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nature.com
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(en) Heather J. Painter, Joanne M. Morrisey, Michael W. Mather et Akhil B. Vaidya, « Specific role of mitochondrial electron transport in blood-stage Plasmodium falciparum », Nature, vol. 446, no 7131, , p. 88-91 (PMID17330044, DOI10.1038/nature05572, Bibcode2007Natur.446...88P, lire en ligne)
(en) Karim S. Echtay, Damien Roussel, Julie St-Pierre, Mika B. Jekabsons, Susana Cadenas, Jeff A. Stuart, James A. Harper, Stephen J. Roebuck, Alastair Morrison, Susan Pickering, John C. Clapham et Martin D. Brand, « Superoxide activates mitochondrial uncoupling proteins », Nature, vol. 415, no 6867, , p. 96-99 (PMID11780125, DOI10.1038/415096a, Bibcode2002Natur.415...96E, lire en ligne)
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(en) Deborah C. Johnson, Dennis R. Dean, Archer D. Smith et Michael K. Johnson, « STRUCTURE, FUNCTION, AND FORMATION OF BIOLOGICAL IRON-SULFUR CLUSTERS », Annual Review of Biochemistry, vol. 74, , p. 247-281 (PMID15952888, DOI10.1146/annurev.biochem.74.082803.133518, lire en ligne)
(en) David Leys et Nigel S Scrutton, « Electrical circuitry in biology: emerging principles from protein structure », Current Opinion in Structural Biology, vol. 14, no 6, , p. 642-647 (PMID15582386, DOI10.1016/j.sbi.2004.10.002, lire en ligne)
(en) Christopher C. Page, Christopher C. Moser, Xiaoxi Chen et P. Leslie Dutton, « Natural engineering principles of electron tunnelling in biological oxidation–reduction », Nature, vol. 402, no 6757, , p. 47-52 (PMID10573417, DOI10.1038/46972, Bibcode1999Natur.402...47P, lire en ligne)
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(en) Giorgio Lenaz, Romana Fato, Maria Luisa Genova, Christian Bergamini, Cristina Bianchi et Annalisa Biondi, « Mitochondrial Complex I: Structural and functional aspects », Biochimica et Biophysica Acta (BBA) - Bioenergetics, vol. 1757, nos 9-10, , p. 1406-1420 (PMID16828051, DOI10.1016/j.bbabio.2006.05.007, lire en ligne)
(en) Ekaterina A. Baranova, Peter J. Holt et Leonid A. Sazanov, « Projection Structure of the Membrane Domain of Escherichia coli Respiratory Complex I at 8 Å Resolution », Journal of Molecular Biology, vol. 366, no 1, , p. 140-154 (PMID17157874, DOI10.1016/j.jmb.2006.11.026, lire en ligne)
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(en) Victoria Yankovskaya, Rob Horsefield, Susanna Törnroth, César Luna-Chavez, Hideto Miyoshi, Christophe Léger, Bernadette Byrne, Gary Cecchini et So Iwata, « Architecture of Succinate Dehydrogenase and Reactive Oxygen Species Generation », Science, vol. 299, no 5607, , p. 700-704 (PMID12560550, DOI10.1126/science.1079605, Bibcode2003Sci...299..700Y, lire en ligne)
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(en) Heather J. Painter, Joanne M. Morrisey, Michael W. Mather et Akhil B. Vaidya, « Specific role of mitochondrial electron transport in blood-stage Plasmodium falciparum », Nature, vol. 446, no 7131, , p. 88-91 (PMID17330044, DOI10.1038/nature05572, Bibcode2007Natur.446...88P, lire en ligne)
