10.1104/pp.113.4.1329

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    Ullrich A. Knecht W. Piskur J. Löffler M. (2002 ). Plant dihydroorotate dehydrogenase differs significantly in substrate specificity and inhibition from the animal enzymes. FEBS Lett. 529, 346–350

    Not in our library10.1016/s0014-5793(02)03425-7

  119. 119.

    van Dongen J. T. Gupta K. J. Ramírez-Aguilar S. J. Araújo W. L. Nunes-Nesi A. Fernie A. R. (2011 ). Regulation of respiration in plants: a role for alternative metabolic pathways. J. Plant Physiol. 168, 1434–1443

    Not in our library10.1016/j.jplph.2010.11.004

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    Verbruggen N. Hua X. J. May M. van Montagu M. (1996 ). Environmental and developmental signals modulate proline homeostasis: evidence for a negative transcriptional regulator. Proc. Natl. Acad. Sci. U.S.A. 93, 8787–8791

    Not in our library10.1073/pnas.93.16.8787

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    Wallström S. V. Florez-Sarasa I. Araújo W. L. Aidemark M. Fernández-Fernández M. Fernie A. R. (2014a ). Suppression of the external mitochondrial NADPH dehydrogenase, NDB1, in Arabidopsis thaliana affects central metabolism and vegetative growth. Mol. Plant 7, 356–368

    Not in our library10.1093/mp/sst115

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    Wallström S. V. Florez-Sarasa I. Araújo W. L. Escobar M. A. Geisler D. A. Aidemark M. (2014b ). Suppression of NDA-type alternative mitochondrial NAD(P)H dehydrogenases in Arabidopsis thaliana modifies growth and metabolism, but not high light stimulation of mitochondrial electron transport. Plant Cell Physiol. [Epub ahead of print].

    Not in our library10.1093/pcp/pcu021

  123. 123.

    Wedding R. T. Black M. K. (1971a ). Evidence for tighter binding of magnesium-thiamine pyrophosphate to -ketoglutarate dehydrogenase when activated by adenosine monophosphate. J. Biol. Chem. 246, 4097–4099

    Not in our library

  124. 124.

    Wedding R. T. Black M. K. (1971b ). Nucleotide activation of cauliflower alpha-ketoglutarate dehydrogenase. J. Biol. Chem. 246, 1638–1643

    Not in our library

  125. 125.

    Wienstroer J. Engqvist M. K. M. Kunz H.-H. Flügge U.-I. Maurino V. G. (2012 ). D-Lactate dehydrogenase as a marker gene allows positive selection of transgenic plants. FEBS Lett. 586, 36–40

    Not in our library10.1016/j.febslet.2011.11.020

  126. 126.

    Wulff A. Oliveira H. C. Saviani E. E. Salgado I. (2009 ) Nitrite reduction and superoxide-dependent nitric oxide degradation by Arabidopsis mitochondria: influence of external NAD(P)H dehydrogenases and alternative oxidase in the control of nitric oxide levels. Nitric Oxide 21, 132–139

    Not in our library10.1016/j.niox.2009.06.003

  127. 127.

    Yamaya T. Oaks A. Matsumoto H. (1984 ). Characteristics of glutamate dehydrogenase in mitochondria prepared from corn shoots. Plant Physiol. 76, 1009–1013

    Not in our library10.1104/pp.76.4.1009

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    Yu H. Du X. Zhang F. Zhang F. Hu Y. Liu S. (2012 ). A mutation in the E2 subunit of the mitochondrial pyruvate dehydrogenase complex in Arabidopsis reduces plant organ size and enhances the accumulation of amino acids and intermediate products of the TCA cycle. Planta 236, 387–399

    Not in our library10.1007/s00425-012-1620-3

  129. 129.

    Zabaleta E. Martin M. V. Braun H.-P. (2012 ). A basal carbon concentrating mechanism in plants? Plant Sci. 187, 97–104

    Not in our library10.1016/j.plantsci.2012.02.001

  130. 130.

    Zhu X. Tang G. Galili G. (2000 ) Characterization of the two saccharopine dehydrogenase isozymes of lysine catabolism encoded by the single composite AtLKR=SDH locus of Arabidopsis. Plant Physiol. 124, 1363–1372

    Not in our library10.1104/pp.124.3.1363

  131. 131.

    Zou J. Qi Q. Katavic V. Marillia E. F. Taylor D. C. (1999 ). Effects of antisense repression of an Arabidopsis thaliana pyruvate dehydrogenase kinase cDNA on plant development. Plant Mol. Biol. 41, 837–849

    Not in our library10.1023/a:1006393726018

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