Mitchell, P. (1961) Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism. Nature 191, 144-148, https://doi.org/10.1038/191144a0
Dröse, S. and Brandt, U. (2012) Molecular mechanisms of superoxide production by the mitochondrial respiratory chain. In Mitochondrial Oxidative Phosphorylation (Kadenbach, B., ed.), pp. 107-169, Springer
Guénebaut, V., Schlitt, A., Weiss, H., Leonard, K. and Friedrich, T. (1998) Consistent structure between bacterial and mitochondrial NADH:ubiquinone oxidoreductase (complex I). J. Mol. Biol. 276, 105-112, https://doi.org/10.1006/jmbi.1997.1518
Baradaran, R., Berrisford, J.M., Minhas, G.S. and Sazanov, L. aa (2013) Crystal structure of the entire respiratory complex I. Nature 494, 443-448, https://doi.org/10.1038/nature11871
Zickermann, V., Wirth, C., Nasiri, H., Siegmund, K., Schwalbe, H., Hunte, C. et al. (2015) Mechanistic insight from the crystal structure of mitochondrial complex I. Science 5, 4-10
Zhu, J., Vinothkumar, K.R. and Hirst, J. (2016) Structure of mammalian respiratory complex I. Nature 536, 354-358, https://doi.org/10.1038/nature19095
Vinothkumar, K.R., Zhu, J. and Hirst, J. (2014) Architecture of mammalian respiratory complex I. Nature 515, 80-84, https://doi.org/10.1038/nature13686
Fiedorczuk, K., Letts, J.A., Degliesposti, G., Kaszuba, K., Skehel, M. and Sazanov, L.A. (2016) Atomic structure of the entire mammalian mitochondrial complex I. Nature 538, 406-410, https://doi.org/10.1038/nature19794
Massoz, S., Cardol, P., González-Halphen, D. and Remacle, C. (2017) Mitochondrial bioenergetics pathways in Chlamydomonas. In Chlamydomonas: Molecular Genetics and Physiology (Hippler, M., ed.), pp. 59-95, Springer
Efremov, R.G., Baradaran, R. and Sazanov, L. a. (2010) The architecture of respiratory complex I. Nature 465, 441-445, https://doi.org/10.1038/nature09066
Berrisford, J.M., Baradaran, R. and Sazanov, L.A. (2016) Structure of bacterial respiratory complex I. Biochim. Biophys. Acta 1857, 892-901, https://doi.org/10.1016/j.bbabio.2016.01.012
Hirst, J., Carroll, J., Fearnley, I.M., Shannon, R.J. and Walker, J.E. (2003) The nuclear encoded subunits of complex I from bovine heart mitochondria. Biochim. Biophys. Acta 1604, 135-150, https://doi.org/10.1016/S0005-2728(03)00059-8
Ohnishi, T. (1998) Iron-sulfur clusters/semiquinones in complex I.. Biochim. Biophys. Acta 1364, 186-206, https://doi.org/10.1016/S0005-2728(98)00027-9
Brandt, U. (2011) A two-state stabilization-change mechanism for proton-pumping complex I. Biochim. Biophys. Acta 1807, 1364-1369, https://doi.org/10.1016/j.bbabio.2011.04.006
Hummer, G. and Wikström, M. (2016) Molecular simulation and modeling of complex I. Biochim. Biophys. Acta 1857, 915-921, https://doi.org/10.1016/j.bbabio.2016.01.005
Stepanova, A., Kahl, A., Konrad, C., Ten, V., Starkov, A.S. and Galkin, A. (2017) Reverse electron transfer results in a loss of flavin from mitochondrial complex I: Potential mechanism for brain ischemia reperfusion injury. J. Cereb. Blood Flow Metab. 37, 3649-3658, https://doi.org/10.1177/0271678X17730242
Wenz, T., Hielscher, R., Hellwig, P., Schägger, H., Richers, S. and Hunte, C. (2009) Role of phospholipids in respiratory cytochrome bc1 complex catalysis and supercomplex formation. Biochim. Biophys. Acta 1787, 609-616, https://doi.org/10.1016/j.bbabio.2009.02.012