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(en) Kimitsune Ishizaki, Tony R. Larson, Nicolas Schauer, Alisdair R. Fernie, Ian A. Graham et Christopher J. Leaver, « The Critical Role of Arabidopsis Electron-Transfer Flavoprotein:Ubiquinone Oxidoreductase during Dark-Induced Starvation », American Society of Plant Biologists, vol. 17, no 9, , p. 2587-2600 (PMID16055629, PMCID1197437, DOI10.1105/tpc.105.035162, lire en ligne)
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(en) Bernard L. Trumpower, « The protonmotive Q cycle. Energy transduction by coupling of proton translocation to electron transfer by the cytochrome bc1 complex », Journal of Biological Chemistry, vol. 265, no 20, , p. 11409-11412 (PMID2164001, lire en ligne)
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(en) Melissa W. Calhoun, Jeffrey W. Thomas et Robert B. Gennis, « The cytochrome oxidase superfamily of redox-driven proton pumps », Trends in Biochemical Sciences, vol. 19, no 8, , p. 325-330 (PMID7940677, DOI10.1016/0968-0004(94)90071-X, lire en ligne)
(en) Tomitake Tsukihara, Hiroshi Aoyama, Eiki Yamashita, Takashi Tomizaki, Hiroshi Yamaguchi, Kyoko Shinzawa-Itoh, Ryosuke Nakashima, Rieko Yaono et Shinya Yoshikawa, « The Whole Structure of the 13-Subunit Oxidized Cytochrome c Oxidase at 2.8 Å », Science, vol. 272, no 5265, , p. 1136-1144 (PMID8638158, DOI10.1126/science.272.5265.1136, Bibcode1996Sci...272.1136T, lire en ligne)
(en) Shinya Yoshikawa, Kazumasa Muramoto, Kyoko Shinzawa-Itoh, Hiroshi Aoyama, Tomitake Tsukihara, Kunitoshi Shimokata, Yukie Katayama et Hideo Shimada, « Proton pumping mechanism of bovine heart cytochrome c oxidase », Biochimica et Biophysica Acta (BBA) - Bioenergetics, vol. 1757, nos 9-10, , p. 1110-1116 (PMID16904626, DOI10.1016/j.bbabio.2006.06.004, lire en ligne)
(en) R. Ian Menz et David A. Day, « Purification and Characterization of a 43-kDa Rotenone-insensitive NADH Dehydrogenase from Plant Mitochondria », Journal of Biological Chemistry, vol. 271, no 38, , p. 23117-23120 (PMID8798503, DOI10.1074/jbc.271.38.23117, lire en ligne)
(en) Allison E. McDonald et Greg C. Vanlerberghe, « Branched Mitochondrial Electron Transport in the Animalia: Presence of Alternative Oxidase in Several Animal Phyla », IUBMB Life, vol. 56, no 6, , p. 333-341 (PMID15370881, DOI10.1080/1521-6540400000876, lire en ligne)
(en) F. E. Sluse et W. Jarmuszkiewicz, « Alternative oxidase in the branched mitochondrial respiratory network: an overview on structure, function, regulation, and role », Brazilian Journal of Medical and Biological Research, vol. 31, no 6, , p. 733-747 (PMID9698817, DOI10.1590/S0100-879X1998000600003, lire en ligne)
(en) Anthony L. Moore et James N. Siedow, « The regulation and nature of the cyanide-resistant alternative oxidase of plant mitochondria », Biochimica et Biophysica Acta (BBA) - Bioenergetics, vol. 1059, no 2, , p. 121-140 (PMID1883834, DOI10.1016/S0005-2728(05)80197-5, lire en ligne)
(en) Greg C. Vanlerberghe et Lee McIntosh, « ALTERNATIVE OXIDASE: From Gene to Function », Annual Review of Plant Physiology and Plant Molecular Biology, vol. 48, , p. 703-734 (PMID15012279, DOI10.1146/annurev.arplant.48.1.703, lire en ligne)
