Occurrence, biosynthesis and function of isoprenoid quinones

Biochimica et Biophysica Acta - Bioenergetics

Volumn 1797, Issue 9, 2010, Pages 1587-1605

  Nowicka, Beatrycze ^a   Kruk, Jerzy ^a  

^a JAGIELLONIAN UNIVERSITY   (Poland)

Author keywords

Biosynthesis; Electron transport chain; Isoprenoid quinone; Naphthoquinone; Plastoquinone; Ubiquinone

Indexed keywords

ALPHA TOCOPHERYLQUINONE; BENZOQUINONE; ISOPRENOID QUINONE DERIVATIVE; MENAQUINONE; NAPHTHOQUINONE; PHYTOMENADIONE; PLASTOQUINONE; QUINONE DERIVATIVE; UBIQUINONE; UNCLASSIFIED DRUG;

BACTERIAL METABOLISM; BIOSYNTHESIS; CHLOROPLAST; CYANOBACTERIUM; MITOCHONDRION; NONHUMAN; PHOTOSYNTHESIS; PHOTOSYSTEM I; PLANT METABOLISM; PRIORITY JOURNAL; RESPIRATORY CHAIN; REVIEW; SULFOLOBALES;

BENZOQUINONES; ELECTRON TRANSPORT; NAPHTHOQUINONES; PLASTOQUINONE; UBIQUINONE; VITAMIN E; VITAMIN K 1; VITAMIN K 2;

ANIMALIA; BACTERIA (MICROORGANISMS); CYANOBACTERIA; EUKARYOTA;

EID: 77954762555     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2010.06.007     Document Type: Review

References (266)

1. Collins M.D., Jones D. Distribution of isoprenoid quinone structural types in bacteria and their taxonomic implications. Microbiol. Rev. 1981, 45:316-354.
2. Beifuss U., Tietze M. Methanophenazine and other natural biologically active phenazines. Top. Curr. Chem. 2005, 244:77-113.
3. Lenaz G., Fato R., Formiggini G., Genova M.L. The role of coenzyme Q in mitochondrial electron transport. Mitochondrion 2007, 7:8-33.
4. Fiorini R., Ragni L., Ambrosi S., Littarru G.P., Gratton E., Hazlett T. Fluorescence studies of the interactions of ubiquinol-10 with liposomes. Photochem. Photobiol. 2008, 84:209-214.
5. Lichtenthaler H.K. Regulation of prenylquinone synthesis in higher plants. Lipids and Lipid Polymers in Higher Plants 1977, 231-258. Springer, Berlin. M. Tevini, H.K. Lichtenthaler (Eds.).
6. Goodwin T.W. The prenyllipids of the membranes of higher plants. Lipids and Lipid Polymers in Higher Plants 1977, 29-47. Springer, Berlin. M. Tevini, H.K. Lichtenthaler (Eds.).
7. Kawamukai M. Biosynthesis, bioproduction and novel roles of ubiquinone. J. Biosci. Bioeng. 2002, 94:511-517.
8. Nitschke W., Kramer D.M., Riedel A., Liebl U. From naphtho- to benzoquinones-(r)evolutionary reorganisations of electron transfer chain. Photosynthesis: From Light to Biosphere 1995, Vol. I:945-950. Kluwer Academic Publishers, Dordrecht.
9. Lubben M. Cytochromes of archaeal electron transfer chains. Biochim. Biophys. Acta 1995, 1229:1-22.
10. Soballe B., Poole R.K. Microbial ubiquinones: multiple roles in respiration, gene regulation and oxidative stress management. Microbiology 1999, 145:1817-1830.
11. Schoepp-Cothenet B., Lieutaud C., Baymann F., Vermeglio A., Friedrich T., Kramerd D.M., Nitschke W. Menaquinone as pool quinone in a purple bacterium. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:8549-8554.
12. Brooijmans R., Smit B., Santos F., van Riel J., de Vos W.M., Hugenholtz J. Heme and menaquinone induced electron transport in lactic acid bacteria. Microb. Cell Factories 2009, 8:28-38.
13. Shimada H., Shida Y., Nemoto N., Oshima T., Yamagishi K. Quinone profiles of Thermoplasma acidophilum HO-62. J. Bacteriol. 2001, 183:1462-1465.
14. Biel S., Simon J., Gross R., Ruiz T., Ruitenberg M., Kroger A. Reconstitution of coupled fumarate respiration in liposomes by incorporating the electron transport enzymes isolated from Wolinella succinogenes. Eur. J. Biochem. 2002, 269:1974-1983.
15. Biswas S., Haque R., Bhuyan N.R., Bera T. Participation of chlorobiumquinone in the transplasma membrane electron transport system of Leishmania donovani promastigote: effect of near-ultraviolet light on the redox reaction of plasma membrane. Biochim. Biophys. Acta 2008, 1780:116-127.
16. Lange B.M., Rujan T., Martin W., Croteau R. Isoprenoid biosynthesis: the evolution of two ancient and distinct pathways across genomes. Proc. Natl. Acad. Sci. U. S. A. 2000, 97:13172-13177.
17. Lichtenthaler H.K. The 1-deoxy-d-xylulose-5-phosphate pathway of isoprenoid biosynthesis in plants. Annu. Rev. Plant Physiol. Plant Mol. Biol. 1999, 50:47-65.
18. 1. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:5599-5603.
19. Jiang M., Chen X.L., Guo Z.F., Cao Y., Chen M.J., Guo Z.H. Identification and characterization of (1R, 6R)-2-succinyl-6-hydroxy-2, 4-cyclohexadiene-1-carboxylate synthase in the menaquinone biosynthesis of Escherichia coli. Biochemistry 2008, 47:3426-3434.
20. Hedrick D.B., Peacock A.D., Lovley D.R., Woodard T.L., Nevin K.P., Long P.E., White D.C. Polar lipid fatty acids, LPS-hydroxy fatty acids, and respiratory quinones of three Geobacter strains, and variation with electron acceptor. J. Ind. Microbiol. Biotechnol. 2009, 36:205-209.
21. Bentley R., Meganathan R. Biosynthesis of vitamin K (menaquinone) in bacteria. Microbiol. Mol. Biol. Rev. 1982, 46:241-280.
22. Hiratsuka T., Furihata K., Ishikawa J., Yamashita H., Itoh N., Seto H., Dairi T. An alternative menaquinone biosynthetic pathway operating in microorganisms. Science 2008, 321:1670-1673.
23. Hiratsuka T., Itoh N., Seto H., Dairi T. Enzymatic properties of futalosine hydrolase, an enzyme essential to a newly identified menaquinone biosynthetic pathway. Biosci. Biotechnol. Biochem. 2009, 73:1137-1141.
24. Marcelli S.W., Chang H.-T., Chapman T., Chalk P.A., Miles R.J., Poole R.K. The respiratory chain of Helicobacter pylori: identification of cytochromes and the effects of oxygen on cytochrome and menaquinone levels. FEMS Microbiol. Lett. 1996, 138:59-64.
25. Richardson D.J. Bacterial respiration: a flexible process for a changing environment. Microbiology 2000, 146:551-571.
26. Klonowska A., Heulin T., Vermeglio A. Selenite and tellurite reduction by Shewanella oneidensis. Appl. Environ. Microbiol. 2005, 71:5607-5609.
27. Ruebush S.S., Icopini G.A., Brantley S.L., Tien M. In vitro enzymatic reduction kinetics of mineral oxides by membrane fractions from Shewanella oneidensis MR-1. Geochim. Cosmochim. Acta 2006, 70:56-70.