Mitchell, P. (1975) The protonmotive Q cycle: a general formulation. FEBS Lett. 59, 137-139, https://doi.org/10.1016/0014-5793(75)80359-0
Zhang, Z., Huang, L., Shulmeister, V.M., Chi, Y.-I., Kim, K.K., Hung, L.-W. et al. (1998) Electron transfer by domain movement in cytochrome bc1. Nature 392, 677-684, https://doi.org/10.1038/33612
Hunte, C. (2003) Protonmotive pathways and mechanisms in the cytochrome bc1 complex. FEBS Lett. 545, 39-46, https://doi.org/10.1016/S0014-5793(03)00391-0
Xia, D., Esser, L., Tang, W.K., Zhou, F., Zhou, Y., Yu, L. et al. (2013) Structural analysis of cytochrome bc1 complexes: implications to the mechanism of function. Biochim. Biophys. Acta 1827, 1278-1294, https://doi.org/10.1016/j.bbabio.2012.11.008
Bleier, L. and Dröse, S. (2013) Superoxide generation by complex III: From mechanistic rationales to functional consequences. Biochim. Biophys. Acta 1827, 1320-1331, https://doi.org/10.1016/j.bbabio.2012.12.002
Dröse, S. (2013) Differential effects of complex II on mitochondrial ROS production and their relation to cardioprotective pre- and postconditioning. Biochim. Biophys. Acta 1827, 578-587, https://doi.org/10.1016/j.bbabio.2013.01.004
Quinlan, C.L., Orr, A.L., Perevoshchikova, I. V, Treberg, J.R., Ackrell, B.A. and Brand, M.D. (2012) Mitochondrial complex II can generate reactive oxygen species at high rates in both the forward and reverse reactions. J. Biol. Chem. 287, 27255-27264, https://doi.org/10.1074/jbc.M112.374629
Wong, H.S., Dighe, P.A., Mezera, V., Monternier, P.A. and Brand, M.D. (2017) Production of superoxide and hydrogen peroxide from specific mitochondrial sites under different bioenergetic conditions. J. Biol. Chem. 292, 16804-16809, https://doi.org/10.1074/jbc.R117.789271
Brand, M.D. (2016) Mitochondrial generation of superoxide and hydrogen peroxide as the source of mitochondrial redox signaling. Free Radic. Biol. Med. 100, 14-31, https://doi.org/10.1016/j.freeradbiomed.2016.04.001
Quinlan, C.L., Goncalves, R.L.S., Hey-Mogensen, M., Yadava, N., Bunik, V.I. and Brand, M.D. (2014) The 2-oxoacid dehydrogenase complexes in mitochondria can produce superoxide/hydrogen peroxide at much higher rates than complex I.. J. Biol. Chem. 289, 8312-8325, https://doi.org/10.1074/jbc.M113.545301
Schertl, P. and Braun, H.-P. (2014) Respiratory electron transfer pathways in plant mitochondria. Front. Plant Sci. 5, 163
Goncalves, R.L.S., Bunik, V.I. and Brand, M.D. (2016) Production of superoxide/hydrogen peroxide by the mitochondrial 2-oxoadipate dehydrogenase complex. Free Radic. Biol. Med. 91, 247-255, https://doi.org/10.1016/j.freeradbiomed.2015.12.020
Shen, W., Wei, Y., Dauk, M., Zheng, Z. and 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, https://doi.org/10.1016/S0014-5793(03)00033-4
Mráček, T., Drahota, Z. and Houštěk, J. (2013) The function and the role of the mitochondrial glycerol-3-phosphate dehydrogenase in mammalian tissues. Biochim. Biophys. Acta 1827, 401-410, https://doi.org/10.1016/j.bbabio.2012.11.014
Mráček, T., Holzerová, E., Drahota, Z., Kovářová, N., Vrbacký, M., Ješina, P. et al. (2014) ROS generation and multiple forms of mammalian mitochondrial glycerol-3-phosphate dehydrogenase. Biochim. Biophys. Acta 1837, 98-111, https://doi.org/10.1016/j.bbabio.2013.08.007
