메뉴 건너뛰기




Volumn 15, Issue 3, 2010, Pages 1531-1553

Vitamin K2 in electron transport system: Are enzymes involved in vitamin K2 biosynthesis promising drug targets?

Author keywords

Antibacterial agent; Electron transport system; Electron transport system inhibitor; MenA; Menaquinone; Menaquinone biosynthesis; Menaquinone biosynthesis inhibitor; Multidrug resistant bacteria; Vitamin K2

Indexed keywords

FARNOQUINONE;

EID: 77950354085     PISSN: None     EISSN: 14203049     Source Type: Journal    
DOI: 10.3390/molecules15031531     Document Type: Review
Times cited : (126)

References (112)
  • 1
    • 0025274835 scopus 로고
    • Vitamin K concentrations in the plasma and liver of surgical patients
    • Usui, Y.; Tanimura, H.; Nishimura, N.; Kobayashi, N. Vitamin K concentrations in the plasma and liver of surgical patients. Am. J. Clin. Nutr. 1990, 51, 846-852.
    • (1990) Am. J. Clin. Nutr. , vol.51 , pp. 846-852
    • Usui, Y.1    Tanimura, H.2    Nishimura, N.3    Kobayashi, N.4
  • 2
    • 0024598655 scopus 로고
    • Effect of various intakes of phylloquinone on signs of vitamin K deficiency and serum and liver phylloquinone concentrations in the rat
    • J. W
    • Kindberg, C. G.; Suttie, J. W. J. W. Effect of various intakes of phylloquinone on signs of vitamin K deficiency and serum and liver phylloquinone concentrations in the rat. Vitamins 1989, 175-180.
    • (1989) Vitamins , pp. 175-180
    • Kindberg, C.G.1    Suttie, J.W.2
  • 3
    • 0019490792 scopus 로고
    • Distribution of isoprenoid quinone structual types in bacterial and their taxonomic implications
    • Collins, M. D.; Jones, D. Distribution of isoprenoid quinone structual types in bacterial and their taxonomic implications. Microbiol. Rev. 1981, 45, 316-354.
    • (1981) Microbiol. Rev. , vol.45 , pp. 316-354
    • Collins, M.D.1    Jones, D.2
  • 4
    • 84947006998 scopus 로고
    • Nomenclature of quinones with isoprenoid side-chains
    • Nomenclature of quinones with isoprenoid side-chains. Pure Appl. Chem. 1974, 38, 439-447.
    • (1974) Pure Appl. Chem. , vol.38 , pp. 439-447
  • 5
    • 0027499804 scopus 로고
    • Synthesis of vitamin K dependent proteins
    • Suttie, J. W. Synthesis of vitamin K dependent proteins. FASEB 1993, 7, 445-452.
    • (1993) FASEB , vol.7 , pp. 445-452
    • Suttie, J.W.1
  • 6
    • 0030715637 scopus 로고    scopus 로고
    • Assembly of the warfarin-sensitive vitamin K 2,3-epoxide reductase
    • Cain, D.; Hutson, S. M.; Wallin, R. Assembly of the warfarin-sensitive vitamin K 2,3-epoxide reductase. J. Biol. Chem. 1997, 272, 29068-29075.
    • (1997) J. Biol. Chem. , vol.272 , pp. 29068-29075
    • Cain, D.1    Hutson, S.M.2    Wallin, R.3
  • 7
    • 34250796202 scopus 로고    scopus 로고
    • The conversion of vitamin K epoxide to vitamin K quinone and vitamin K
    • Jin, D.-Y.; Tie J.-K.; Stafford, D. W. The conversion of vitamin K epoxide to vitamin K quinone and vitamin K. Biochemistry 2007, 46, 7279-7283.
    • (2007) Biochemistry , vol.46 , pp. 7279-7283
    • Jin, D.-Y.1    Tie, J.-K.2    Stafford, D.W.3
  • 9
    • 67651171728 scopus 로고    scopus 로고
    • Warfarin: An historical perspective
    • Francis, C. W. Warfarin: An historical perspective. Hematology 2008, 251.
    • (2008) Hematology , pp. 251
    • Francis, C.W.1
  • 10
    • 33846919393 scopus 로고    scopus 로고
    • Synthesis and structure-activity relationships of novel warfarin derivatives
    • DOI 10.1016/j.bmc.2007.01.014, PII S0968089607000296
    • Gebauer, M. Synthesis and structure-activity relationships of novel warfarin derivatives. Bioorg. Med. Chem. 2007, 15, 2414-2420. (Pubitemid 46240909)
    • (2007) Bioorganic and Medicinal Chemistry , vol.15 , Issue.6 , pp. 2414-2420
    • Gebauer, M.1
  • 11
    • 38549085847 scopus 로고    scopus 로고
    • A review of warfarin dosing and monitoring
    • Kuruvilla, M.; Gurk-Turner, C. A review of warfarin dosing and monitoring. BUMC Proc. 2001, 14, 305-306.
    • (2001) BUMC Proc. , vol.14 , pp. 305-306
    • Kuruvilla, M.1    Gurk-Turner, C.2
  • 13
    • 0141638679 scopus 로고    scopus 로고