28. Kroger A., Biel S., Simon J., Gross R., Unden G., Lancaster C.R.D. Fumarate respiration of Wolinella succinogenes: enzymology, energetics and coupling mechanism. Biochim. Biophys. Acta 2002, 1553:23-38.
29. 3 branch of the respiratory network in mycobacteria and network adaptation occurring in response to its disruption. J. Bacteriol. 2005, 187:6300-6308.
30. Mooser D., Maneg O., MacMillan F., Malatesta F., Soulimane T., Ludwig B. The menaquinol-oxidizing cytochrome bc complex from Thermus thermophilus: protein domains and subunits. Biochim. Biophys. Acta 2006, 1757:1084-1095.
31. Dietrich W., Klimmek O. The function of methyl-menaquinone-6 and polysulfide reductase membrane anchor (PsrC) in polysulfide respiration of Wolinella succinogenes. Eur. J. Biochem. 2002, 269:1086-1095.
32. Yamamoto Y., Poyart C., Trieu-Cuot P., Lamberet G., Gruss A., Gaudu P. Roles of environmental heme, and menaquinone, in Streptococcus agalactiae. Biometals 2006, 19:205-210.
33. Brooijmans R.J.W., de Vos W.M., Hugenholtz J. Lactobacillus plantarum WCFS1 electron transport chains. Appl. Environ. Microbiol. 2009, 75:3580-3585.
34. Richardson D., Sawers G. Structural biology. PMF through the redox loop. Science 2002, 295:1842-1843.
35. Nantapong N., Otofuji A., Migita C.T., Adachi O., Toyama H., Matsushita K. Electron transfer ability from NADH to menaquinone and from NADPH to oxygen of Type II NADH dehydrogenase of Corynebacterium glutamicum. Biosci. Biotechnol. Biochem. 2005, 69:149-159.
36. 2-oxidizing subunit. Eur. J. Biochem. 2000, 267:5810-5814.
37. Lancaster C.R.D., Simon J. Succinate:quinone oxidoreductases from ε-proteobacteria. Biochim. Biophys. Acta 2002, 1553:84-101.
38. Lancaster C.R.D. Wolinella succinogenes quinol:fumarate reductase and its comparison to E. coli succinate:quinone reductase. FEBS Lett. 2003, 555:21-28.
39. Kurokawa T., Sakamoto J. Purification and characterization of succinate:menaquinone oxidoreductase from Corynebacterium glutamicum. Arch. Microbiol. 2005, 183:317-324.
40. Fernandes A.S., Konstantinov A.A., Teixeira M., Pereira M.M. Quinone reduction by Rhodothermus marinus succinate:menaquinone oxidoreductase is not stimulated by the membrane potential. Biochem. Biophys. Res. Commun. 2005, 565-570.
41. Madej M.G., Nasiri H.R., Hilgendorff N.S., Schwalbe H., Unden G., Lancaster C.R.D. Experimental evidence for proton motive force-dependent catalysis by the diheme-containing succinate:menaquinone oxidoreductase from the gram-positive bacterium Bacillus licheniformis. Biochemistry 2006, 45:15049-15055.
42. Xin Y., Lu Y.K., Fromme R., Fromme P., Blankenship R.E. Purification, characterization and crystallization of menaquinol:fumarate oxidoreductase from the green filamentous photosynthetic bacterium Chloroflexus aurantiacus. Biochim. Biophys. Acta 2009, 1787:86-96.
43. Azarkina N.V., Konstantinov A.A. Energization of Bacillus subtilis membrane vesicles increases catalytic activity of succinate:menaquinone oxidoreductase. Biochemistry (Moscow) 2010, 75:63-77.
44. Maklashina E., Hellwig P., Rothery R.A., Kotlyar V., Sher Y., Weiner J.H., Cecchini G. Differences in protonation of ubiquinone and menaquinone in fumarate reductase from Escherichia coli. J. Biol. Chem. 2006, 281:26655-26664.
45. Pires R.H., Lourenc A.I., Morais F., Teixeira M., Xavier A.V., Saraiva L.M., Pereira I.A.C. A novel membrane-bound respiratory complex from Desulfovibrio desulfuricans ATCC 27774. Biochim. Biophys. Acta 2003, 1605:67-82.
46. Jormakka M., Tornroth S., Byrne B., Iwata S. Molecular basis of proton motive force generation: structure of formate dehydrogenase-N. Science 2002, 295:1863-1868.
47. Pinho D., Besson S., Silva P.J., de Castro B., Moura I. Isolation and spectroscopic characterization of the membrane-bound nitrate reductase from Pseudomonas chlororaphis DSM 50135. Biochim. Biophys. Acta 2005, 1723:151-162.
48. Brondijk T.H.C., Fiegen D., Richardson D.J., Cole J.A. Roles of NapF, NapG and NapH, subunits of the Escherichia coli periplasmic nitrate reductase, in ubiquinol oxidation. Mol. Microbiol. 2002, 44:245-255.
49. Giordani R., Buc J. Evidence for two different electron transfer pathways in the same enzyme, nitrate reductase A from Escherichia coli. Eur. J. Biochem. 2004, 271:2400-2407.
50. Ma J., Kobayashi D.Y., Yee N. Role of menaquinone biosynthesis genes in selenate reduction by Enterobacter cloacae SLD1a-1 and Escherichia coli K12. Environ. Microbiol. 2009, 11:149-158.
51. Jormakka M., Yokoyama K., Yano T., Tamakoshi M., Akimoto S., Shimamura T., Curmi P., Iwata S. Molecular mechanism of energy conservation in polysulfide respiration. Nat. Struct. Mol. Biol. 2008, 15:730-737.
52. 1 complexes of microorganisms. Microbiol. Mol. Biol. Rev. 1990, 54:101-129.
53. Schutz M., Brugna M., Lebrun E., Baymann F., Huber R., Stetter K.O., Hauska G., Toci R., Lemesle-Meunier D., Tron P., Schmidt C., Nitschke W. Early evolution of cytochrome bc complexes. J. Mol. Biol. 2000, 300:663-675.
54. Kusumoto K., Sakiyama M., Sakamoto J., Noguchi S., Sone N. Menaquinol oxidase activity and primary structure of cytochrome bd from the amino-acid fermenting bacterium Corynebacterium glutamicum. Arch. Microbiol. 2000, 173:390-397.
55. Junemann S. Cytochrome bd terminal oxidase. Biochim. Biophys. Acta 1997, 1321:107-127.
56. Simon J., Pisa R., Stein T., Eichler R., Klimmek O., Gross R. The tetraheme cytochrome c NrfH is required to anchor the cytochrome c nitrite reductase (NrfA) in the membrane of Wolinella succinogenes. Eur. J. Biochem. 2001, 268:5776-5782.
57. Schwalb C., Chapman S.K., Reid G.A. The tetraheme cytochrome CymA is required for anaerobic respiration with dimethyl sulfoxide and nitrite in Shewanella oneidensis. Biochemistry 2003, 42:9491-9497.
58. Fu Q.S., Boonchayaanant B., Tang W., Trost B.M., Criddle C.S. Simple menaquinones reduce carbon tetrachloride and iron. Biodegradation 2009, 20:109-116.
59. Wallace B.J., Young I.G. Role of quionones in electron transport to oxygen and nitrate in Escherichia coli: studies with a ubiA menA double mutants. Biochim. Biophys. Acta 1977, 461:84-100.
60. Wissenbach U., Kroger A., Unden G. The specific functions of menaquinone and demethylmenaquinone in anaerobic respiration with fumarate, dimethylsulfoxide, trimethylamine N-oxide and nitrate by Escherichia coli. Arch. Microbiol. 1990, 154:60-66.
