Page CC, Moser CC, Chen X, Dutton PL; Moser; Chen; Dutton. Natural engineering principles of electron tunnelling in biological oxidation-reduction. Nature. 1999, 402 (6757): 47–52. Bibcode:1999Natur.402...47P. PMID 10573417. doi:10.1038/46972.
Leys D, Scrutton NS. Electrical circuitry in biology: emerging principles from protein structure. Current Opinion in Structural Biology. 2004, 14 (6): 642–7. PMID 15582386. doi:10.1016/j.sbi.2004.10.002.
Boxma B; de Graaf RM; van der Staay GW; Van Alen; Ricard; Gabaldón; Van Hoek; Moon-Van Der Staay; Koopman; Van Hellemond; Tielens; Friedrich; Veenhuis; Huynen; Hackstein; et al. An anaerobic mitochondrion that produces hydrogen. Nature. 2005, 434 (7029): 74–9. Bibcode:2005Natur.434...74B. PMID 15744302. doi:10.1038/nature03343.
Baranova EA, Holt PJ, Sazanov LA. Projection structure of the membrane domain of Escherichia coli respiratory complex I at 8 A resolution. J. Mol. Biol. 2007, 366 (1): 140–54. PMID 17157874. doi:10.1016/j.jmb.2006.11.026.
Friedrich T, Böttcher B. The gross structure of the respiratory complex I: a Lego System. Biochim. Biophys. Acta. 2004, 1608 (1): 1–9. PMID 14741580. doi:10.1016/j.bbabio.2003.10.002.
Hirst J. Towards the molecular mechanism of respiratory complex I. Biochem. J. January 2010, 425 (2): 327–39. PMID 20025615. doi:10.1042/BJ20091382.
Yankovskaya, V.; Horsefield, R.; Tornroth, S.; Luna-Chavez, C.; Miyoshi, H.; Leger, C.; Byrne, B.; Cecchini, G.; Iwata, S.; et al. Architecture of succinate dehydrogenase and reactive oxygen species generation. Science. 2003, 299 (5607): 700–704. Bibcode:2003Sci...299..700Y. PMID 12560550. doi:10.1126/science.1079605.
Horsefield R, Iwata S, Byrne B. Complex II from a structural perspective. Curr. Protein Pept. Sci. 2004, 5 (2): 107–18. PMID 15078221. doi:10.2174/1389203043486847.
Kita K, Hirawake H, Miyadera H, Amino H, Takeo S. Role of complex II in anaerobic respiration of the parasite mitochondria from Ascaris suum and Plasmodium falciparum. Biochim. Biophys. Acta. 2002, 1553 (1–2): 123–39. PMID 11803022. doi:10.1016/S0005-2728(01)00237-7.
Painter HJ, Morrisey JM, Mather MW, Vaidya AB; Morrisey; Mather; Vaidya. Specific role of mitochondrial electron transport in blood-stage Plasmodium falciparum. Nature. 2007, 446 (7131): 88–91. Bibcode:2007Natur.446...88P. PMID 17330044. doi:10.1038/nature05572.
Hunte C, Palsdottir H, Trumpower BL. Protonmotive pathways and mechanisms in the cytochrome bc1 complex. FEBS Lett. 2003, 545 (1): 39–46. PMID 12788490. doi:10.1016/S0014-5793(03)00391-0.
Calhoun M, Thomas J, Gennis R. The cytochrome oxidase superfamily of redox-driven proton pumps. Trends Biochem Sci. 1994, 19 (8): 325–30. PMID 7940677. doi:10.1016/0968-0004(94)90071-X.
Tsukihara T, Aoyama H, Yamashita E, Tomizaki T, Yamaguchi H, Shinzawa-Itoh K, Nakashima R, Yaono R, Yoshikawa S.; Aoyama; Yamashita; Tomizaki; Yamaguchi; Shinzawa-Itoh; Nakashima; Yaono; Yoshikawa. The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 A. Science. 1996, 272 (5265): 1136–44. Bibcode:1996Sci...272.1136T. PMID 8638158. doi:10.1126/science.272.5265.1136.
Yoshikawa S; Muramoto K; Shinzawa-Itoh K; et al. Proton pumping mechanism of bovine heart cytochrome c oxidase. Biochim. Biophys. Acta. 2006, 1757 (9–10): 1110–6. PMID 16904626. doi:10.1016/j.bbabio.2006.06.004.