(en) Yusuke Ito, Daisuke Saisho, Mikio Nakazono, Nobuhiro Tsutsumi et Atsushi Hirai, « Transcript levels of tandem-arranged alternative oxidase genes in rice are increased by low temperature », Gene, vol. 203, no 2, , p. 121-129 (PMID9426242, DOI10.1016/S0378-1119(97)00502-7, lire en ligne)
(en) Denis P. Maxwell, Yong Wang et Lee McIntosh, « The alternative oxidase lowers mitochondrial reactive oxygen production in plant cells », Proceedings of the National Academy of Sciences of the United States of America, vol. 96, no 14, , p. 8271-8276 (PMID10393984, PMCID22224, DOI10.1073/pnas.96.14.8271, Bibcode1999PNAS...96.8271M, lire en ligne)
(en) Jesco Heinemeyer, Hans-Peter Braun, Egbert J. Boekema et Roman Kouřil, « A Structural Model of the Cytochrome c Reductase/Oxidase Supercomplex from Yeast Mitochondria », Journal of Biological Chemistry, vol. 282, no 16, , p. 12240-12248 (PMID17322303, DOI10.1074/jbc.M610545200, lire en ligne)
(en) S. Gupte, E. S. Wu, L. Hoechli, M. Hoechli, K. Jacobson, A. E. Sowers et C. R. Hackenbrock, « Relationship between lateral diffusion, collision frequency, and electron transfer of mitochondrial inner membrane oxidation-reduction components », Proceedings of the National Academy of Sciences of the United States of America, vol. 81, no 9, , p. 2606-2610 (PMID6326133, PMCID345118, DOI10.1073/pnas.81.9.2606, Bibcode1984PNAS...81.2606G, lire en ligne)
(en) Hermann Schägger, « Respiratory chain supercomplexes of mitochondria and bacteria », Biochimica et Biophysica Acta (BBA) - Bioenergetics, vol. 1555, nos 1-3, , p. 154-159 (PMID12206908, DOI10.1016/S0005-2728(02)00271-2, lire en ligne)
(en) Hermann Schägger et Kathy Pfeiffer, « The Ratio of Oxidative Phosphorylation Complexes I, II, III, IV, and V in Bovine Heart Mitochondria, and the Composition of Respiratory Chain Supercomplexes », Journal of Biological Chemistry, vol. 276, no 41, , p. 37861-37867 (PMID11483615, DOI10.1074/jbc.M106474200, lire en ligne)
(en) Kenneth H. Nealson, « Post-Viking Microbiology: New Approaches, New Data, New Insights », Origins of life and evolution of the biosphere, vol. 29, no 1, , p. 73-93 (PMID11536899, DOI10.1023/A:1006515817767, lire en ligne)
(en) Günter Schäfer, Martin Engelhard et Volker Müller, « Bioenergetics of the Archaea », Microbiology and Molecular Biology Reviews, vol. 63, no 3, , p. 570-620 (PMID10477309, PMCID103747, lire en ligne)
(en) W. John Ingledew et Robert K. Poole, « The respiratory chains of Escherichia coli », Microbiology and Molecular Biology Reviews, vol. 48, no 3, , p. 222-271 (PMID6387427, PMCID373010, lire en ligne)
(en) G. Unden et J. Bongaerts, « Alternative respiratory pathways of Escherichia coli: energetics and transcriptional regulation in response to electron acceptors », Biochimica et Biophysica Acta (BBA) - Bioenergetics, vol. 1320, no 3, , p. 217-234 (PMID9230919, DOI10.1016/S0005-2728(97)00034-0, lire en ligne)
(en) Gary Cecchini, Imke Schröder, Robert P Gunsalus et Elena Maklashina, « Succinate dehydrogenase and fumarate reductase from Escherichia coli », Biochimica et Biophysica Acta (BBA) - Bioenergetics, vol. 1553, nos 1-2, , p. 140-157 (PMID11803023, DOI10.1016/S0005-2728(01)00238-9, lire en ligne)