61. Ke B. Photosynthesis: Photobiochemistry and Photobiophysics. Advances of Photosynthesis 2001, Vol. 10. Kluwer Academic Publishers, Dordrecht.
62. Hale M.B., Blankenship R.E., Fuller R.C. Menaquinone is the sole quinone in the facultatively aerobic green photosynthetic bacterium Chloroflexus aurantiacus. Biochim. Biophys. Acta 1983, 723:376-382.
63. Hauska G., Schoedl T., Remigy H., Tsiotis G. The reaction center of green sulfur bacteria. Biochim. Biophys. Acta 2001, 1507:260-277.
64. Neerken S., Ames J. The antenna reaction center complex of heliobacteria: composition, energy conversion and electron transfer. Biochim. Biophys. Acta 2001, 1507:278-290.
65. Oh-oka H. Type 1 reaction center of photosynthetic heliobacteria. Photochem. Photobiol. 2007, 83:177-186.
66. B and containing plastoquinone or exchanged 9,10-anthraquinone. J. Biol. Chem. 2005, 280:12371-12381.
67. Mimuro M., Tsuchiya T., Inoue H., Sakuragi Y., Itoh Y., Gotoh T., Miyashita H., Bryant D.A., Kobayashi M. The secondary electron acceptor of photosystem I in Gloeobacter violaceus PCC 7421 is menaquinone-4 that is synthesized by a unique but unknown pathway. FEBS Lett. 2005, 579:3493-3496.
68. Ikeda Y., Komura M., Watanabe M., Minami C., Koike H., Itoh S., Kashino Y., Satoh K. Photosystem I complexes associated with fucoxanthin-chlorophyll-binding proteins from a marine centric diatom, Chaetoceros gracilis. Biochim. Biophys. Acta 2008, 1777:351-361.
69. Frigaard N.U., Takaichi S., Hirota M., Shimada K., Matsuura K. Quinones in chlorosomes of green sulfur bacteria and their role in the redox-dependent fluorescence studied in chlorosome-like bacteriochlorophyll c aggregates. Arch. Microbiol. 1997, 167:343-349.
70. Frigaard N.U., Matsuura K., Hirota M., Miller M., Cox R.P. Studies of the location and function of isoprenoid quinones in chlorosomes from green sulfur bacteria. Photosynth. Res. 1998, 58:81-90.
71. Kim H., Li H., Maresca J.A., Bryant D.A., Savikhin S. Triplet exciton formation as a novel photoprotection mechanism in chlorosomes of Chlorobium tepidum. Biophys. J. 2007, 93:192-201.
72. Thummer R., Klimmek O., Schmitz R.A. Biochemical studies of Klebsiella pneumoniae NifL reduction using reconstituted partial anaerobic respiratory chains of Wolinella succinogenes. J. Biol. Chem. 2007, 282:12517-12526.
73. Holsclaw C.M., Sogi K.M., Gilmore S.A., Schelle M.W., Leavell M.D., Bertozzi C.R., Leary J.A. Structural characterization of a novel sulfated menaquinone produced by stf3 from Mycobacterium tuberculosis. ACS Chem. Biol. 2008, 3:619-624.
74. Lichtenthaler H.K. Verbreitung und relative Konzentration der lipophilen Plastidenchinone in grunen Pflanzen. Planta 1968, 81:140-152.
75. 1 in chloroplasts. Nature 1962, 194:1282.
76. Lichtenthaler H.K., Park R.B. Chemical composition of chloroplast lamellae from spinach. Nature 1963, 198:1070-1072.
77. Lichtenthaler H.K., Calvin M. Quinone and pigment composition of chloroplasts and quantasome aggregates from Spinacia oleracea. Biochim. Biophys. Acta 1964, 79:30-40.
78. Lichtenthaler H.K. Localization and functional concentrations of lipoquinones in chloroplasts. Progress in Photosynthesis Research 1969, vol. I:304-314. Laupp Press, Tübingen. H. Metzner (Ed.).
79. Interschick-Niebler E., Lichtenthaler H.K. Partition of phylloquinone K1 between digitonin particles and chlorophyll-proteins of chloroplast membranes from Nicotiana tabacum. Z. Naturforsch. 1981, 36c:276-283.
80. Lichtenthaler H.K., Sprey B. Über die osmiophilen globulären Lipideinschlüsse der Chloroplasten. Z. Naturforsch. 1966, 21b:690-697.
81. Lichtenthaler H.K. Biosynthesis, accumulation and emission of carotenoids, tocopherol, plastoquinone and isoprene in leaves under high photosynthetic irradiance. Photosynth. Res. 2007, 92:163-179.
82. Lohmann A., Schottler M.A., Brehelin C., Kessler F., Bock R., Cahoon E.B., Dormann P. Deficiency in phylloquinone (Vitamin K1) methylation affects prenyl quinone distribution, photosystem I abundance, and anthocyanin accumulation in the Arabidopsis AtmenG Mutant. J. Biol. Chem. 2006, 281:40461-40472.
83. 1) biosynthesis originated from a fusion of four eubacterial genes. J. Biol. Chem. 2006, 281:17189-17196.
84. Lichtenthaler H.K., Prenzel U., Douce R., Joyard J. Localization of prenylquinones in the envelope of spinach chloroplasts. Biochim. Biophys. Acta 1981, 641:99-105.
85. Lochner K., Döring O., Böttger M. Phylloquinone, what can we learn from plants?. Biofactors 2003, 18:73-78.
86. Lichtenthaler H.K. Die Verbreitung der lipophilen Plastidenchinone in nicht-grunen Pflanzengeweben. Z. Pflanzenphysiol. 1968, 59:195-210.
87. 1 quinol in leaf tissues. Phytochemistry 2008, 69:2457-2462.
88. Bouvier F., Rahier A., Camara B. Biogenesis, molecular regulation and function of plant isoprenoids. Prog. Lipid Res. 2005, 44:357-429.
89. 1) by spinach chloroplasts. Eur. J. Biochem. 1981, 117:329-332.
90. Joliot P., Joliot A. In vivo analysis of the electron transfer within photosystem I: are the two phylloquinones involved?. Biochemistry 1999, 38:11130-11136.
91. Guergova-Kuras M., Boudreaux B., Joliot A., Joliot P., Redding K. Evidence for two active branches for electron transfer in photosystem I. Proc. Natl. Acad. Sci. U. S. A. 2001, 98:4437-4442.
92. Lefebvre-Legendre L., Rappaport F., Finazzi G., Ceol M., Grivet C., Hopfgartner G., Rochaix J.D. Loss of phylloquinone in Chlamydomonas affects plastoquinone pool size and photosystem II synthesis. J. Biol. Chem. 2007, 282:13250-13263.
93. 1 hydroquinone oxidase activity. Biochim. Biophys. Acta 2000, 1463:448-458.
94. Van Winckel M., De Bruyne R., Van De Velde S., Van Biervliet S. Vitamin K, an update for the paediatrician. Eur. J. Pediatr. 2009, 168:127-134.
95. 2) in mice: two possible routes for menaquinone-4 accumulation in cerebra of mice. J. Biol. Chem. 2008, 283:11270-11279.
96. Vermeer C., Schurgers L. A comprehensive review of vitamin K and the vitamin K antagonists. Hematol. Oncol. Clin. N. Am. 2000, 14:339-353.
97. Kaneki M., Hosoi T., Ouchi Y., Orimo H. Pleiotropic actions of vitamin K: protector of bone health and beyond?. Nutrition 2006, 22:845-852.