Orr, A.L., Quinlan, C.L., Perevoshchikova, I. V. and Brand, M.D. (2012) A refined analysis of superoxide production by mitochondrial sn-glycerol 3-phosphate dehydrogenase. J. Biol. Chem. 287, 42921-42935, https://doi.org/10.1074/jbc.M112.397828
Hey-Mogensen, M., Goncalves, R.L.S., Orr, A.L. and Brand, M.D. (2014) Production of superoxide/H2O2 by dihydroorotate dehydrogenase in rat skeletal muscle mitochondria. Free Radic. Biol. Med. 72, 149-155, https://doi.org/10.1016/j.freeradbiomed.2014.04.007
Watmough, N.J. and Frerman, F.E. (2010) The electron transfer flavoprotein: Ubiquinone oxidoreductases. Biochim. Biophys. Acta 1797, 1910-1916, https://doi.org/10.1016/j.bbabio.2010.10.007
Ayala, A., Munoz, M.F. and Arguelles, S. (2014) Lipid peroxidation: production, metabolism, and signaling mechanisms of malondialdehyde and 4-hydroxy-2-nonenal. Oxid. Med. Cell Longev. 2014, 360438, https://doi.org/10.1155/2014/360438
Adam-Vizi, V. (2005) Production of reactive oxygen species in brain mitochondria: contribution by electron transport chain and non-electron transport chain sources. Antioxid. Redox Signal. 7, 1140-1149, https://doi.org/10.1089/ars.2005.7.1140
Mittler, R., Vanderauwera, S., Suzuki, N., Miller, G., Tognetti, V.B., Vandepoele, K et al. (2011) ROS signaling: the new wave? Trends Plant Sci. 16, 300-309, https://doi.org/10.1016/j.tplants.2011.03.007
Aon, M.A., Cortassa, S. and O'Rourke, B. (2010) Redox-optimized ROS balance: a unifying hypothesis. Biochim. Biophys. Acta 1797, 865-877, https://doi.org/10.1016/j.bbabio.2010.02.016
Pozniakovsky, A.I., Knorre, D.A., Markova, O. V, Hyman, A.A., Skulachev, V.P. and Severin, F.F. (2005) Role of mitochondria in the pheromone- and amiodarone-induced programmed death of yeast. J. Cell Biol. 168, 257-269, https://doi.org/10.1083/jcb.200408145
Finkel, T. and Holbrook, N.J. (2000) Oxidants, oxidative stress and the biology of ageing. Nature 408, 239-247, https://doi.org/10.1038/35041687
Squarcina, A., Sorarù, A., Carraro, M., Geremia, S., Morosinotto, T. and Bonchio, M. (2017) Merged heme and non-heme manganese cofactors for a dual antioxidant surveillance in photosynthetic organisms. ACS Catal. 7, 1971-1976, https://doi.org/10.1021/acscatal.7b00004
Suzuki, Y.J., Carini, M. and Butterfield, D.A. (2010) Protein carbonylation. Antioxid. Redox Signal. 12, 323-325, https://doi.org/10.1089/ars.2009.2887
Browne, R.W. and Armstrong, D. (2000) HPLC analysis of lipid-derived polyunsaturated fatty acid peroxidation products in oxidatively modified human plasma. Clin. Chem. 46, 829-836
Schneider, C., Boeglin, W.E., Yin, H., Porter, N.A. and Brash, A.R. (2008) Intermolecular peroxyl radical reactions during autoxidation of hydroxy and hydroperoxy arachidonic acids generate a novel series of epoxidized products. Chem. Res. Toxicol. 21, 895-903, https://doi.org/10.1021/tx700357u
Bielski, B.H., Arudi, R.L. and Sutherland, M.W. (1983) A study of the reactivity of HO2/O2- with unsaturated fatty acids. J. Biol. Chem. 258, 4759-4761
Birben, E., Sahiner, U.M., Sackesen, C., Erzurum, S. and Kalayci, O. (2012) Oxidative stress and antioxidant defense. World Allergy Organ. J. 5, 9-19, https://doi.org/10.1097/WOX.0b013e3182439613
Cooke, M.S., Evans, M.D., Dizdaroglu, M. and Lunec, J. (2003) Oxidative DNA damage: mechanisms, mutation, and disease. FASEB J. 17, 1195-1214, https://doi.org/10.1096/fj.02-0752rev