McDonald A, Vanlerberghe G. Branched mitochondrial electron transport in the Animalia: presence of alternative oxidase in several animal phyla. IUBMB Life. 2004, 56 (6): 333–41. PMID 15370881. doi:10.1080/1521-6540400000876.
Sluse FE, Jarmuszkiewicz W. Alternative oxidase in the branched mitochondrial respiratory network: an overview on structure, function, regulation, and role. Braz. J. Med. Biol. Res. 1998, 31 (6): 733–47. PMID 9698817. doi:10.1590/S0100-879X1998000600003.
Moore AL, Siedow JN. The regulation and nature of the cyanide-resistant alternative oxidase of plant mitochondria. Biochim. Biophys. Acta. 1991, 1059 (2): 121–40. PMID 1883834. doi:10.1016/S0005-2728(05)80197-5.
Vanlerberghe GC, McIntosh L. Alternative oxidase: From Gene to Function. Annual Review of Plant Physiology and Plant Molecular Biology. 1997, 48: 703–34. PMID 15012279. doi:10.1146/annurev.arplant.48.1.703.
Ito Y, Saisho D, Nakazono M, Tsutsumi N, Hirai A. Transcript levels of tandem-arranged alternative oxidase genes in rice are increased by low temperature. Gene. 1997, 203 (2): 121–9. PMID 9426242. doi:10.1016/S0378-1119(97)00502-7.
Heinemeyer J, Braun HP, Boekema EJ, Kouril R. A structural model of the cytochrome C reductase/oxidase supercomplex from yeast mitochondria. J. Biol. Chem. 2007, 282 (16): 12240–8. PMID 17322303. doi:10.1074/jbc.M610545200.
Nealson KH. Post-Viking microbiology: new approaches, new data, new insights. Origins of life and evolution of the biosphere: the journal of the International Society for the Study of the Origin of Life. 1999, 29 (1): 73–93. PMID 11536899. doi:10.1023/A:1006515817767.
Unden G, Bongaerts J. Alternative respiratory pathways of Escherichia coli: energetics and transcriptional regulation in response to electron acceptors. Biochim. Biophys. Acta. 1997, 1320 (3): 217–34. PMID 9230919. doi:10.1016/S0005-2728(97)00034-0.
Cecchini G, Schröder I, Gunsalus RP, Maklashina E. Succinate dehydrogenase and fumarate reductase from Escherichia coli. Biochim. Biophys. Acta. 2002, 1553 (1–2): 140–57. PMID 11803023. doi:10.1016/S0005-2728(01)00238-9.
Van Walraven HS, Strotmann H, Schwarz O, Rumberg B. The H+/ATP coupling ratio of the ATP synthase from thiol-modulated chloroplasts and two cyanobacterial strains is four. FEBS Lett. 1996, 379 (3): 309–13. PMID 8603713. doi:10.1016/0014-5793(95)01536-1.
Yoshida M, Muneyuki E, Hisabori T. ATP synthase—a marvellous rotary engine of the cell. Nature Reviews Molecular Cell Biology. 2001, 2 (9): 669–77. PMID 11533724. doi:10.1038/35089509.
Capaldi R, Aggeler R. Mechanism of the F(1)F(0)-type ATP synthase, a biological rotary motor. Trends Biochem Sci. 2002, 27 (3): 154–60. PMID 11893513. doi:10.1016/S0968-0004(01)02051-5.
Müller V. An exceptional variability in the motor of archaeal A1A0 ATPases: from multimeric to monomeric rotors comprising 6–13 ion binding sites. J. Bioenerg. Biomembr. 2004, 36 (1): 115–25. PMID 15168615. doi:10.1023/B:JOBB.0000019603.68282.04.
Valko M, Leibfritz D, Moncol J, Cronin MT, Mazur M, Telser J. Free radicals and antioxidants in normal physiological functions and human disease. Int. J. Biochem. Cell Biol. 2007, 39 (1): 44–84. PMID 16978905. doi:10.1016/j.biocel.2006.07.001.
Finkel T, Holbrook NJ. Oxidants, oxidative stress and the biology of ageing. Nature. 2000, 408 (6809): 239–47. PMID 11089981. doi:10.1038/35041687.
Kadenbach B, Ramzan R, Wen L, Vogt S. New extension of the Mitchell Theory for oxidative phosphorylation in mitochondria of living organisms. Biochim. Biophys. Acta. May 2009, 1800 (3): 205–212. PMID 19409964. doi:10.1016/j.bbagen.2009.04.019.