98. Wallin R., Schurgers Leon, Wajih N. Effects of the blood coagulation vitamin K as an inhibitor of arterial calcification. Thromb. Res. 2008, 122:411-417.
99. Shea M.K., Booth S.L. Update on the role of vitamin K in skeletal health. Nutr. Rev. 2008, 66:549-557.
100. 2 regulation of bone homeostasis is mediated by the steroid and xenobiotic receptor SXR. J. Biol. Chem. 2003, 278:43919-43927.
101. Igarashi M., Yogiashi Y., Mihara M., Takada I., Kitagawa H., Kato S. Vitamin K induces osteoblast differentiation through pregnane X receptor-mediated transcriptional control of the Msx2 gene. Mol. Cell. Biol. 2007, 27:7947-7954.
102. Suhara Y., Murakami A., Nakagawa K., Mizuguchi Y., Okano T. Comparative uptake, metabolism, and utilization of menaquinone-4 and phylloquinone in human cultured cell lines. Bioorg. Med. Chem. 2006, 14:6601-6607.
103. Saxena S.P., Israels E.D., Israels L.G. Novel vitamin K-dependent pathways regulating cell survival. Apoptosis 2001, 6:57-68.
104. Denisova N.A., Booth Vitamin S.L. K and sphingolipid metabolism: evidence to date. Nutr. Rev. 2005, 63:111-121.
105. 2 selectively induces apoptosis of blastic cells in mye-lodysplastic syndrome: flow cytometric detection of apoptotic cells using APO2.7 monoclonal antibody. Leukemia 1998, 12:1392-1397.
106. 2 on colon cancer cell lines via different types of cell death including autophagy and apoptosis. Int. J. Mol. Med. 2009, 23:709-716.
107. Li J., Wang H., Rosenberg P.A. Vitamin K prevents oxidative cell death by inhibiting activation of 12-lipoxygenase in developing oligodendrocytes. J. Neurosci. Res. 2009, 87:1997-2005.
108. Shearer M.J., Newman P. Metabolism and cell biology of vitamin K. Thromb. Haemost. 2008, 100:530-547.
109. De Rosa M., De Rosa S., Gambacorta A., Minale L. Caldariellaquinone, a unique benzo[b]thiophen-4, 7-quinone from Caldariella acidophila, an extremely thermophilic and acidophilic bacterium. J. Chem. Soc. Perkin Trans. 1977, 1:653-657.
110. Zhou D., White R.H. Biosynthesis of Caldariellaquinone in Sulfolobus spp. J. Bacteriol. 1989, 171:6610-6616.
111. Müller F.H., Bandeiras T.M., Urich T., Teixeira M., Gomes C.M., Kletzin A. Coupling of the pathway of sulphur oxidation to dioxygen reduction: characterization of a novel membrane-bound thiosulphate:quinone oxidoreductase. Mol. Microbiol. 2004, 53:1147-1160.
112. Ernster L., Dallner G. Biochemical, physiological and medical aspects of ubiquinone function. Biochim. Biophys. Acta 1995, 1271:195-204.
113. Bentinger M., Brismar K., Dallner G. The antioxidant role of coenzyme Q. Mitochondrion 2007, 7:41-50.
114. Crane F.L. Discovery of ubiquinone (coenzyme Q) and an overview of function. Mitochondrion 2007, 7:2-7.
115. Crane F.L. Distribution of ubiquinones. Biochemistry of Quinones 1965, 183-206. Academic Press, London. R. Morton (Ed.).
116. Takahashi S., Ohtani T., Satoh H., Nakamura Y., Kawamukai M., Kadowaki K. Development of coenzyme Q10-enriched rice using sugary and shrunken mutants. Biosci. Biotechnol. Biochem. 2010, 74:182-184.
117. Schindler S., Lichtenthaler H.K. Distrubution and levels of ubiquinone homologues in higher plants. Biochemistry and Metabolism of Plant Lipids 1982, 545-548. Elsevier Biomedical Press B.V. J.F.G.M. Wintermans, P.J.C. Kuiper (Eds.).
118. Clarke C.F. New advance in coenzyme Q biosynthesis. Protoplasma 2000, 213:134-147.
119. Tran U.P.C., Clarke C.F. Endogenous synthesis of coenzyme Q in eukaryotes. Mitochondrion 2007, 7:62-71.
120. Szkopińska A. Ubiquinone. Biosynthesis of quinone ring and its isoprenoid side chain. Intracellular localization. Acta Biochim. Pol. 2000, 47:469-480.
121. Meganathan R. Ubiquinone biosynthesis in microorganisms. FEMS Microbiol. Lett. 2001, 203:131-139.
122. Kawamukai M. Biosynthesis and bioproduction of coenzyme Q10 by yeast and other organisms. Biotechnol. Appl. Biochem. 2009, 53:217-226.
123. Padilla-Lopez S., Jimenez-Hidalgo M., Martin-Montalvo A., Clarke C.F., Navas P., Santos-Ocana C. Genetic evidence for the requirement of the endocytic pathway in the uptake of coenzyme Q6 in Saccharomyces cerevisiae. Biochim. Biophys. Acta 2009, 1788:1238-1248.
124. Saito Y., Fukuhara A., Nishio K., Hayakawa M., Ogawa Y., Sakamoto H., Fujii K., Yoshida Y., Niki E. Characterization of cellular uptake and distribution of coenzyme Q10 and vitamin E in PC12 cells. J. Nutr. Biochem. 2009, 20:350-357.
125. Yoshida H., Kotani Y., Ochiai K., Araki K. Production of ubiquinone-10 using bacteria. J. Gen. Appl. Microbiol. 1998, 44:19-26.
126. Jeya M., Moon H.J., Lee J.L., Kim I.W., Lee J.K. Current state of coenzyme Q10 production and its applications. Appl. Microbiol. Biotechn. 2010, 85:1653-1663.
127. Miles M.V. The uptake and distribution of coenzyme Q(10). Mitochondrion 2007, 7:72-77.
128. Lenaz G., Genova M.L. Structural and functional organization of the mitochondrial respiratory chain: a dynamic super-assembly. Int. J. Biochem. Cell Biol. 2009, 41:1750-1772.
129. Lenaz G., Genova M.L. Mobility and function of Coenzyme Q (ubiquinone) in the mitochondrial respiratory chain. Biochim. Biophys. Acta 2009, 1787:563-573.
130. 1 complex stability in yeast coq mutants. J. Biol. Chem. 2002, 277:10973-10981.
131. Barros M.H., Johnson A., Gin P., Marbois B.N., Clarke C.F., Tzagoloff A. The Saccharomyces cerevisiae COQ10 gene encodes a START domain protein required for function of coenzyme Q in respiration. J. Biol. Chem. 2005, 280:42627-42635.
132. Cui T.Z., Kawamukai M. Coq10, a mitochondrial coenzyme Q binding protein, is required for proper respiration in Schizosaccharomyces pombe. FEBS J. 2009, 276:748-759.
133. Busso C., Bleicher L., Ferreira-Junior J.R., Barros M.H. Site-directed mutagenesis and structural modeling of Coq10p indicate the presence of a tunnel for coenzyme Q6 binding. FEBS Lett. 2010, 584:1609-1614.
134. Rasmusson A.G., Geisler D.A., Moller I.M. The multiplicity of dehydrogenases in the electron transport chain of plant mitochondria. Mitochondrion 2008, 8:47-60.
135. Garofano, Eschemann A., Brandt U., Kerscher S. Substrate-inducible versions of internal alternative NADH: ubiquinone oxidoreductase from Yarrowia lipolytica. Yeast 2006, 23:1129-1136.
