References analysis of the Wikipedia article "Fosforylacja oksydacyjna" in the Polish version

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Mitchell P, Moyle J. Chemiosmotic hypothesis of oxidative phosphorylation. „Nature”. 213 (5072), s. 137–139, 1967. DOI: 10.1038/213137a0. PMID: 4291593.

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Mathews FS. The structure, function and evolution of cytochromes. „Prog. Biophys. Mol. Biol.”. 45 (1), s. 1–56, 1985. DOI: 10.1016/0079-6107(85)90004-5. PMID: 3881803.

Wood PM. Why do c-type cytochromes exist?. „FEBS Lett.”. 164 (2), s. 223–226, 1983. DOI: 10.1016/0014-5793(83)80289-0. PMID: 6317447.

Mitchell P. Keilin’s respiratory chain concept and its chemiosmotic consequences. „Science”. 206 (4423), s. 1148–1159, 1979. DOI: 10.1126/science.388618. PMID: 388618.

Johnson D, Dean D, Smith A, Johnson M. Structure, function, and formation of biological iron-sulfur clusters. „Annu Rev Biochem”. 74, s. 247–281, 2005. DOI: 10.1146/annurev.biochem.74.082803.133518. PMID: 15952888.

Page CC, Moser CC, Chen X, Dutton PL. Natural engineering principles of electron tunnelling in biological oxidation-reduction. „Nature”. 402 (6757), s. 47–52, 1999. DOI: 10.1038/46972. PMID: 10573417.

Leys D, Scrutton NS. Electrical circuitry in biology: emerging principles from protein structure. „Curr. Opin. Struct. Biol.”. 14 (6), s. 642–647, 2004. DOI: 10.1016/j.sbi.2004.10.002. PMID: 15582386.

Boxma B, de Graaf RM, van der Staay GW, et al. An anaerobic mitochondrion that produces hydrogen. „Nature”. 434 (7029), s. 74–79, 2005. DOI: 10.1038/nature03343. PMID: 15744302.

van der Giezen M., Tovar J., Clark CG. Mitochondrion-derived organelles in protists and fungi. „International review of cytology”. 244, s. 175–225, 2005. DOI: 10.1016/S0074-7696(05)44005-X. PMID: 16157181.

Lenaz G, Fato R, Genova M, Bergamini C, Bianchi C, Biondi A. Mitochondrial Complex I: structural and functional aspects. „Biochim Biophys Acta”. 1757 (9–10), s. 1406–1420, 2006. DOI: 10.1016/j.bbabio.2006.05.007. PMID: 16828051.

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.”. 366 (1), s. 140–154, 2007. DOI: 10.1016/j.jmb.2006.11.026. PMID: 17157874.

Friedrich T, Böttcher B. The gross structure of the respiratory complex I: a Lego System. „Biochim. Biophys. Acta”. 1608 (1), s. 1–9, 2004. DOI: 10.1016/j.bbabio.2003.10.002. PMID: 14741580.

Brandt U, Kerscher S, Dröse S, Zwicker K, Zickermann V. Proton pumping by NADH: ubiquinone oxidoreductase. A redox driven conformational change mechanism?. „FEBS Lett.”. 545 (1), s. 9–17, 2003. DOI: 10.1016/S0014-5793(03)00387-9. PMID: 12788486.

Cecchini G. Function and structure of complex II of the respiratory chain. „Annu Rev Biochem”. 72, s. 77–109, 2003. DOI: 10.1146/annurev.biochem.72.121801.161700. PMID: 14527321.

Horsefield R, Iwata S, Byrne B. Complex II from a structural perspective. „Curr. Protein Pept. Sci.”. 5 (2), s. 107–118, 2004. DOI: 10.2174/1389203043486847. PMID: 15078221.

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”. 1553 (1–2), s. 123–139, 2002. DOI: 10.1016/S0005-2728(01)00237-7. PMID: 11803022.

Painter HJ, Morrisey JM, Mather MW, Vaidya AB. Specific role of mitochondrial electron transport in blood-stage Plasmodium falciparum. „Nature”. 446 (7131), s. 88–91, 2007. DOI: 10.1038/nature05572. PMID: 17330044.