Sheng, Y., Abreu, I.A., Cabelli, D.E., Maroney, M.J., Miller, A.F., Teixeira, M. et al. (2014) Superoxide dismutases and superoxide reductases. Chem. Rev. 114, 3854-3918, https://doi.org/10.1021/cr4005296
Fridovich, I. (1995) Superoxide radical and superoxide dismutases. Annu. Rev. Biochem. 64, 97-112, https://doi.org/10.1146/annurev.bi.64.070195.000525
Youn, H.D., Kim, E.J., Roe, J.H., Hah, Y.C. and Kang, S.O. (1996) A novel nickel-containing superoxide dismutase from Streptomyces spp. Biochem. J. 318, 889-896, https://doi.org/10.1042/bj3180889
Kowaltowski, A.J., de Souza-Pinto, N.C., Castilho, R.F. and Vercesi, A.E. (2009) Mitochondria and reactive oxygen species. Free Radic. Biol. Med. 47, 333-343, https://doi.org/10.1016/j.freeradbiomed.2009.05.004
Wolfe-Simon, F., Starovoytov, V., Reinfelder, J.R., Schofield, O. and Falkowski, P.G. (2006) Localization and role of manganese superoxide dismutase in a marine diatom. Plant Physiol. 142, 1701-1709, https://doi.org/10.1104/pp.106.088963
Ueda, M., Kinoshita, H., Maeda, S.I., Zou, W. and Tanaka, A. (2003) Structure-function study of the amino-terminal stretch of the catalase subunit molecule in oligomerization, heme binding, and activity expression. Appl. Microbiol. Biotechnol. 61, 488-494, https://doi.org/10.1007/s00253-003-1251-5
Gill, S.S. and Tuteja, N. (2010) Reactive oxygen species and antioxidant machinery in abiotic stress tolerance in crop plants. Plant Physiol. Biochem. 48, 909-930, https://doi.org/10.1016/j.plaphy.2010.08.016
Heazlewood, J.L., Tonti-Filippini, J.S., Gout, A.M., Day, D.A., Whelan, J. and Millar, A.H. (2004) Experimental analysis of the arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins. Plant Cell 16, 241-256, https://doi.org/10.1105/tpc.016055
Petrova, V.Y., Drescher, D., Kujumdzieva, A. V and Schmitt, M.J. (2004) Dual targeting of yeast catalase A to peroxisomes and mitochondria. Biochem. J. 380, 393-400, https://doi.org/10.1042/bj20040042
Mhamdi, A., Queval, G., Chaouch, S., Vanderauwera, S., Van Breusegem, F. and Noctor, G. (2010) Catalase function in plants: a focus on Arabidopsis mutants as stress-mimic models. J. Exp. Bot. 61, 4197-4220, https://doi.org/10.1093/jxb/erq282
Merchant, S.S., Prochnik, S.E., Vallon, O., Harris, E.H., Karpowicz, S.J., Witman, G.B. et al. (2007) The Chlamydomonas genome reveals the evolution of key animal and plant functions. Science 318, 245-250, https://doi.org/10.1126/science.1143609
Kato, J., Yamahara, T., Tanaka, K., Takio, S. and Satoh, T. (1997) Characterization of catalase from green algae Chlamydomonas reinhardtii. J. Plant Physiol. 151, 262-268, https://doi.org/10.1016/S0176-1617(97)80251-9
Atteia, A., Adrait, A., Brugire, S., Tardif, M., Van Lis, R., Deusch, O. et al. (2009) A proteomic survey of Chlamydomonas reinhardtii mitochondria sheds new light on the metabolic plasticity of the organelle and on the nature of the α-proteobacterial mitochondrial ancestor. Mol. Biol. Evol. 26, 1533-1548, https://doi.org/10.1093/molbev/msp068
Tardif, M., Atteia, A., Specht, M., Cogne, G., Rolland, N., Brugière, S. et al. (2012) Predalgo: a new subcellular localization prediction tool dedicated to green algae. Mol. Biol. Evol. 29, 3625-3639, https://doi.org/10.1093/molbev/mss178