136. Dym O., Pratt E.A., Ho C., Eisenberg D. The crystal structure of d-lactate dehydrogenase, a peripheral membrane respiratory enzyme. Proc. Natl. Acad. Sci. U. S. A. 2000, 97:9413-9418.
137. Mustafa G., Migita C.T., Ishikawa Y., Kobayashi K., Tagawa S., Yamada M. Menaquinone as well as ubiquinone as a bound quinone crucial for catalytic activity and intramolecular electron transfer in Escherichia coli membrane-bound glucose dehydrogenase. J. Biol. Chem. 2008, 283:28169-28175.
138. Mustafa G., Ishikawa Y., Kobayashi K., Migita C.T., Elias M.D., Nakamura S., Tagawa S., Yamada M. Amino acid residues interacting with both the bound quinone and coenzyme, pyrroloquinoline quinone, in Escherichia coli membrane-bound glucose dehydrogenase. J. Biol. Chem. 2008, 283:22215-22221.
139. Ling M., Allen S.W., Wood J.M. Sequence analysis identifies the proline dehydrogenase and delta 1-pyrroline-5-carboxylate dehydrogenase domains of the multifunctional Escherichia coli PutA protein. J. Mol. Biol. 1994, 243:950-956.
140. Matsushita K., Kobayashi Y., Mizuguchi M., Toyama H., Adachi O., Sakamoto K., Miyoshi H. A tightly bound quinone functions in the ubiquinone reaction sites of quinoprotein alcohol dehydrogenase of an acetic acid bacterium, Gluconobacter suboxydans. Biosci. Biotechnol. Biochem. 2008, 72:2723-2731.
141. Ermler U., Michel H., Schiffer M. Structure and function of the photosynthetic reaction center from Rhodobacter sphaeroides. J. Bioenerg. Biomembr. 1994, 26:5-15.
142. Shibata H., Takahashi M., Yamaguchi I., Kobayashi S. Sulfide oxidation by gene expression of sulfide-quinone oxidoreductase and ubiquinone-8 biosynthase in Eschericha coli. J. Biosci. Bioeng. 1999, 88:244-249.
143. Griesbeck C., Hauska G., Schütz M. Biological sulfide oxidation: sulfide-quinone reductase (SQR), the primary reaction. Rec. Res. Dev. Microb. 2000, 4:179-203.
144. Chan L.K., Morgan-Kiss R.M., Hanson T.E. Functional analysis of three sulfide:quinone oxidoreductase homologs in Chlorobaculum tepidum. J. Bacteriol. 2009, 191:1026-1034.
145. Hildebrandt T.M., Grieshaber M.K. Three enzymatic activities catalyze the oxidation of sulfide to thiosulfate in mammalian and invertebrate mitochondria. FEBS J. 2008, 275:3352-3361.
146. Theissen U., Martin W. Sulfide: quinone oxidoreductase (SQR) from the lugworm Arenicola marina shows cyanide- and thioredoxin dependent activity. FEBS J. 2008, 275:1131-1139.
147. Theissen U., Hoffmeister M., Grieshaber M., Martin W. Single eubacterial origin of eukaryotic sulfide:quinone oxidoreductase, a mitochondrial enzyme conserved from the early evolution of eukaryotes during anoxic and sulfidic times. Mol. Biol. Evol. 2003, 20:1564-1574.
148. 2S be the third endogenous gaseous transmitter?. FASEB J. 2002, 16:1792-1798.
149. m552 of the ammonia-oxidizing Nitrosomonas europaea: a ubiquinone reductase. Biochemistry 2008, 47:6539-6551.
150. + translocating NADH:quinone oxidoreductase from Vibrio harveyi. Biochemistry 2007, 46:10186-10191.
151. +-translocating NADH: ubiquinone oxidoreductase of Azotobacter vinelandii negatively regulates alginate synthesis. Microbiology 2009, 155:249-256.
152. Hase C.C., Fedorova N.D., Galperin M.Y., Dibrov P.A. Sodium ion cycle in bacterial pathogens: evidence from cross-genome comparisons. Microbiol. Mol. Biol. Rev. 2001, 65:353-370.
153. Xie T., Yu L., Bader M.W., Bardwell J.C., Yu C.A. Identification of the ubiquinone-binding domain in the disulfide catalyzed disulfide bond protein. J. Biol. Chem. 2002, 277:1649-1652.
154. Inaba K., Murakami S., Suzuki M., Nakagawa A., Yamashita E., Okada K., Ito K. Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation. Cell 2006, 127:789-801.
155. Inaba K., Ito K. Structure and mechanisms of the DsbB-DsbA disulfide bond generation machine. Biochim. Biophys. Acta 2008, 1783:520-529.
156. Georgelis D., Kwon O., Lin E.C.C. Quinones as the redox signal for the Arc two-component system of bacteria. Science 2001, 292:2314-2317.
157. Jung W.S., Jung Y.R., Oh D.B., Kang H.A., Lee S.Y., Chavez-Canales M., Georgellis D., Kwon Oh. Characterization of the Arc two-component signal transduction system of the capnophilic rumen bacterium Mannheimia succiniciproducens. FEMS Microbiol. Lett. 2008, 284:109-119.
158. Malpica R., Franco B., Rodriguez C., Kwon O., Georgellis D. Identification of a quinone-sensitive redox switch in the ArcB sensor kinase. Proc. Natl. Acad. Sci. U. S. A. 2004, 101:13318-13323.
159. Bekker M., Alexeeva S., Laan W., Sawers G., Teixeira de Mattos J., Hellingwerf K. The ArcBA two-component system of Escherichia coli is regulated by the redox state of both the ubiquinone and the menaquinone pool. J. Bacteriol. 2010, 192:746-754.
160. Swem L.R., Elsen S., Bird T.H., Swem D.L., Koch H.G., Myllykallio H., Daldal F., Bauer C.E. The RegB/RegA two-component regulatory system controls synthesis of photosynthesis and respiratory electron transfer components in Rhodobacter capsulatus. J. Mol. Biol. 2001, 309:121-138.
161. Swem L.R., Gong X., Yu C.A., Bauer C.E. Identification of a ubiquinone-binding site that affects autophosphorylation of the sensor kinase RegB. J. Biol. Chem. 2006, 281:6768-6775.
162. Grammel H., Ghosh R. Redox-state dynamics of ubiquinone-10 imply cooperative regulation of photosynthetic membrane expression in Rhodospirillum rubrum. J. Bacteriol. 2008, 190:4912-4921.
163. Bock A., Gross R. The unorthodox histidine kinases BvgS and EvgS are responsive to the oxidation status of a quinone electron carrier. Eur. J. Biochem. 2002, 269:3479-3484.
164. Groneberg D.A., Kindermann B., Althammer M., Klapper M., Vormannd J., Littarrue G.P., Doring F. Coenzyme Q10 affects expression of genes involved in cell signalling, metabolism and transport in human CaCo-2 cells. Int. J. Biochem. Cell Biol. 2005, 37:1208-1218.
165. Fontaine E., Eriksson O., Ichas F., Bernardi P. Regulation of the permeability transition pore in skeletal muscle mitochondria. Modulation by electron flow through the respiratory chain complex I. J. Biol. Chem. 1998, 273:12662-12668.
166. Echtay K.S., Winkler E., Klingenberg M. Coenzyme Q is an obligatory cofactor for uncoupling protein function. Nature 2000, 408:609-613.