Zhang J, Frerman FE, Kim JJ. Structure of electron transfer flavoprotein-ubiquinone oxidoreductase and electron transfer to the mitochondrial ubiquinone pool. „Proc. Natl. Acad. Sci. U.S.A.”. 103 (44), s. 16212–16217, 2006. DOI: 10.1073/pnas.0604567103. PMID: 17050691.

Ishizaki K, Larson TR, Schauer N, Fernie AR, Graham IA, Leaver CJ. The critical role of Arabidopsis electron-transfer flavoprotein:ubiquinone oxidoreductase during dark-induced starvation. „Plant Cell”. 17 (9), s. 2587–2600, 2005. DOI: 10.1105/tpc.105.035162. PMID: 16055629.

Berry E, Guergova-Kuras M, Huang L, Crofts A. Structure and function of cytochrome bc complexes. „Annu Rev Biochem”. 69, s. 1005–1075, 2000. DOI: 10.1146/annurev.biochem.69.1.1005. PMID: 10966481.

Crofts AR. The cytochrome bc1 complex: function in the context of structure. „Annu. Rev. Physiol.”. 66, s. 689–733, 2004. DOI: 10.1146/annurev.physiol.66.032102.150251. PMID: 14977419.

Iwata S, Lee JW, Okada K, et al. Complete structure of the 11-subunit bovine mitochondrial cytochrome bc1 complex. „Science”. 281 (5373), s. 64–71, 1998. DOI: 10.1126/science.281.5373.64. PMID: 9651245.

Hunte C, Palsdottir H, Trumpower BL. Protonmotive pathways and mechanisms in the cytochrome bc1 complex. „FEBS Lett.”. 545 (1), s. 39–46, 2003. DOI: 10.1016/S0014-5793(03)00391-0. PMID: 12788490.

Calhoun M, Thomas J, Gennis R. The cytochrome oxidase superfamily of redox-driven proton pumps. „Trends Biochem Sci”. 19 (8), s. 325–330, 1994. DOI: 10.1016/0968-0004(94)90071-X. PMID: 7940677.

Tsukihara T, Aoyama H, Yamashita E, Tomizaki T, Yamaguchi H, Shinzawa-Itoh K, Nakashima R, Yaono R, Yoshikawa S. TThe whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 A. „Science”. 272 (5265), s. 1136–1144, 1996. DOI: 10.1126/science.272.5265.1136. PMID: 8638158.

Yoshikawa S, Muramoto K, Shinzawa-Itoh K, et al. Proton pumping mechanism of bovine heart cytochrome c oxidase. „Biochim. Biophys. Acta”. 1757 (9–10), s. 1110–1116, 2006. DOI: 10.1016/j.bbabio.2006.06.004. PMID: 16904626.

Rasmusson AG, Soole KL, Elthon TE. Alternative NAD(P)H dehydrogenases of plant mitochondria. „Annual review of plant biology”. 55, s. 23–39, 2004. DOI: 10.1146/annurev.arplant.55.031903.141720. PMID: 15725055.

Menz RI, Day DA. Purification and characterization of a 43-kDa rotenone-insensitive NADH dehydrogenase from plant mitochondria. „J. Biol. Chem.”. 271 (38), s. 23117–23120, 1996. DOI: 10.1074/jbc.271.38.23117. PMID: 8798503.

McDonald A, Vanlerberghe G. Branched mitochondrial electron transport in the Animalia: presence of alternative oxidase in several animal phyla. „IUBMB Life”. 56 (6), s. 333–341, 2004. DOI: 10.1080/1521-6540400000876. PMID: 15370881.

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.”. 31 (6), s. 733–747, 1998. DOI: 10.1590/S0100-879X1998000600003. PMID: 9698817.

Moore AL, Siedow JN. The regulation and nature of the cyanide-resistant alternative oxidase of plant mitochondria. „Biochim. Biophys. Acta”. 1059 (2), s. 121–140, 1991. DOI: 10.1016/S0005-2728(05)80197-5. PMID: 1883834.

Vanlerberghe GC, McIntosh L. Alternative oxidase: From Gene to Function. „Annual Review of Plant Physiology and Plant Molecular Biology”. 48, s. 703–734, 1997. DOI: 10.1146/annurev.arplant.48.1.703. PMID: 15012279.