(en) Shawn R. Starkenburg, Patrick S. G. Chain, Luis A. Sayavedra-Soto, Loren Hauser, Miriam L. Land, Frank W. Larimer, Stephanie A. Malfatti, Martin G. Klotz, Peter J. Bottomley, Daniel J. Arp et William J. Hickey, « Genome Sequence of the Chemolithoautotrophic Nitrite-Oxidizing Bacterium Nitrobacter winogradskyi Nb-255 », Applied and Environmental Microbiology, vol. 72, no 3, , p. 2050-2063 (PMID16517654, PMCID1393235, DOI10.1128/AEM.72.3.2050-2063.2006, lire en ligne)
(en) M. W. Calhoun, K. L. Oden, R. B. Gennis, M. J. de Mattos et O. M. Neijssel, « Energetic efficiency of Escherichia coli: effects of mutations in components of the aerobic respiratory chain », Journal of Bacteriology, vol. 175, no 10, , p. 3020-3025 (PMID8491720, PMCID204621, lire en ligne)
(en) Marian Valko, Dieter Leibfritz, Jan Moncol, Mark T.D. Cronin, Milan Mazur et Joshua Telser, « Free radicals and antioxidants in normal physiological functions and human disease », The International Journal of Biochemistry & Cell Biology, vol. 39, no 1, , p. 44-84 (PMID16978905, DOI10.1016/j.biocel.2006.07.001, lire en ligne)
(en) Bernhard Kadenbach, Rabia Ramzan, Li Wen et Sebastian Vogt, « New extension of the Mitchell Theory for oxidative phosphorylation in mitochondria of living organisms », Biochimica et Biophysica Acta (BBA) - General Subjects, vol. 1800, no 3, , p. 205-212 (PMID19409964, DOI10.1016/j.bbagen.2009.04.019, lire en ligne)
(en) Karim S. Echtay, Damien Roussel, Julie St-Pierre, Mika B. Jekabsons, Susana Cadenas, Jeff A. Stuart, James A. Harper, Stephen J. Roebuck, Alastair Morrison, Susan Pickering, John C. Clapham et Martin D. Brand, « Superoxide activates mitochondrial uncoupling proteins », Nature, vol. 415, no 6867, , p. 96-99 (PMID11780125, DOI10.1038/415096a, Bibcode2002Natur.415...96E, lire en ligne)
(en) Adrian J. Lambert et Martin D. Brand, « Inhibitors of the quinone-binding site allow rapid superoxide production from mitochondrial NADH:ubiquinone oxidoreductase (complex I) », Journal of Biological Chemistry, vol. 279, no 38, , p. 39414-39420 (PMID15262965, DOI10.1074/jbc.M406576200, lire en ligne)
(en) D. V. Dervartanian et C. Veeger, « Studies on succinate dehydrogenase: I. Spectral properties of the purified enzyme and formation of enzyme-competitive inhibitor complexes », Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, vol. 92, no 2, , p. 233-247 (PMID14249115, DOI10.1016/0926-6569(64)90182-8, lire en ligne)
(en) Motonari Tsubaki et Shinya Yoshikawa, « Fourier-transform infrared study of cyanide binding to the Fea3-CuB binuclear site of bovine heart cytochrome c oxidase: implication of the redox-linked conformational change at the binuclear site », Biochemistry, vol. 32, no 1, , p. 164-173 (PMID8380331, DOI10.1021/bi00052a022, lire en ligne)
(en) Saroj Joshi et Yougou Huang, « ATP synthase complex from bovine heart mitochondria: The oligomycin sensitivity conferring protein is essential for dicyclohexyl carbodiimide-sensitive ATPase », Biochimica et Biophysica Acta (BBA) - Biomembranes, vol. 1067, no 2, , p. 255-258 (PMID1831660, DOI10.1016/0005-2736(91)90051-9, lire en ligne)