167. Swida-Barteczka A., Woyda-Ploszczyca A., Sluse F.E., Jarmuszkiewicz W. Uncoupling protein 1 inhibition by purine nucleotides is under the control of the endogenous ubiquinone redox state. Biochem. J. 2009, 424:297-306.
168. Gille L., Nohl H. The existence of a lysosomal redox chain and the role of ubiquinone. Arch. Biochem. Biophys. 2000, 375:347-354.
169. Hamiaux C., Stanley D., Greenwood D.R., Baker E.N., Newcomb R.D. Crystal structure of Epiphyas postvittana takeout 1 with bound ubiquinone supports a role as ligand carriers for takeout proteins in insects. J. Biol. Chem. 2009, 284:3496-3503.
170. James A.M., Smith R.A.J., Murphya M.P. Antioxidant and prooxidant properties of mitochondrial coenzyme Q. Arch. Biochem. Biophys. 2004, 423:47-56.
171. Frei B., Kim M.C., Ames B.N. Ubiquinol-10 is an effective lipid-soluble antioxidant at physiological concentration. Proc. Natl. Acad. Sci. U. S. A. 1990, 87:4879-4883.
172. Maroz A., Anderson R.F., Smith R.A.J., Murphy M.P. Reactivity of ubiquinone and ubiquinol with superoxide and the hydroperoxyl radical: implications for in vivo antioxidant activity. Free Radic. Biol. Med. 2009, 46:105-109.
173. Petillo D., Hultin H.O. Ubiquinone-10 as an antioxidant. J. Food Biochem. 2008, 32:173-181.
174. Shi H., Noguchi N., Niki E. Comparative study on dynamics of antioxidative action of α-tocopheryl hydroquinone, ubiquinol, and α-tocopherol against lipid peroxidation. Free Radic. Biol. Med. 1999, 27:334-346.
175. Radi R., Cassina A., Hodara R. Nitric oxide and peroxynitrite interactions with mitochondria. Biol. Chem. 2002, 383:401-409.
176. Takahashi T., Okamoto T., Kishi T. Characterization of NADPH-dependent ubiquinone reductase activity in rat liver cytosol: effect of various factors on ubiquinone-reducing activity and discrimination from other quinone reductases. J. Biochem. 1996, 119:256-263.
177. Beyer R.E., Seguraaguilar J., Dibernardo S., Cavazzoni M., Fato R., Fiorentini D., Galli M.C., Setti M., Landi L., Lenaz G. The role of DT-diaphorase in the maintenance of the reduced antioxidant form of coenzyme Q in membrane systems. Proc. Natl. Acad. Sci. 1996, 93:2528-2532.
178. Navas P., Villalba J.M., de Cabo R. The importance of plasma membrane coenzyme Q in aging and stress responses. Mitochondrion 2007, 7:34-40.
179. Bjornstedt M., Nordman T., Olsson J.M. Extramitochondrial reduction of ubiquinone by flavoenzymes. Meth. Enzymol. 2004, 378:131-138.
180. Kontush A., Hubner C., Finckh B., Kohlschutter A., Beisiegel U. Antioxidative activity of ubiquinol-10 at physiologic concentrations in human low density lipoprotein. Biochim. Biophys. Acta 1995, 1258:177-187.
181. Turunen M., Olsson J., Dallner G. Metabolism and function of coenzyme Q. Biochim. Biophys. Acta 2004, 1660:171-199.
182. Bentinger M., Turunen M., Zhang X.X., Wan Y.J., Dallner G. Involvement of retinoid X receptor alpha in coenzyme Q metabolism. J. Mol. Biol. 2003, 326:795-803.
183. Muralikrishnanan D., Jun R. The emerging role of coenzyme Q-10 in aging, neurodegeneration, cardiovascular disease, cancer and diabetes mellitus. Curr. Neurovasc. Res. 2005, 2:447-459.
184. Dhanasekaren M., Ren J. The emerging role of coenzyme Q10 in aging, neurodegeneration, cardiovascular disease, cancer, and diabetes. Curr. Neurovasc. Res. 2005, 2:1-13.
185. Hyun D.H., Hernandez J.O., Mattson M.P., de Cabo R. The plasma membrane redox system in aging. Ageing Res. Rev. 2006, 5:209-220.
186. Pepe S., Marasco S.F., Haas S.J., Sheeran F.L., Krum H., Rosenfeldt F.L. Coenzyme Q10 in cardiovascular disease. Mitochondrion 2007, 7:154-167.
187. Kumar A., Kaur H., Devi P., Mohan V. Role of coenzyme Q10 (CoQ10) in cardiac disease, hypertension and Meniere-like syndrome. Pharm. Ther. 2009, 124:259-268.
188. Yap L.P., Garcia J.V., Han D., Cadenas E. The energy-redox axis in aging and age-related neurodegeneration. Adv. Drug Deliv. Rev. 2009, 61:1283-1298.
189. Glover J., Threlfall D.R. A new quinone (rhodoquinone) related to ubiquinone in the photosynthetic bacterium Rhodospirillum rubrum. Biochem. J. 1962, 85:14-15.
190. Hirashi A., Hoshino Y. Distribution of rhodoquinone in Rhodospirillaceae and its taxonomic implications. J. Gen. Appl. Microbiol. 1984, 30:435-448.
191. Hiraishi A., Shin Y.-K., Sugiyama J. Brachymonas denitrificans gen. nov., sp. nov., an aerobic chemoorganotrophic bacterium which contains rhodoquinones, and evolutionary relations of rhodoquinone producers to bacterial species with various quinone classes. J. Gen. Appl. Microbiol. 1995, 41:99-117.
192. Van Hellemond J.J., Klockiewicz M., Gaasenbeek C.P.H., Roos M.H., Tielens A.G.M. Rhodoquinone and complex II of the electron transport chain in anaerobically functioning eukaryotes. J. Biol. Chem. 1995, 270:31065-31070.
193. Brajcich B.C., Iarocci A.L., Johnstone L.A.G., Morgan R.K., Lonjers Z.T., Hotchko M.J., Muhs J.D., Kieffer A., Reynolds B.J., Mandel S.M., Marbois B.N., Clarke C.F., Shepherd J.N. Evidence that ubiquinone is a required intermediate for rhodoquinone biosynthesis in Rhodospirillum rubrum. J. Bacteriol. 2010, 192:436-445.
194. Jonassen T., Larsen P.L., Clarke C.F. A dietary source of coenzyme Q is essential for growth of long-lived Caenorhabditis elegans clk-1 mutants. Proc. Natl. Acad. Sci. U. S. A. 2001, 98:421-426.
195. Hoffmeister M., van der Klei A., Rotte C., van Grinsven K.W.A., van Hellemond J.J., Henze K., Tielens A.G.M., Martin W. Euglena gracilis rhodoquinone:ubiquinone ratio and mitochondrial proteome differ under aerobic and anaerobic conditions. J. Biol. Chem. 2004, 279:22422-22429.
196. Miyadera H., Hiraishi A., Miyoshi H., Sakamoto K., Mineki R., Murayama K., Nagashima K.V.P., Matsuura K., Kojima S., Kita K. Complex II from phototrophic purple bacterium Rhodoferax fermentans displays rhodoquinol-fumarate reductase activity. Eur. J. Biochem. 2003, 270:1863-1874.
197. Crane F.L. Discovery of plastoquinones: a personal perspective. Photosynth. Res. 2010, 103:195-209.
198. Etman-Gervais C., Tendille C., Polonsky J. 3-demethylplastoquinone-9 et 3-demethylplastoquinone-8 isolees des bulbes d'Iris hollandica. New J. Chem. 1977, 1:323-325.