Reumann, S., Chowdhary, G. and Lingner, T. (2016) Characterization, prediction and evolution of plant peroxisomal targeting signals type 1 (PTS1s). Biochim. Biophys. Acta 1863, 790-803, https://doi.org/10.1016/j.bbamcr.2016.01.001
Mittler, R. (2002) Oxidative stress, antioxidants and stress tolerance. Trends Plant Sci. 7, 405-410, https://doi.org/10.1016/S1360-1385(02)02312-9
Mittler, R., Vanderauwera, S., Gollery, M. and Van Breusegem, F. (2004) Reactive oxygen gene network of plants. Trends Plant Sci. 9, 490-498, https://doi.org/10.1016/j.tplants.2004.08.009
Smirnoff, N. (2018) Ascorbic acid metabolism and functions: a comparison of plants and mammals. Free Radic Biol Med., https://doi.org/10.1016/j.freeradbiomed.2018.03.033
Brigelius-Flohé, R. and Maiorino, M. (2013) Glutathione peroxidases. Biochim. Biophys. Acta 1830, 3289-3303, https://doi.org/10.1016/j.bbagen.2012.11.020
Miranda-Vizuete, A., Damdimopoulos, A.E. and Spyrou, G. (2000) The mitochondrial thioredoxin system. Antioxid. Redox Signal. 2, 801-810, https://doi.org/10.1089/ars.2000.2.4-801
Guerrero-Castillo, S., Cabrera-Orefice, A., Vázquez-Acevedo, M., González-Halphen, D. and Uribe-Carvajal, S. (2012) During the stationary growth phase, Yarrowia lipolytica prevents the overproduction of reactive oxygen species by activating an uncoupled mitochondrial respiratory pathway. Biochim. Biophys. Acta 1817, 353-362, https://doi.org/10.1016/j.bbabio.2011.11.007
Saha, B., Borovskii, G. and Panda, S.K. (2016) Alternative oxidase and plant stress tolerance. Plant Signal. Behav. 11, e1256530, https://doi.org/10.1080/15592324.2016.1256530
Feng, Y., Li, W., Li, J., Wang, J., Ge, J., Xu, D. et al. (2012) Structural insight into the type-II mitochondrial NADH dehydrogenases. Nature 491, 478-482, https://doi.org/10.1038/nature11541
Lecler, R., Vigeolas, H., Emonds-Alt, B., Cardol, P. and Remacle, C. (2012) Characterization of an internal type-II NADH dehydrogenase from chlamydomonas reinhardtii mitochondria. Curr. Genet. 58, 205-216
Del-Saz, N.F., Ribas-Carbo, M., McDonald, A.E., Lambers, H., Fernie, A.R. and Florez-Sarasa, I. (2017) An in vivo perspective of the role(s) of the alternative oxidase pathway. Trends Plant Sci. 23, 206-219, https://doi.org/10.1016/j.tplants.2017.11.006
Skovsen, E., Snyder, J.W., Lambert, J.D. and Ogilby, P.R. (2005) Lifetime and diffusion of singlet oxygen in a cell. J. Phys. Chem. B 109, 8570-8573, https://doi.org/10.1021/jp051163i
Wood, Z.A., Poole, L.B. and Karplus, P.A. (2003) Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling. Science 300, 650-653, https://doi.org/10.1126/science.1080405
Allen, R.G. and Tresini, M. (2000) Oxidative stress and gene regulation. Free Radic. Biol. Med. 28, 463-499, https://doi.org/10.1016/S0891-5849(99)00242-7
Huang, J., Willems, P., Van Breusegem, F. and Messens, J. (2018) Pathways crossing mammalian and plant sulfenomic landscapes. Free Radic. Biol. Med. 122, 193-201, https://doi.org/10.1016/j.freeradbiomed.2018.02.012
Reczek, C.R. and Chandel, N.S. (2015) ROS-dependent signal transduction. Curr. Opin. Cell Biol. 33, 8-13, https://doi.org/10.1016/j.ceb.2014.09.010
Schieber, M. and Chandel, N.S. (2014) ROS function in redox signaling and oxidative stress. Curr. Biol. 24, R453-R462, https://doi.org/10.1016/j.cub.2014.03.034
Truong, T.H. and Carroll, K.S. (2013) Redox regulation of protein kinases. Crit. Rev. Biochem. Mol. Biol. 48, 332-356, https://doi.org/10.3109/10409238.2013.790873