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(en) Kimitsune Ishizaki, Tony R. Larson, Nicolas Schauer, Alisdair R. Fernie, Ian A. Graham et Christopher J. Leaver, « The Critical Role of Arabidopsis Electron-Transfer Flavoprotein:Ubiquinone Oxidoreductase during Dark-Induced Starvation », American Society of Plant Biologists, vol. 17, no 9, , p. 2587-2600 (PMID16055629, PMCID1197437, DOI10.1105/tpc.105.035162, lire en ligne)
pnas.org
(en) Jian Zhang , Frank E. Frerman et Jung-Ja P. Kim, « Structure of electron transfer flavoprotein-ubiquinone oxidoreductase and electron transfer to the mitochondrial ubiquinone pool », Proceedings of the National Academy of Sciences of the United States of America, vol. 103, no 44, , p. 16212-16217 (PMID17050691, PMCID1637562, DOI10.1073/pnas.0604567103, Bibcode2006PNAS..10316212Z, lire en ligne)
(en) Denis P. Maxwell, Yong Wang et Lee McIntosh, « The alternative oxidase lowers mitochondrial reactive oxygen production in plant cells », Proceedings of the National Academy of Sciences of the United States of America, vol. 96, no 14, , p. 8271-8276 (PMID10393984, PMCID22224, DOI10.1073/pnas.96.14.8271, Bibcode1999PNAS...96.8271M, lire en ligne)
(en) S. Gupte, E. S. Wu, L. Hoechli, M. Hoechli, K. Jacobson, A. E. Sowers et C. R. Hackenbrock, « Relationship between lateral diffusion, collision frequency, and electron transfer of mitochondrial inner membrane oxidation-reduction components », Proceedings of the National Academy of Sciences of the United States of America, vol. 81, no 9, , p. 2606-2610 (PMID6326133, PMCID345118, DOI10.1073/pnas.81.9.2606, Bibcode1984PNAS...81.2606G, lire en ligne)
scielo.br
(en) F. E. Sluse et W. Jarmuszkiewicz, « Alternative oxidase in the branched mitochondrial respiratory network: an overview on structure, function, regulation, and role », Brazilian Journal of Medical and Biological Research, vol. 31, no 6, , p. 733-747 (PMID9698817, DOI10.1590/S0100-879X1998000600003, lire en ligne)
(en) David Leys et Nigel S Scrutton, « Electrical circuitry in biology: emerging principles from protein structure », Current Opinion in Structural Biology, vol. 14, no 6, , p. 642-647 (PMID15582386, DOI10.1016/j.sbi.2004.10.002, lire en ligne)
(en) Giorgio Lenaz, Romana Fato, Maria Luisa Genova, Christian Bergamini, Cristina Bianchi et Annalisa Biondi, « Mitochondrial Complex I: Structural and functional aspects », Biochimica et Biophysica Acta (BBA) - Bioenergetics, vol. 1757, nos 9-10, , p. 1406-1420 (PMID16828051, DOI10.1016/j.bbabio.2006.05.007, lire en ligne)
(en) Ekaterina A. Baranova, Peter J. Holt et Leonid A. Sazanov, « Projection Structure of the Membrane Domain of Escherichia coli Respiratory Complex I at 8 Å Resolution », Journal of Molecular Biology, vol. 366, no 1, , p. 140-154 (PMID17157874, DOI10.1016/j.jmb.2006.11.026, lire en ligne)
(en) Thorsten Friedrich et Bettina Böttcher, « The gross structure of the respiratory complex I: a Lego System », Biochimica et Biophysica Acta (BBA) - Bioenergetics, vol. 1608, no 1, , p. 1-9 (PMID14741580, DOI10.1016/j.bbabio.2003.10.002, lire en ligne)
(en) Kiyoshi Kita, Hiroko Hirawake, Hiroko Miyadera, Hisako Amino et Satoru Takeo, « Role of complex II in anaerobic respiration of the parasite mitochondria from Ascaris suum and Plasmodium falciparum », Biochimica et Biophysica Acta (BBA) - Bioenergetics, vol. 1553, nos 1-2, , p. 123-139 (PMID11803022, DOI10.1016/S0005-2728(01)00237-7, lire en ligne)