199. Barr R., Henninger M.D., Crane F.L. Comparative studies on plastoquinone. II. Analysis of plastoquinones A, B, C and D. Plant Physiol. 1967, 42:1246-1254.
200. Kruk J., Burda K., Schmid G.H., Radunz A., Strzałka K. Function of plastoquinones B and C as electron acceptors in photosystem II. Fatty acids analysis of plastoquinone. Photosynth. Res. 1998, 58:203-209.
201. Kruk J., Strzałka K. Identification of plastoquinone-C in spinach and maple leaves by reverse-phase high-performance liquid chromatography. Phytochemistry 1998, 49:2267-2271.
202. Gruszka J., Pawlak A., Kruk J. Tocochromanols, plastoquinol and other biological prenyllipids as singlet oxygen quenchers-determination of singlet oxygen quenching rate constants and oxidation products. Free Radic. Biol. Med. 2008, 45:920-928.
203. DellaPenna D. A decade in progress in understanding vitamin E synthesis in plants. J. Plant Physiol. 2005, 162:729-737.
204. Soll J., Schultz G., Joyard J., Douce R., Block M.A. Localization and synthesis of prenylquinones in isolated outer and inner envelope membranes from spinach-chloroplasts. Arch. Biochem. Biophys. 1985, 238:290-299.
205. Swiezewska E., Dallner G., Andersson B., Ernster L. Biosynthesis of ubiquinone and plastoquinone in the endoplasmic reticulum-golgi membranes of spinach leaves. J. Biol. Chem. 1993, 268:1494-1499.
206. Dahnhardt D., Falk J., Appel J., van der Kooij T.A.W., Schulz-Friedrich R., Krupinska K. The hydroxyphenylpyruvate dioxygenase from Synechocystis sp. PCC 6803 is not required for plastoquinone biosynthesis. FEBS Lett. 2002, 523:177-181.
207. Kruk J., Strzałka K. Redox changes of cytochrome b-559 in the presence of plastoquinones. J. Biol. Chem. 2001, 276:86-91.
208. Guskov A., Kern J., Gabdulkhakov A., Broser M., Zouni A., Saenger W. Cyanobacterial photosystem II at 2.9Å resolution and the role of quinones, lipids, channels and chloride. Nat. Struct. Mol. Biol. 2009, 16:334-342.
209. Hirano M., Satoh K., Katoh S. Plastoquinone as a common link between photosynthesis and respiration in a blue-green alga. Photosynth. Res. 1980, 1:149-162.
210. + oxidoreductase in the presence of sodium cholate micelles. Significance for cyclic electron transport and chlororespiration. Phytochemistry 2003, 64:1055-1060.
211. Carol P., Kuntz M. A plastid terminal oxidase comes to light: implications for carotenoids biosynthesis and respiration. Trends Plant Sci. 2001, 6:31-36.
212. Kruk J., Strzałka K. Dark reoxidation of the PQ-pool proceeds via the low-potential form of cytochrome b-559 in spinach thylakoids. Photosynth. Res. 1999, 62:273-279.
213. Millner P.A., Barber J. Plastoquinone as a mobile redox carrier in the photosynthetic membrane. FEBS Lett. 1984, 169:1-6.
214. Kruk J. Charge-transfer complexes of plastoquinone and -tocopherol quinone in vitro. Biophys. Chem. 1988, 30:143-149.
215. Kruk J. Physicochemical properties of charge-transfer complexes of plastoquinone and -tocopherol quinone, and their possible role in vivo. Biophys. Chem. 1988, 32:51-56.
216. Kruk J., Strzałka K., Leblanc R.M. Monolayer study of plastoquinones, -tocopherolquinone, their hydroquinone forms and their interaction with monogalactosyldiacylglycerol. Charge-transfer complexes in a mixed monolayer. Biochim. Biophys. Acta 1992, 1112:19-26.
217. Kruk J., Strzałka K. Charge-transfer complexes of plastoquinone and -tocopherol quinone in lecithin and octadecane. Chem. Phys. Lipids 1994, 70:199-204.
218. Skowronek M., Jemioła-Rzemińska M., Kruk J., Strzałka K. Influence of the redox state of ubiquinones and plastoquinones on the order of lipid bilayers studied by fluorescence anizotropy of diphenyl-hexatriene and trimethylammonium-diphenyl-hexatriene. Biochim. Biophys. Acta 1996, 1280:115-119.
219. Hundal T., Forsmark-Andree P., Ernster L., Andersson B. Antioxidant activity of reduced plastoquinone in chloroplast thylakoid membranes. Arch. Biochem. Biophys. 1995, 324:117-122.
220. Kruk J., Trebst A. Plastoquinol as a singlet oxygen scavenger in photosystem II. Biochim. Biophys. Acta 2008, 1777:154-162.
221. Kruk J., Jemioła-Rzemińska M., Strzałka K. Plastoquinol and α-tocopherol quinol are more active than ubiquinol and α-tocopherol in inhibition of lipid peroxidation. Chem. Phys. Lipids 1997, 87:73-80.
222. Kruk J., Strzałka K., Schmid G.H. Antioxidant properties of plastoquinol and other biological prenylquinols in liposomes and solution. Free Radic. Res. 1994, 21:409-416.
223. Kruk J., Jemioła-Rzemińska M., Burda K., Schmid G.H., Strzałka K. Scavenging of superoxide generated in photosystem I by plastoquinol and other prenyllipids in thylakoid membranes. Biochemistry 2003, 42:8501-8505.
224. Szymańska R., Kruk J. Plastoquinol is the main prenyllipid synthesized during acclimation to high light conditions in Arabidopsis and is converted to plastochromanol by tocopherol cyclase. Plant Cell Physiol. 2010, 51:537-545.
225. Pshybytko N.L., Kruk J., Kabashnikova L.F., Strzałka K. Function of plastoquinone in heat stress reactions of plants. Biochim. Biophys. Acta 2008, 1777:1393-1399.
226. Mayer M.P., Beyer P., Kleinig H. Quinone compounds are able to replace molecular oxygen as terminal electron acceptor in phytoene desaturation in chloroplasts of Narcissus pseudonarcissus L. Eur. J. Biochem. 1990, 191:359-363.
227. Norris S.R., Barrette T.R., DellaPenna D. Genetic dissection of carotenoid synthesis in Arabidopsis defines plastoquinone as an essential component of phytoene desaturation. Plant Cell 1995, 7:2139-2149.
228. Sandmann G. Evolution of carotene desaturation: the complication of a simple pathway. Arch. Biochem. Biophys. 2009, 483:169-174.
229. Allen J.F., Bennett J., Steinback K.E., Arntzen C.J. Chloroplast protein phosphorylation couples plastoquinone redox state to distribution of excitation energy between photosystems. Nature 1981, 291:25-29.
230. Pfannschmidt T., Nilsson A., Allen J.F. Photosynthetic control of chloroplast gene expression. Nature 1999, 397:625-628.
231. Chang C.C.C., Ball L., Fryer M.J., Baker N.R., Karpinski S., Mullineaux P.M. Induction of ascorbate peroxidase 2 expression in wounded Arabidopsis leaves does not involve known wound-signalling pathways but is associated with changes in photosynthesis. Plant J. 2004, 38:499-511.
232. Fryer M.J., Ball L., Oxborough K., Karpinski S., Mullineaux P.M., Baker N.R. Control of Ascorbate Peroxidase 2 expression by hydrogen peroxide and leaf water status during excess light stress reveals a functional organisation of Arabidopsis leaves. Plant J. 2003, 33:691-705.