Joshi S, Huang YG. ATP synthase complex from bovine heart mitochondria: the oligomycin sensitivity conferring protein is essential for dicyclohexyl carbodiimide-sensitive ATPase. Biochim. Biophys. Acta. 1991, 1067 (2): 255–8. PMID 1831660. doi:10.1016/0005-2736(91)90051-9.
Tsubaki M; Yoshikawa, Shinya. 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. 1993, 32 (1): 164–73. PMID 8380331. doi:10.1021/bi00052a022.
Dervartanian DV, Veeger C. Studies on succinate dehydrogenase. I. Spectral properties of the purified enzyme and formation of enzyme-competitive inhibitor complexes. Biochim. Biophys. Acta. November 1964, 92: 233–47. PMID 14249115. doi:10.1016/0926-6569(64)90182-8.
Borecký J, Vercesi AE. Plant uncoupling mitochondrial protein and alternative oxidase: energy metabolism and stress. Biosci. Rep. 2005, 25 (3–4): 271–86. PMID 16283557. doi:10.1007/s10540-005-2889-2.
Harden A, Young WJ. The alcoholic ferment of yeast-juice. Proceedings of the Royal Society. 1906, B (77): 405–20. doi:10.1098/rspb.1906.0029.
Kalckar HM. Origins of the concept oxidative phosphorylation. Mol. Cell. Biochem. 1974, 5 (1–2): 55–63. PMID 4279328. doi:10.1007/BF01874172.
Page CC, Moser CC, Chen X, Dutton PL; Moser; Chen; Dutton. Natural engineering principles of electron tunnelling in biological oxidation-reduction. Nature. 1999, 402 (6757): 47–52. Bibcode:1999Natur.402...47P. PMID 10573417. doi:10.1038/46972.
Boxma B; de Graaf RM; van der Staay GW; Van Alen; Ricard; Gabaldón; Van Hoek; Moon-Van Der Staay; Koopman; Van Hellemond; Tielens; Friedrich; Veenhuis; Huynen; Hackstein; et al. An anaerobic mitochondrion that produces hydrogen. Nature. 2005, 434 (7029): 74–9. Bibcode:2005Natur.434...74B. PMID 15744302. doi:10.1038/nature03343.
Yankovskaya, V.; Horsefield, R.; Tornroth, S.; Luna-Chavez, C.; Miyoshi, H.; Leger, C.; Byrne, B.; Cecchini, G.; Iwata, S.; et al. Architecture of succinate dehydrogenase and reactive oxygen species generation. Science. 2003, 299 (5607): 700–704. Bibcode:2003Sci...299..700Y. PMID 12560550. doi:10.1126/science.1079605.
Painter HJ, Morrisey JM, Mather MW, Vaidya AB; Morrisey; Mather; Vaidya. Specific role of mitochondrial electron transport in blood-stage Plasmodium falciparum. Nature. 2007, 446 (7131): 88–91. Bibcode:2007Natur.446...88P. PMID 17330044. doi:10.1038/nature05572.
Page CC, Moser CC, Chen X, Dutton PL; Moser; Chen; Dutton. Natural engineering principles of electron tunnelling in biological oxidation-reduction. Nature. 1999, 402 (6757): 47–52. Bibcode:1999Natur.402...47P. PMID 10573417. doi:10.1038/46972.
Leys D, Scrutton NS. Electrical circuitry in biology: emerging principles from protein structure. Current Opinion in Structural Biology. 2004, 14 (6): 642–7. PMID 15582386. doi:10.1016/j.sbi.2004.10.002.
Boxma B; de Graaf RM; van der Staay GW; Van Alen; Ricard; Gabaldón; Van Hoek; Moon-Van Der Staay; Koopman; Van Hellemond; Tielens; Friedrich; Veenhuis; Huynen; Hackstein; et al. An anaerobic mitochondrion that produces hydrogen. Nature. 2005, 434 (7029): 74–9. Bibcode:2005Natur.434...74B. PMID 15744302. doi:10.1038/nature03343.
Baranova EA, Holt PJ, Sazanov LA. Projection structure of the membrane domain of Escherichia coli respiratory complex I at 8 A resolution. J. Mol. Biol. 2007, 366 (1): 140–54. PMID 17157874. doi:10.1016/j.jmb.2006.11.026.
Friedrich T, Böttcher B. The gross structure of the respiratory complex I: a Lego System. Biochim. Biophys. Acta. 2004, 1608 (1): 1–9. PMID 14741580. doi:10.1016/j.bbabio.2003.10.002.