(en) Melissa W. Calhoun, Jeffrey W. Thomas et Robert B. Gennis, « The cytochrome oxidase superfamily of redox-driven proton pumps », Trends in Biochemical Sciences, vol. 19, no 8, , p. 325-330 (PMID7940677, DOI10.1016/0968-0004(94)90071-X, lire en ligne)
(en) Shinya Yoshikawa, Kazumasa Muramoto, Kyoko Shinzawa-Itoh, Hiroshi Aoyama, Tomitake Tsukihara, Kunitoshi Shimokata, Yukie Katayama et Hideo Shimada, « Proton pumping mechanism of bovine heart cytochrome c oxidase », Biochimica et Biophysica Acta (BBA) - Bioenergetics, vol. 1757, nos 9-10, , p. 1110-1116 (PMID16904626, DOI10.1016/j.bbabio.2006.06.004, lire en ligne)
(en) Anthony L. Moore et James N. Siedow, « The regulation and nature of the cyanide-resistant alternative oxidase of plant mitochondria », Biochimica et Biophysica Acta (BBA) - Bioenergetics, vol. 1059, no 2, , p. 121-140 (PMID1883834, DOI10.1016/S0005-2728(05)80197-5, lire en ligne)
(en) Yusuke Ito, Daisuke Saisho, Mikio Nakazono, Nobuhiro Tsutsumi et Atsushi Hirai, « Transcript levels of tandem-arranged alternative oxidase genes in rice are increased by low temperature », Gene, vol. 203, no 2, , p. 121-129 (PMID9426242, DOI10.1016/S0378-1119(97)00502-7, lire en ligne)
(en) Hermann Schägger, « Respiratory chain supercomplexes of mitochondria and bacteria », Biochimica et Biophysica Acta (BBA) - Bioenergetics, vol. 1555, nos 1-3, , p. 154-159 (PMID12206908, DOI10.1016/S0005-2728(02)00271-2, lire en ligne)
(en) G. Unden et J. Bongaerts, « Alternative respiratory pathways of Escherichia coli: energetics and transcriptional regulation in response to electron acceptors », Biochimica et Biophysica Acta (BBA) - Bioenergetics, vol. 1320, no 3, , p. 217-234 (PMID9230919, DOI10.1016/S0005-2728(97)00034-0, lire en ligne)
(en) Gary Cecchini, Imke Schröder, Robert P Gunsalus et Elena Maklashina, « Succinate dehydrogenase and fumarate reductase from Escherichia coli », Biochimica et Biophysica Acta (BBA) - Bioenergetics, vol. 1553, nos 1-2, , p. 140-157 (PMID11803023, DOI10.1016/S0005-2728(01)00238-9, lire en ligne)
(en) Marian Valko, Dieter Leibfritz, Jan Moncol, Mark T.D. Cronin, Milan Mazur et Joshua Telser, « Free radicals and antioxidants in normal physiological functions and human disease », The International Journal of Biochemistry & Cell Biology, vol. 39, no 1, , p. 44-84 (PMID16978905, DOI10.1016/j.biocel.2006.07.001, lire en ligne)
(en) Bernhard Kadenbach, Rabia Ramzan, Li Wen et Sebastian Vogt, « New extension of the Mitchell Theory for oxidative phosphorylation in mitochondria of living organisms », Biochimica et Biophysica Acta (BBA) - General Subjects, vol. 1800, no 3, , p. 205-212 (PMID19409964, DOI10.1016/j.bbagen.2009.04.019, lire en ligne)
(en) D. V. Dervartanian et C. Veeger, « Studies on succinate dehydrogenase: I. Spectral properties of the purified enzyme and formation of enzyme-competitive inhibitor complexes », Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, vol. 92, no 2, , p. 233-247 (PMID14249115, DOI10.1016/0926-6569(64)90182-8, lire en ligne)
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