233. Karpinski S., Escobar C., Karpinska B., Creissen G., Mullineaux P.M. Photosynthetic electron transport regulates the expression of cytosolic ascorbate peroxidase genes in Arabidopsis during excess light stress. Plant Cell 1997, 9:627-640.
234. Karpinski S., Reynolds H., Karpinska B., Wingsle G., Creissen G., Mullineaux P.M. Systemic signaling and acclimation in response to excess excitation energy in Arabidopsis. Science 1999, 284:654-657.
235. Ślesak I., Karpinska B., Surówka E., Miszalski Z., Karpinski S. Redox changes in the chloroplast and hydrogen peroxide are essential for regulation of C-3-CAM transition and photooxidative stress responses in the facultative CAM plant Mesembryanthemum crystallinum. Plant Cell Physiol. 2003, 44:573-581.
236. Steinbrenner J., Linden H. Light induction of carotenoid biosynthesis genes in the green alga Haematococcus pluvialis: regulation by photosynthetic redox control. Plant Mol. Biol. 2003, 52:343-356.
237. Piippo M., Allahverdiyeva Y., Paakkarinen V., Suoranta U.M., Battchikova N., Aro E.M. Chloroplast-mediated regulation of nuclear genes in Arabidopsis thaliana in the absence of light stress. Physiol. Genom. 2006, 25:142-152.
238. Figerio S., Campoli C., Zorzan S., Fantoni L.I., Crosatti C., Drepper F., Haehnel W., Cattivelli L., Morosinotto T., Bassi R. R, Photosynthetic antenna size in higher plants is controlled by the plastoquinone redox state at the post-transcriptional rather than transcriptional level. J. Biol. Chem. 2007, 282:29457-29469.
239. Adamiec M., Drath M., Jackowski G. Redox state of plastoquionone pool regulates expression of Arabidopsis thaliana genes in response to elevated irradiance. Acta Biochim. Pol. 2008, 55:161-173.
240. Bucke C., Leech R.M., Hallaway M., Morton R.A. The taxonomic distribution of plastoquinone and tocopherolquinone and their intracellular distribution in leaves of Vicia faba L. Biochim. Biophys. Acta 1966, 112:19-34.
241. Kruk J., Strzałka K. Occurrence and function of α-tocopherol quinone in plants. J. Plant Physiol. 1995, 145:405-409.
242. Kruk J., Szymałska R., Krupinska K. Tocopherol quinone content of green algae and higher plants revised by a new high-sensitive fluorescence detection method using HPLC-effects of high-light stress and senescence. J. Plant Physiol. 2008, 165:1238-1247.
243. Lichtenthaler H.K. Light-stimulated synthesis of plastid quinones and pigments in etiolated barley seedlings. Biochim. Biophys. Acta 1969, 184:164-172.
244. Lichtenthaler H.K. Zur Synthese der lipophilen Plastidenchinone und Sekundarcarotinoide wahrend der Chromoplastenentwicklung. Ber. Dtsch. Bot. Ges. 1969, 82:483-497.
245. Lichtenthaler H.K. Die unterschiedliche Synthese der lipophilen Plastidenchinone in Sonnen- und Schattenblattern von Fagus silvatica L. Z. Naturforsch. 1971, 26b:832-842.
246. Lin S., Bunder B.F., Hart E.R. Insect feeding stimulants from the leaf surface of Populus. J. Chem. Ecol. 1999, 24:1781-1790.
247. Hughes P.E., Tove S. Occurrence of α-tocopherolquinone and α-tocopherolquinol in microorganisms. J. Bacteriol. 1982, 151:1397-1402.
248. Hughes P.E., Tove S. Synthesis of α-tocopherolquinone by the rat and its reduction by mitochondria. J. Biol. Chem. 1980, 255:7095-7097.
249. Bieri J.G., Tolliver R.T.J. On the occurrence of α-tocopherolquinone in rat tissue. Lipids 1981, 16:777-779.
250. Hayashi T., Kanetoshi A., Nakamura M., Tamura M., Shirahama H. Reduction of α-tocopherolquinone to α-tocopherol hydroquinone in rat hepatocytes. Biochem. Pharmacol. 1992, 44:489-493.
251. Dasilva E.J., Jensen A. Content of α-tocopherol in some blue-green algae. Biochim. Biophys. Acta 1971, 239:345-347.
252. Kruk J., Schmid G.H., Strzałka K. Influence of α-tocopherol quinone, α-tocopherol and other prenyllipids on fluorescence quantum yield of photosystem II. Plant Physiol. Biochem. 2000, 38:271-277.
253. - mutant and their interactions with α-tocopherol quinone. FEBS Lett. 2003, 535:159-165.
254. Kruk J., Burda K., Radunz A., Strzałka K., Schmid G.H. Antagonistic effects of α-tocopherol and α-tocopherolquinone in the regulation of cyclic electron transport around photosystem II. Z. Naturforsch. 1997, 52c:766-774.
255. Munne-Bosch S., Shikanai T., Asada K. Enhanced ferredoxin-dependent cyclic electron flow around photosystem I and α-tocopherol quinone accumulation in water-stressed ndhB inactivated tobacco mutants. Planta 2005, 222:502-511.
256. Muller M., Hernandez I., Alegre L., Munne-Bosch S. Enhanced α-tocopherol quinone levels and xanthophyll cycle de-epoxidation in rosemary plants exposed to water deficit during a Mediterranean winter. J. Plant Physiol. 2006, 163:601-616.
257. Szymańska R., Kruk J. α-Tocopherol dominates in young leaves of runner bean (Phaseolus coccineus) under a variety of growing conditions, The possible functions of α-tocopherol. Phytochemistry 2008, 69:2142-2148.
258. Mukai K., Morimoto H., Kikuchi S., Naganka S. Kinetic study of free-radical-scavenging action of biological hydroquinones (reduced form of ubiquinone, vitamin K and tocopherol quinone) in solution. Biochim. Biophys. Acta 1993, 1157:313-317.
259. Neuzil J., Witting P.K., Stocker R. α-Tocopheryl hydroquinone is an efficient multifunctional inhibitor of radical-initiated oxidation of low density lipoprotein lipids. Proc. Natl. Acad. Sci. U. S. A. 1997, 94:7885-7890.
260. Siegel D., Bolton E.M., Burr J.A., Liebler D.C., Ross D. The reduction of α-tocopherylquinone by human NAD(P)H quinone oxidoreductase: the role of α-tocopheryl hydroquinone as a cellular antioxidant. Mol. Pharmacol. 1997, 52:300-305.
261. 1 complex. Biochem. Pharmacol. 2004, 68:373-381.
262. Hughes P.E., Tove S.B. Identification of an endogenous electron donor for biohydrogenation as α-tocopherolquinol. J. Biol. Chem. 1980, 255:4447-4452.
263. Hughes P.E., Tove S.B. Identification of deoxy-α-tocopherolquinol as another endogenous electron donor for biohydrogenation. J. Biol. Chem. 1980, 255:11802-11806.
264. Infante J.P. A function for the vitamine E metabolite α-tocopherol quinone as an essential enzyme cofactor for the mitochondrial fatty acid desaturases. FEBS Lett. 1999, 446:1-5.
265. Thornton D.E., Jones K.J., Jiang Z., Zhang H., Liu G., Cornwell D.G. Antioxidant and cytotoxic tocopheryl quinones in normal and cancer cells. Free Radic. Biol. Med. 1995, 18:963-976.
266. Stocker A., Baumann U. Supernatant protein factor in complex with RRR-a-tocopherylquinone: a link between oxidized vitamin E and cholesterol biosynthesis. J. Mol. Biol. 2003, 332:759-765.