    • Comparative effects of vitamin K and vitamin D supplementation on prevention of osteopenia in calcium-deficient young rats
    • DOI 10.1016/S8756-3282(03)00249-7
    • Iwamoto, J.; Yeh, J. K.; Takeda, T.; Ichimura, S.; Sato, Y. Comparative effects of vitamin K and vitamin D supplementation on prevention of osteopenia in calcium-deficient young rats. Bone 2003, 33, 557-566. (Pubitemid 37222382)
    • (2003) Bone , vol.33 , Issue.4 , pp. 557-566
    • Iwamoto, J.1    Yeh, J.K.2    Takeda, T.3    Ichimura, S.4    Sato, Y.5
  • 14
    • 0019254237 scopus 로고
    • Some speculations on the mechanisms of the vitamins E and K starting from origin of life considerations and the antioxidant theory
    • Visser, C. M. Some speculations on the mechanisms of the vitamins E and K starting from origin of life considerations and the antioxidant theory. Bioorg. Chem. 1980, 9, 411-422.
    • (1980) Bioorg. Chem. , vol.9 , pp. 411-422
    • Visser, C.M.1
  • 15
    • 33748914544 scopus 로고    scopus 로고
    • Vitamin K deficiency reduces testosterone production in the testis through down-regulation of the Cyp11a a cholesterol side chain cleavage enzyme in rats
    • DOI 10.1016/j.bbagen.2006.05.008, PII S0304416506001590
    • Shirakawa, H.; Ohsaki, Y.; Minegishi, Y.; Takumi, N.; Ohinata, K.; Furukawa, Y.; Mizutani, T.; Komai, M. Vitamin K deficiency reduces testosterone production in the testis through downregulation of the Cyp11a a cholesterol side chain cleavage enzyme in rats. Biochim. Biophys. Acta 2006, 1760, 1482-1488. (Pubitemid 44428023)
    • (2006) Biochimica et Biophysica Acta - General Subjects , vol.1760 , Issue.10 , pp. 1482-1488
    • Shirakawa, H.1    Ohsaki, Y.2    Minegishi, Y.3    Takumi, N.4    Ohinata, K.5    Furukawa, Y.6    Mizutani, T.7    Komai, M.8
  • 16
    • 0019956605 scopus 로고
    • Prostate and menadiol sodium diphosphate. 1. Menadiol sodium diphosphate as a new substrate for measuring acid phosphatase activity and a discussion of prostatic tumor models
    • Awato, K. Prostate and menadiol sodium diphosphate. 1. Menadiol sodium diphosphate as a new substrate for measuring acid phosphatase activity and a discussion of prostatic tumor models. Nippon Hinyokika Gakkai Zasshi 1982, 73, 507-515.
    • (1982) Nippon Hinyokika Gakkai Zasshi , vol.73 , pp. 507-515
    • Awato, K.1
  • 17
    • 0034930680 scopus 로고    scopus 로고
    • Increased warfarin sensitivity as an early manifestation of occult prostate cancer with chronic disseminated intravascular coagulation
    • DOI 10.1159/000046542
    • Munter, G.; Hershko, C. Increased warfarin sensitivity as an early manifestation of occult prostate cancer with chronic disseminated intravascular coagulation. Act. Haematol. 2001, 105, 97-99. (Pubitemid 32620109)
    • (2001) Acta Haematologica , vol.105 , Issue.2 , pp. 97-99
    • Munter, G.1    Hershko, C.2
  • 19
    • 0030029030 scopus 로고    scopus 로고
    • Vitamin K status in human tissues: Tissue-specific accumulation of phylloquinone and menaquinone-4
    • Thijssen, H. H. W.; Drittij-Reijnders, M. J. Vitamin K status in human tissues: tissue-specific accumulation of phylloquinone and menaquinone-4. British J. Nutr. 1996, 75, 121-127.
    • (1996) British J. Nutr. , vol.75 , pp. 121-127
    • Thijssen, H.H.W.1    Drittij-Reijnders, M.J.2
  • 20
    • 48049112025 scopus 로고    scopus 로고
    • Synthesis and development of biologically active fluorescent-labeled vitamin K analogues and monitoring of their subcellular distribution
    • Yoshitomo, S.; Shinya, A.; Aya, M.; Yuka, S.; Kimie, N.; Maya, K.; Naoko, T.; Toshio, O. Synthesis and development of biologically active fluorescent-labeled vitamin K analogues and monitoring of their subcellular distribution. Tetrahedron 2008, 64, 8789-8796.
    • (2008) Tetrahedron. , vol.64 , pp. 8789-8796
    • Yoshitomo, S.1    Shinya, A.2    Aya, M.3    Yuka, S.4    Kimie, N.5    Maya, K.6    Naoko, T.7    Toshio, O.8
  • 23
    • 36949083936 scopus 로고
    • Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism
    • Mitchell, P. Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism. Nature 1961, 191, 144-148.