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”. 203 (2), s. 121–129, 1997. DOI: 10.1016/S0378-1119(97)00502-7. PMID: 9426242.

Maxwell DP, Wang Y, McIntosh L. The alternative oxidase lowers mitochondrial reactive oxygen production in plant cells. „Proc. Natl. Acad. Sci. U.S.A.”. 96 (14), s. 8271–8276, 1999. DOI: 10.1073/pnas.96.14.8271. PMID: 10393984.

Lenaz G. A critical appraisal of the mitochondrial coenzyme Q pool. „FEBS Lett.”. 509 (2), s. 151–155, 2001. DOI: 10.1016/S0014-5793(01)03172-6. PMID: 11741580.

Heinemeyer J, Braun HP, Boekema EJ, Kouril R. A structural model of the cytochrome C reductase/oxidase supercomplex from yeast mitochondria. „J. Biol. Chem.”. 282 (16), s. 12240–12248, 2007. DOI: 10.1074/jbc.M610545200. PMID: 17322303.

Schägger H, Pfeiffer K. Supercomplexes in the respiratory chains of yeast and mammalian mitochondria. „EMBO J.”. 19 (8), s. 1777–1783, 2000. DOI: 10.1093/emboj/19.8.1777. PMID: 10775262.

Schägger H. Respiratory chain supercomplexes of mitochondria and bacteria. „Biochim. Biophys. Acta”. 1555 (1–3), s. 154–159, 2002. DOI: 10.1016/S0005-2728(02)00271-2. PMID: 12206908.

Schägger H, Pfeiffer K. The ratio of oxidative phosphorylation complexes I-V in bovine heart mitochondria and the composition of respiratory chain supercomplexes. „J. Biol. Chem.”. 276 (41), s. 37861–37867, 2001. DOI: 10.1074/jbc.M106474200. PMID: 11483615.

Gupte S, Wu ES, Hoechli L, et al. Relationship between lateral diffusion, collision frequency, and electron transfer of mitochondrial inner membrane oxidation-reduction components. „Proc. Natl. Acad. Sci. U.S.A.”. 81 (9), s. 2606–2610, 1984. DOI: 10.1073/pnas.81.9.2606. PMID: 6326133.

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”. 29 (1), s. 73–93, 1999. DOI: 10.1023/A:1006515817767. PMID: 11536899.

Unden G, Bongaerts J. Alternative respiratory pathways of Escherichia coli: energetics and transcriptional regulation in response to electron acceptors. „Biochim. Biophys. Acta”. 1320 (3), s. 217–234, 1997. DOI: 10.1016/S0005-2728(97)00034-0. PMID: 9230919.

Cecchini G, Schröder I, Gunsalus RP, Maklashina E. Succinate dehydrogenase and fumarate reductase from Escherichia coli. „Biochim. Biophys. Acta”. 1553 (1–2), s. 140–157, 2002. DOI: 10.1016/S0005-2728(01)00238-9. PMID: 11803023.

Freitag A, Bock E. Energy conservation in Nitrobacter. „FEMS Microbiology Letters”. 66 (1–3), s. 157–162, 1990. DOI: 10.1111/j.1574-6968.1990.tb03989.x.

Starkenburg SR, Chain PS, Sayavedra-Soto LA, et al. Genome sequence of the chemolithoautotrophic nitrite-oxidizing bacterium Nitrobacter winogradskyi Nb-255. „Appl. Environ. Microbiol.”. 72 (3), s. 2050–2063, 2006. DOI: 10.1128/AEM.72.3.2050-2063.2006. PMID: 16517654.

Iuchi S, Lin EC. Adaptation of Escherichia coli to redox environments by gene expression. „Mol. Microbiol.”. 9 (1), s. 9–15, 1993. DOI: 10.1111/j.1365-2958.1993.tb01664.x. PMID: 8412675.

Boyer PD. The ATP synthase–a splendid molecular machine. „Annu. Rev. Biochem.”. 66, s. 717–749, 1997. DOI: 10.1146/annurev.biochem.66.1.717. PMID: 9242922.

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.”. 379 (3), s. 309–313, 1996. DOI: 10.1016/0014-5793(95)01536-1. PMID: 8603713.