Hirst J. Towards the molecular mechanism of respiratory complex I. Biochem. J. January 2010, 425 (2): 327–39. PMID 20025615. doi:10.1042/BJ20091382.
Yankovskaya, V.; Horsefield, R.; Tornroth, S.; Luna-Chavez, C.; Miyoshi, H.; Leger, C.; Byrne, B.; Cecchini, G.; Iwata, S.; et al. Architecture of succinate dehydrogenase and reactive oxygen species generation. Science. 2003, 299 (5607): 700–704. Bibcode:2003Sci...299..700Y. PMID 12560550. doi:10.1126/science.1079605.
Horsefield R, Iwata S, Byrne B. Complex II from a structural perspective. Curr. Protein Pept. Sci. 2004, 5 (2): 107–18. PMID 15078221. doi:10.2174/1389203043486847.
Kita K, Hirawake H, Miyadera H, Amino H, Takeo S. Role of complex II in anaerobic respiration of the parasite mitochondria from Ascaris suum and Plasmodium falciparum. Biochim. Biophys. Acta. 2002, 1553 (1–2): 123–39. PMID 11803022. doi:10.1016/S0005-2728(01)00237-7.
Painter HJ, Morrisey JM, Mather MW, Vaidya AB; Morrisey; Mather; Vaidya. Specific role of mitochondrial electron transport in blood-stage Plasmodium falciparum. Nature. 2007, 446 (7131): 88–91. Bibcode:2007Natur.446...88P. PMID 17330044. doi:10.1038/nature05572.
Hunte C, Palsdottir H, Trumpower BL. Protonmotive pathways and mechanisms in the cytochrome bc1 complex. FEBS Lett. 2003, 545 (1): 39–46. PMID 12788490. doi:10.1016/S0014-5793(03)00391-0.
Calhoun M, Thomas J, Gennis R. The cytochrome oxidase superfamily of redox-driven proton pumps. Trends Biochem Sci. 1994, 19 (8): 325–30. PMID 7940677. doi:10.1016/0968-0004(94)90071-X.
Tsukihara T, Aoyama H, Yamashita E, Tomizaki T, Yamaguchi H, Shinzawa-Itoh K, Nakashima R, Yaono R, Yoshikawa S.; Aoyama; Yamashita; Tomizaki; Yamaguchi; Shinzawa-Itoh; Nakashima; Yaono; Yoshikawa. The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 A. Science. 1996, 272 (5265): 1136–44. Bibcode:1996Sci...272.1136T. PMID 8638158. doi:10.1126/science.272.5265.1136.
Yoshikawa S; Muramoto K; Shinzawa-Itoh K; et al. Proton pumping mechanism of bovine heart cytochrome c oxidase. Biochim. Biophys. Acta. 2006, 1757 (9–10): 1110–6. PMID 16904626. doi:10.1016/j.bbabio.2006.06.004.
McDonald A, Vanlerberghe G. Branched mitochondrial electron transport in the Animalia: presence of alternative oxidase in several animal phyla. IUBMB Life. 2004, 56 (6): 333–41. PMID 15370881. doi:10.1080/1521-6540400000876.
Sluse FE, Jarmuszkiewicz W. Alternative oxidase in the branched mitochondrial respiratory network: an overview on structure, function, regulation, and role. Braz. J. Med. Biol. Res. 1998, 31 (6): 733–47. PMID 9698817. doi:10.1590/S0100-879X1998000600003.
Moore AL, Siedow JN. The regulation and nature of the cyanide-resistant alternative oxidase of plant mitochondria. Biochim. Biophys. Acta. 1991, 1059 (2): 121–40. PMID 1883834. doi:10.1016/S0005-2728(05)80197-5.
Vanlerberghe GC, McIntosh L. Alternative oxidase: From Gene to Function. Annual Review of Plant Physiology and Plant Molecular Biology. 1997, 48: 703–34. PMID 15012279. doi:10.1146/annurev.arplant.48.1.703.
Ito Y, Saisho D, Nakazono M, Tsutsumi N, Hirai A. Transcript levels of tandem-arranged alternative oxidase genes in rice are increased by low temperature. Gene. 1997, 203 (2): 121–9. PMID 9426242. doi:10.1016/S0378-1119(97)00502-7.