Roos, G. and Messens, J. (2011) Protein sulfenic acid formation: from cellular damage to redox regulation. Free Radic. Biol. Med. 51, 314-326, https://doi.org/10.1016/j.freeradbiomed.2011.04.031
Biteau, B., Labarre, J. and Toledano, M.B. (2003) ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin. Nature 425, 980-984, https://doi.org/10.1038/nature02075
Jonsson, T.J., Murray, M.S., Johnson, L.C. and Lowther, W.T. (2008) Reduction of cysteine sulfinic acid in peroxiredoxin by sulfiredoxin proceeds directly through a sulfinic phosphoryl ester intermediate. J. Biol. Chem. 283, 23846-23851, https://doi.org/10.1074/jbc.M803244200
Rey, P., Becuwe, N., Barrault, M.B., Rumeau, D., Havaux, M., Biteau, B. et al. (2007) The Arabidopsis thaliana sulfiredoxin is a plastidic cysteine-sulfinic acid reductase involved in the photooxidative stress response. Plant J. 49, 505-514, https://doi.org/10.1111/j.1365-313X.2006.02969.x
Jonsson, T.J., Tsang, A.W., Lowther, W.T. and Furdui, C.M. (2008) Identification of intact protein thiosulfinate intermediate in the reduction of cysteine sulfinic acid in peroxiredoxin by human sulfiredoxin. J. Biol. Chem. 283, 22890-22894, https://doi.org/10.1074/jbc.C800124200
Dixon, D.P., Skipsey, M., Grundy, N.M. and Edwards, R. (2005) Stress-induced protein S-glutathionylation in Arabidopsis. Plant Physiol. 138, 2233-2244, https://doi.org/10.1104/pp.104.058917
Liao, X. and Butow, R.A. (1993) RTG1 and RTG2: two yeast genes required for a novel path of communication from mitochondria to the nucleus. Cell 72, 61-71, https://doi.org/10.1016/0092-8674(93)90050-Z
Guha, M. and Avadhani, N.G. (2013) Mitochondrial retrograde signaling at the crossroads of tumor bioenergetics, genetics and epigenetics. Mitochondrion 13, 577-591, https://doi.org/10.1016/j.mito.2013.08.007
Starkov, A.A. (2008) The role of mitochondria in reactive oxygen species metabolism and signaling. Ann. N.Y. Acad. Sci. 1147, 37-52, https://doi.org/10.1196/annals.1427.015
Gordeeva, A. V, Zvyagilskaya, R.A. and Labas, Y.A. (2003) Cross-talk between reactive oxygen species and calcium in living cells. Biochem 68, 1077-1080
Adam-Vizi, V. and Starkov, A.A. (2010) Calcium and mitochondrial reactive oxygen species generation: how to read the facts. J. Alzheimers Dis. 20 (Suppl. 2), S413-S426, https://doi.org/10.3233/JAD-2010-100465
Zima, A. V and Blatter, L.A. (2006) Redox regulation of cardiac calcium channels and transporters. Cardiovasc. Res. 71, 310-321, https://doi.org/10.1016/j.cardiores.2006.02.019
Brookes, P.S., Yoon, Y., Robotham, J.L., Anders, M.W. and Sheu, S.S. (2004) Calcium, ATP, and ROS: a mitochondrial love-hate triangle. Am. J. Physiol. Cell Physiol. 287, C817-C833, https://doi.org/10.1152/ajpcell.00139.2004
Carden, T., Singh, B., Mooga, V., Bajpai, P. and Singh, K.K. (2017) Epigenetic modification of miR-663 controls mitochondria-to-nucleus retrograde signaling and tumor progression. J. Biol. Chem. 292, 20694-20706, https://doi.org/10.1074/jbc.M117.797001
Acín-Pérez, R., Carrascoso, I., Baixauli, F., Roche-Molina, M., Latorre-Pellicer, A., Fernández-Silva, P. et al. (2014) ROS-triggered phosphorylation of complex II by Fgr kinase regulates cellular adaptation to fuel use. Cell Metab. 19, 1020-1033, https://doi.org/10.1016/j.cmet.2014.04.015