Yoshida M, Muneyuki E, Hisabori T. ATP synthase–a marvellous rotary engine of the cell. „Nat. Rev. Mol. Cell Biol.”. 2 (9), s. 669–677, 2001. DOI: 10.1038/35089509. PMID: 11533724.

Rubinstein JL, Walker JE, Henderson R. Structure of the mitochondrial ATP synthase by electron cryomicroscopy. „EMBO J.”. 22 (23), s. 6182–6192, 2003. DOI: 10.1093/emboj/cdg608. PMID: 14633978.

Leslie AG, Walker JE. Structural model of F1-ATPase and the implications for rotary catalysis. „Philos. Trans. R. Soc. Lond., B, Biol. Sci.”. 355 (1396), s. 465–471, 2000. DOI: 10.1098/rstb.2000.0588. PMID: 10836500.

Noji H, Yoshida M. The rotary machine in the cell, ATP synthase. „J. Biol. Chem.”. 276 (3), s. 1665–1668, 2001. DOI: 10.1074/jbc.R000021200. PMID: 11080505.

Capaldi R, Aggeler R. Mechanism of the F(1)F(0)-type ATP synthase, a biological rotary motor. „Trends Biochem Sci”. 27 (3), s. 154–160, 2002. DOI: 10.1016/S0968-0004(01)02051-5. PMID: 11893513.

Dimroth P, von Ballmoos C, Meier T. Catalytic and mechanical cycles in F-ATP synthases. Fourth in the Cycles Review Series. „EMBO Rep”. 7 (3), s. 276–282, 2006. DOI: 10.1038/sj.embor.7400646. PMID: 16607397.

Dimroth P. Bacterial sodium ion-coupled energetics. „Antonie Van Leeuwenhoek”. 65 (4), s. 381–395, 1994. DOI: 10.1007/BF00872221. PMID: 7832594.

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.”. 36 (1), s. 115–125, 2004. DOI: 10.1023/B:JOBB.0000019603.68282.04. PMID: 15168615.

Rattan SI. Theories of biological aging: genes, proteins, and free radicals. „Free Radic. Res.”. 40 (12), s. 1230–1238, 2006. DOI: 10.1080/10715760600911303. PMID: 17090411.

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Raha S, Robinson B. Mitochondria, oxygen free radicals, disease and ageing. „Trends Biochem Sci”. 25 (10), s. 502–508, 2000. DOI: 10.1016/S0968-0004(00)01674-1. PMID: 11050436.

Finkel T, Holbrook NJ. Oxidants, oxidative stress and the biology of ageing. „Nature”, s. 239–247, 2000. DOI: 10.1038/35041687. PMID: 11089981.

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”. 1067 (2), s. 255–258, 1991. DOI: 10.1016/0005-2736(91)90051-9. PMID: 1831660.

Tsubaki M. 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”. 32 (1), s. 164–173, 1993. DOI: 10.1021/bi00052a022. PMID: 8380331.

Heytler PG. Uncouplers of oxidative phosphorylation. „Meth. Enzymol.”. 55, s. 462–442, 1979. DOI: 10.1016/0076-6879(79)55060-5. PMID: 156853.

Lambert AJ, Brand MD. Inhibitors of the quinone-binding site allow rapid superoxide production from mitochondrial NADH: ubiquinone oxidoreductase (complex I). „J. Biol. Chem.”. 279 (38), s. 39414–39420, 2004. DOI: 10.1074/jbc.M406576200. PMID: 15262965.

Ricquier D, Bouillaud F. The uncoupling protein homologues: UCP1, UCP2, UCP3, StUCP and AtUCP. „Biochem. J.”. 345 Pt 2, s. 161–179, 2000. DOI: 10.1042/0264-6021:3450161. PMID: 10620491.

Borecký J, Vercesi AE. Plant uncoupling mitochondrial protein and alternative oxidase: energy metabolism and stress. „Biosci. Rep.”. 25 (3–4), s. 271–286, 2005. DOI: 10.1007/s10540-005-2889-2. PMID: 16283557.

Kalckar HM. Origins of the concept oxidative phosphorylation. „Mol. Cell. Biochem.”. 5 (1–2), s. 55–63, 1974. DOI: 10.1007/BF01874172. PMID: 4279328.