Heinemeyer J, Braun HP, Boekema EJ, Kouril R. A structural model of the cytochrome C reductase/oxidase supercomplex from yeast mitochondria. J. Biol. Chem. 2007, 282 (16): 12240–8. PMID 17322303. doi:10.1074/jbc.M610545200.
Nealson KH. Post-Viking microbiology: new approaches, new data, new insights. Origins of life and evolution of the biosphere: the journal of the International Society for the Study of the Origin of Life. 1999, 29 (1): 73–93. PMID 11536899. doi:10.1023/A:1006515817767.
Unden G, Bongaerts J. Alternative respiratory pathways of Escherichia coli: energetics and transcriptional regulation in response to electron acceptors. Biochim. Biophys. Acta. 1997, 1320 (3): 217–34. PMID 9230919. doi:10.1016/S0005-2728(97)00034-0.
Cecchini G, Schröder I, Gunsalus RP, Maklashina E. Succinate dehydrogenase and fumarate reductase from Escherichia coli. Biochim. Biophys. Acta. 2002, 1553 (1–2): 140–57. PMID 11803023. doi:10.1016/S0005-2728(01)00238-9.
Van Walraven HS, Strotmann H, Schwarz O, Rumberg B. The H+/ATP coupling ratio of the ATP synthase from thiol-modulated chloroplasts and two cyanobacterial strains is four. FEBS Lett. 1996, 379 (3): 309–13. PMID 8603713. doi:10.1016/0014-5793(95)01536-1.
Yoshida M, Muneyuki E, Hisabori T. ATP synthase—a marvellous rotary engine of the cell. Nature Reviews Molecular Cell Biology. 2001, 2 (9): 669–77. PMID 11533724. doi:10.1038/35089509.
Capaldi R, Aggeler R. Mechanism of the F(1)F(0)-type ATP synthase, a biological rotary motor. Trends Biochem Sci. 2002, 27 (3): 154–60. PMID 11893513. doi:10.1016/S0968-0004(01)02051-5.
Müller V. An exceptional variability in the motor of archaeal A1A0 ATPases: from multimeric to monomeric rotors comprising 6–13 ion binding sites. J. Bioenerg. Biomembr. 2004, 36 (1): 115–25. PMID 15168615. doi:10.1023/B:JOBB.0000019603.68282.04.
Davies K. Oxidative stress: the paradox of aerobic life. Biochem Soc Symp. 1995, 61: 1–31. PMID 8660387.
Valko M, Leibfritz D, Moncol J, Cronin MT, Mazur M, Telser J. Free radicals and antioxidants in normal physiological functions and human disease. Int. J. Biochem. Cell Biol. 2007, 39 (1): 44–84. PMID 16978905. doi:10.1016/j.biocel.2006.07.001.
Finkel T, Holbrook NJ. Oxidants, oxidative stress and the biology of ageing. Nature. 2000, 408 (6809): 239–47. PMID 11089981. doi:10.1038/35041687.
Kadenbach B, Ramzan R, Wen L, Vogt S. New extension of the Mitchell Theory for oxidative phosphorylation in mitochondria of living organisms. Biochim. Biophys. Acta. May 2009, 1800 (3): 205–212. PMID 19409964. doi:10.1016/j.bbagen.2009.04.019.
Joshi S, Huang YG. ATP synthase complex from bovine heart mitochondria: the oligomycin sensitivity conferring protein is essential for dicyclohexyl carbodiimide-sensitive ATPase. Biochim. Biophys. Acta. 1991, 1067 (2): 255–8. PMID 1831660. doi:10.1016/0005-2736(91)90051-9.
Tsubaki M; Yoshikawa, Shinya. 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. 1993, 32 (1): 164–73. PMID 8380331. doi:10.1021/bi00052a022.
Dervartanian DV, Veeger C. Studies on succinate dehydrogenase. I. Spectral properties of the purified enzyme and formation of enzyme-competitive inhibitor complexes. Biochim. Biophys. Acta. November 1964, 92: 233–47. PMID 14249115. doi:10.1016/0926-6569(64)90182-8.
Borecký J, Vercesi AE. Plant uncoupling mitochondrial protein and alternative oxidase: energy metabolism and stress. Biosci. Rep. 2005, 25 (3–4): 271–86. PMID 16283557. doi:10.1007/s10540-005-2889-2.
Kalckar HM. Origins of the concept oxidative phosphorylation. Mol. Cell. Biochem. 1974, 5 (1–2): 55–63. PMID 4279328. doi:10.1007/BF01874172.