Bleier, L., Wittig, I., Heide, H., Steger, M., Brandt, U. and Dröse, S. (2015) Generator-specific targets of mitochondrial reactive oxygen species. Free Radic. Biol. Med. 78, 1-10, https://doi.org/10.1016/j.freeradbiomed.2014.10.511
Nadtochiy, S.M., Baker, P.R., Freeman, B.A. and Brookes, P.S. (2009) Mitochondrial nitroalkene formation and mild uncoupling in ischaemic preconditioning: implications for cardioprotection. Cardiovasc. Res. 82, 333-340, https://doi.org/10.1093/cvr/cvn323
Schopfer, F.J., Batthyany, C., Baker, P.R., Bonacci, G., Cole, M.P., Rudolph, V. et al. (2009) Detection and quantification of protein adduction by electrophilic fatty acids: mitochondrial generation of fatty acid nitroalkene derivatives. Free Radic. Biol. Med. 46, 1250-1259, https://doi.org/10.1016/j.freeradbiomed.2008.12.025
Koenitzer, J.R. and Freeman, B.A. (2010) Redox signaling in inflammation: interactions of endogenous electrophiles and mitochondria in cardiovascular disease. Ann. N.Y. Acad. Sci. 1203, 45-52, https://doi.org/10.1111/j.1749-6632.2010.05559.x
Frohnert, B.I. and Bernlohr, D.A. (2013) Protein carbonylation, mitochondrial dysfunction, and insulin resistance. Adv. Nutr. 4, 157-163, https://doi.org/10.3945/an.112.003319
Curtis, J.M., Hahn, W.S., Stone, M.D., Inda, J.J., Droullard, D.J., Kuzmicic, J.P. et al. (2012) Protein carbonylation and adipocyte mitochondrial function. J. Biol. Chem. 287, 32967-32980, https://doi.org/10.1074/jbc.M112.400663
Bourges, I., Horan, S. and Meunier, B. (2005) Effect of inhibition of the bc1 complex on gene expression profile in yeast. J. Biol. Chem. 280, 29743-29749, https://doi.org/10.1074/jbc.M505915200
Delaunay, A., Isnard, A.D. and Toledano, M.B. (2000) H2O2 sensing through oxidation of the Yap1 transcription factor. EMBO J. 19, 5157-5166, https://doi.org/10.1093/emboj/19.19.5157
Bersweiler, A., D'Autreaux, B., Mazon, H., Kriznik, A., Belli, G., Delaunay-Moisan, A. et al. (2017) A scaffold protein that chaperones a cysteine-sulfenic acid in H2O2 signaling. Nat. Chem. Biol. 13, 909-915, https://doi.org/10.1038/nchembio.2412
Knorre, D., Sokolov, S., Zyrina, A. and Severin, F. (2016) How do yeast sense mitochondrial dysfunction. Microb. Cell 3, 532-539, https://doi.org/10.15698/mic2016.11.537
Woo, D.K., Green, P.D., Santos, J.H., D'Souza, A.D., Walther, Z., Martin, W.D. et al. (2012) Mitochondrial genome instability and ROS enhance intestinal tumorigenesis in APC(Min/+) mice. Am. J. Pathol. 180, 24-31, https://doi.org/10.1016/j.ajpath.2011.10.003
Singh, R.K., Srivastava, A., Kalaiarasan, P., Manvati, S., Chopra, R. and Bamezai, R.N. (2014) mtDNA germ line variation mediated ROS generates retrograde signaling and induces pro-cancerous metabolic features. Sci. Rep. 4, 6571, https://doi.org/10.1038/srep06571
Ogrunc, M., Di Micco, R., Liontos, M., Bombardelli, L., Mione, M., Fumagalli, M. et al. (2014) Oncogene-induced reactive oxygen species fuel hyperproliferation and DNA damage response activation. Cell Death Differ. 21, 998-1012, https://doi.org/10.1038/cdd.2014.16
Zhang, L., Zhou, L., Du, J., Li, M., Qian, C., Cheng, Y. et al. (2014) Induction of apoptosis in human multiple myeloma cell lines by ebselen via enhancing the endogenous reactive oxygen species production. Biomed. Res. Int. 2014, 696107