Slater EC. Mechanism of Phosphorylation in the Respiratory Chain. „Nature”. 172 (4387), s. 975, 1953. DOI: 10.1038/172975a0.

Mitchell P. Coupling of Phosphorylation to Electron and Hydrogen Transfer by a Chemi-Osmotic type of Mechanism. „Nature”. 191 (4784), s. 144, 1961. DOI: 10.1038/191144a0. PMID: 13771349.

Boyer PD, Cross RL, Momsen W. A new concept for energy coupling in oxidative phosphorylation based on a molecular explanation of the oxygen exchange reactions. „Proc. Natl. Acad. Sci. U.S.A.”. 70 (10), s. 2837–2839, 1973. DOI: 10.1073/pnas.70.10.2837. PMID: 4517936.

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ncbi.nlm.nih.gov

Mitchell P, Moyle J. Chemiosmotic hypothesis of oxidative phosphorylation. „Nature”. 213 (5072), s. 137–139, 1967. DOI: 10.1038/213137a0. PMID: 4291593.

Dimroth P, Kaim G, Matthey U. Crucial role of the membrane potential for ATP synthesis by F(1)F(o) ATP synthases. „J. Exp. Biol.”. 203 (Pt 1), s. 51–59, 2000. PMID: 10600673.

Rich PR. The molecular machinery of Keilin’s respiratory chain. „Biochem. Soc. Trans.”. 31 (Pt 6), s. 1095–1105, 2003. PMID: 14641005. [zarchiwizowane z adresu 2013-01-13].

Porter RK, Brand MD. Mitochondrial proton conductance and H+/O ratio are independent of electron transport rate in isolated hepatocytes. „Biochem. J.”. 310 (Pt 2), s. 379–382, 1995. PMID: 7654171.

Mathews FS. The structure, function and evolution of cytochromes. „Prog. Biophys. Mol. Biol.”. 45 (1), s. 1–56, 1985. DOI: 10.1016/0079-6107(85)90004-5. PMID: 3881803.

Wood PM. Why do c-type cytochromes exist?. „FEBS Lett.”. 164 (2), s. 223–226, 1983. DOI: 10.1016/0014-5793(83)80289-0. PMID: 6317447.

Crane FL. Biochemical functions of coenzyme Q10. „Journal of the American College of Nutrition”. 20 (6), s. 591–598, 2001. PMID: 11771674.

Mitchell P. Keilin’s respiratory chain concept and its chemiosmotic consequences. „Science”. 206 (4423), s. 1148–1159, 1979. DOI: 10.1126/science.388618. PMID: 388618.

Britta Søballe, Robert K. Poole, Microbial ubiquinones: multiple roles in respiration, gene regulation and oxidative stress management [pdf], „Microbiology (Reading, Engl.)”, 145 (Pt 8), 1999, s. 1817–1830, DOI: 10.1099/13500872-145-8-1817, PMID: 10463148 [dostęp 2009-02-18].

Boxma B, de Graaf RM, van der Staay GW, et al. An anaerobic mitochondrion that produces hydrogen. „Nature”. 434 (7029), s. 74–79, 2005. DOI: 10.1038/nature03343. PMID: 15744302.

J. Hirst, Energy transduction by respiratory complex I–an evaluation of current knowledge, „Biochem. Soc. Trans.”, Pt 3, 33, 2005, s. 525–9, DOI: 10.1042/BST0330525, PMID: 15916556 [zarchiwizowane z adresu 2015-11-29].

Friedrich T, Böttcher B. The gross structure of the respiratory complex I: a Lego System. „Biochim. Biophys. Acta”. 1608 (1), s. 1–9, 2004. DOI: 10.1016/j.bbabio.2003.10.002. PMID: 14741580.

Cecchini G. Function and structure of complex II of the respiratory chain. „Annu Rev Biochem”. 72, s. 77–109, 2003. DOI: 10.1146/annurev.biochem.72.121801.161700. PMID: 14527321.

Horsefield R, Iwata S, Byrne B. Complex II from a structural perspective. „Curr. Protein Pept. Sci.”. 5 (2), s. 107–118, 2004. DOI: 10.2174/1389203043486847. PMID: 15078221.

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Lenaz G. A critical appraisal of the mitochondrial coenzyme Q pool. „FEBS Lett.”. 509 (2), s. 151–155, 2001. DOI: 10.1016/S0014-5793(01)03172-6. PMID: 11741580.

Schägger H, Pfeiffer K. Supercomplexes in the respiratory chains of yeast and mammalian mitochondria. „EMBO J.”. 19 (8), s. 1777–1783, 2000. DOI: 10.1093/emboj/19.8.1777. PMID: 10775262.

Schägger H. Respiratory chain supercomplexes of mitochondria and bacteria. „Biochim. Biophys. Acta”. 1555 (1–3), s. 154–159, 2002. DOI: 10.1016/S0005-2728(02)00271-2. PMID: 12206908.

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Iuchi S, Lin EC. Adaptation of Escherichia coli to redox environments by gene expression. „Mol. Microbiol.”. 9 (1), s. 9–15, 1993. DOI: 10.1111/j.1365-2958.1993.tb01664.x. PMID: 8412675.

M.W. Calhoun i inni, Energetic efficiency of Escherichia coli: effects of mutations in components of the aerobic respiratory chain [pdf], „Journal of Bacteriology”, 175 (10), 1993, s. 3020–5, PMID: 8491720.

Boyer PD. The ATP synthase–a splendid molecular machine. „Annu. Rev. Biochem.”. 66, s. 717–749, 1997. DOI: 10.1146/annurev.biochem.66.1.717. PMID: 9242922.

Yoshida M, Muneyuki E, Hisabori T. ATP synthase–a marvellous rotary engine of the cell. „Nat. Rev. Mol. Cell Biol.”. 2 (9), s. 669–677, 2001. DOI: 10.1038/35089509. PMID: 11533724.

Schemidt RA, Qu J, Williams JR, Brusilow WS. Effects of carbon source on expression of F0 genes and on the stoichiometry of the c subunit in the F1F0 ATPase of Escherichia coli. „J. Bacteriol.”. 180 (12), s. 3205–3208, 1998. PMID: 9620972.

Nelson N, Perzov N, Cohen A, Hagai K, Padler V, Nelson H. The cellular biology of proton-motive force generation by V-ATPases. „J. Exp. Biol.”. 203 (Pt 1), s. 89–95, 2000. PMID: 10600677.

Noji H, Yoshida M. The rotary machine in the cell, ATP synthase. „J. Biol. Chem.”. 276 (3), s. 1665–1668, 2001. DOI: 10.1074/jbc.R000021200. PMID: 11080505.

Gresser MJ, Myers JA, Boyer PD. Catalytic site cooperativity of beef heart mitochondrial F1 adenosine triphosphatase. Correlations of initial velocity, bound intermediate, and oxygen exchange measurements with an alternating three-site model. „J. Biol. Chem.”. 257 (20), s. 12030–12038, 1982. PMID: 6214554.

Dimroth P. Bacterial sodium ion-coupled energetics. „Antonie Van Leeuwenhoek”. 65 (4), s. 381–395, 1994. DOI: 10.1007/BF00872221. PMID: 7832594.

Becher B, Müller V. Delta mu Na+ drives the synthesis of ATP via a delta mu Na(+)-translocating F1F0-ATP synthase in membrane vesicles of the archaeon Methanosarcina mazei Gö1. „J. Bacteriol.”. 176 (9), s. 2543–2550, 1994. PMID: 8169202.

Davies K. Oxidative stress: the paradox of aerobic life. „Biochem Soc Symp”. 61, s. 1–31, 1995. PMID: 8660387.

Rattan SI. Theories of biological aging: genes, proteins, and free radicals. „Free Radic. Res.”. 40 (12), s. 1230–1238, 2006. DOI: 10.1080/10715760600911303. PMID: 17090411.

Raha S, Robinson B. Mitochondria, oxygen free radicals, disease and ageing. „Trends Biochem Sci”. 25 (10), s. 502–508, 2000. DOI: 10.1016/S0968-0004(00)01674-1. PMID: 11050436.

Finkel T, Holbrook NJ. Oxidants, oxidative stress and the biology of ageing. „Nature”, s. 239–247, 2000. DOI: 10.1038/35041687. PMID: 11089981.

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