Wenzel, P., Schuhmacher, S., Kienhofer, J., Muller, J., Hortmann, M., Oelze, M. et al. (2008) Manganese superoxide dismutase and aldehyde dehydrogenase deficiency increase mitochondrial oxidative stress and aggravate age-dependent vascular dysfunction. Cardiovasc. Res. 80, 280-289, https://doi.org/10.1093/cvr/cvn182
Ekstrand, M.I., Falkenberg, M., Rantanen, A., Park, C.B., Gaspari, M., Hultenby, K. et al. (2004) Mitochondrial transcription factor A regulates mtDNA copy number in mammals. Hum. Mol. Genet. 13, 935-944, https://doi.org/10.1093/hmg/ddh109
Kunkel, G.H., Chaturvedi, P. and Tyagi, S.C. (2016) Mitochondrial pathways to cardiac recovery: TFAM. Heart Fail. Rev. 21, 499-517, https://doi.org/10.1007/s10741-016-9561-8
Wang, Y., Berkowitz, O., Selinski, J., Xu, Y., Hartmann, A. and Whelan, J. (2018) Stress responsive mitochondrial proteins in Arabidopsis thaliana. Free Radic. Biol. Med., https://doi.org/10.1016/j.freeradbiomed.2018.03.031
Fromm, S., Senkler, J., Eubel, H., Peterhänsel, C. and Braun, H.P. (2016) Life without complex I: proteome analyses of an Arabidopsis mutant lacking the mitochondrial NADH dehydrogenase complex. J. Exp. Bot. 67, 3079-3093, https://doi.org/10.1093/jxb/erw165
Wang, Y., Lyu, W., Berkowitz, O., Radomiljac, J.D., Law, S.R., Murcha, M.W. et al. (2016) Inactivation of mitochondrial complex I induces the expression of a twin cysteine protein that targets and affects cytosolic, chloroplastidic and mitochondrial function. Mol. Plant 9, 696-710, https://doi.org/10.1016/j.molp.2016.01.009
Gleason, C., Huang, S., Thatcher, L.F., Foley, R.C., Anderson, C.R., Carroll, A.J. et al. (2011) Mitochondrial complex II has a key role in mitochondrial-derived reactive oxygen species influence on plant stress gene regulation and defense. Proc. Natl. Acad. Sci. U.S.A. 108, 10768-10773, https://doi.org/10.1073/pnas.1016060108
Ng, S., Ivanova, A., Duncan, O., Law, S.R., Van Aken, O., De Clercq, I. et al. (2013) A membrane-bound NAC transcription factor, ANAC017, mediates mitochondrial retrograde signaling in Arabidopsis. Plant Cell 25, 3450-3471, https://doi.org/10.1105/tpc.113.113985
Larosa, V., Coosemans, N., Motte, P., Bonnefoy, N. and Remacle, C. (2012) Reconstruction of a human mitochondrial complex i mutation in the unicellular green alga Chlamydomonas. Plant J. 70, 759-768, https://doi.org/10.1111/j.1365-313X.2012.04912.x
Massoz, S., Larosa, V., Plancke, C., Lapaille, M., Bailleul, B., Pirotte, D. et al. (2014) Inactivation of genes coding for mitochondrial Nd7 and Nd9 complex I subunits in Chlamydomonas reinhardtii. Impact of complex I loss on respiration and energetic metabolism. Mitochondrion 19, 365-374, https://doi.org/10.1016/j.mito.2013.11.004
Remacle, C., Coosemans, N., Jans, F., Hanikenne, M., Motte, P. and Cardol, P. (2010) Knock-down of the COX3 and COX17 gene expression of cytochrome c oxidase in the unicellular green alga Chlamydomonas reinhardtii. Plant Mol. Biol. 74, 223-233
Roach, T., Na, C.S. and Krieger-Liszkay, A. (2015) High light-induced hydrogen peroxide production in Chlamydomonas reinhardtii is increased by high CO2 availability. Plant J. 81, 759-766, https://doi.org/10.1111/tpj.12768
Murik, O., Elboher, A. and Kaplan, A. (2014) Dehydroascorbate: a possible surveillance molecule of oxidative stress and programmed cell death in the green alga Chlamydomonas reinhardtii. New Phytol. 202, 471-484, https://doi.org/10.1111/nph.12649