    • (1961) Nature , vol.191 , pp. 144-148
    • Mitchell, P.1
  • 24
    • 0013942130 scopus 로고
    • Chemiosmotic coupling in oxidative and photosynthetic phosphorylation
    • Mitchell, P. Chemiosmotic coupling in oxidative and photosynthetic phosphorylation. Biol Rev. Cambridge Phil Soc. 1966, 41, 445-502.
    • (1966) Biol. Rev. Cambridge Phil Soc. , vol.41 , pp. 445-502
    • Mitchell, P.1
  • 25
    • 0015480455 scopus 로고
    • Chemiosmotic coupling in energy transduction: A logical development of biochemical knowledge
    • Mitchell, P. Chemiosmotic coupling in energy transduction: A logical development of biochemical knowledge. Bioenergetics 1972, 3, 5-24.
    • (1972) Bioenergetics , vol.3 , pp. 5-24
    • Mitchell, P.1
  • 26
    • 0014011370 scopus 로고
    • The inhibition of mitochondrial peroxidation by ubiquinone and ubiquinol
    • Mellors A.; Tappel, A. L. The inhibition of mitochondrial peroxidation by ubiquinone and ubiquinol. J. Biol. Chem. 1966, 241, 4353-4356.
    • (1966) J. Biol. Chem. , vol.241 , pp. 4353-4356
    • Mellors, A.1    Tappel, A.L.2
  • 28
    • 0024245469 scopus 로고
    • Free radicals in aging
    • Harman, D. Free radicals in aging. Mol. Cell. Biochem. 1988, 84, 55-61.
    • (1988) Mol. Cell. Biochem. , vol.84 , pp. 55-61
    • Harman, D.1
  • 29
    • 0029042393 scopus 로고
    • Biochemical, physiological and medical aspects of ubiquinone function
    • Emster, L.; Dallner, G. Biochemical, physiological and medical aspects of ubiquinone function. Biochim. Biophys. Acta 1995, 1271, 195-204.
    • (1995) Biochim. Biophys. Acta , vol.1271 , pp. 195-204
    • Emster, L.1    Dallner, G.2
  • 31
    • 0034571905 scopus 로고    scopus 로고
    • Ubiquinone. Biosynthesis of quinone ring and its isoprenoid side chain. Intracellular localization
    • Szkopishka, A. Ubiquinone. Biosynthesis of quinone ring and its isoprenoid side chain. Intracellular localization. Acta Biochim. Pol. 2000, 47, 469-480.
    • (2000) Acta Biochim. Pol. , vol.47 , pp. 469-480
    • Szkopishka, A.1
  • 33
    • 0023887173 scopus 로고
    • Bacterial electron transport chains
    • Yasuhiro, A. Bacterial electron transport chains. Ann. Rev. Biochem. 1988, 57, 101-312.
    • (1988) Ann. Rev. Biochem. , vol.57 , pp. 101-312
    • Yasuhiro, A.1
  • 34
    • 0031596770 scopus 로고    scopus 로고
    • 2) biosynthesis: Localization and characterization of the menA gene from Escherichia coli
    • Suvana, K. D.; Stevenson, R.; Meganathan, R.; Hudspeth, M. E. S.; Menaquinone (vitamin K2) biosynthesis: localization and characterization of the menA gene from Escherichia coli. J. Bacteriol. 1998, 180, 2782-2787. (Pubitemid 28213284)
    • (1998) Journal of Bacteriology , vol.180 , Issue.10 , pp. 2782-2787
    • Suvarna, K.1    Stevenson, D.2    Meganathan, R.3    Hudspeth, M.E.S.4
  • 36
    • 0009014415 scopus 로고
    • Ubiquinone and vitamin K in bacteria
    • Bishop, D. H. L.; Pandya, K. P.; King, H. K. Ubiquinone and vitamin K in bacteria. Biochem. J. 1962, 83, 606-614.
    • (1962) Biochem. J. , vol.83 , pp. 606-614
    • Bishop, D.H.L.1    Pandya, K.P.2    King, H.K.3
  • 37
    • 0024441894 scopus 로고
    • Structure and function of a menaquinone involved in electron transport in membranes of Clostridium thermoautotrophicum and Clostridium thermoaceticum
    • Das, A.; Hugenholtz, J.; van Halbeek, H.; Ljungdal, L. G. Structure and function of a menaquinone involved in electron transport in membranes of Clostridium thermoautotrophicum and Clostridium thermoaceticum. J. Bacteriol. 1989, 171, 5823-5829.
    • (1989) J. Bacteriol. , vol.171 , pp. 5823-5829
    • Das, A.1    Hugenholtz, J.2    Van Halbeek, H.3    Ljungdal, L.G.4
  • 38
    • 0036917889 scopus 로고    scopus 로고
    • F. SAM (dependent) I AM: The S-adenosylmethionine-dependent methyltransferase fold
    • Martin, J. L.; M. McMillan, F. SAM (dependent) I AM: the S-adenosylmethionine-dependent methyltransferase fold. Curr. Opin. Struct. Biol. 2002, 12, 783-793.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 783-793
    • Martin, J.L.1    McMillan, M.2
  • 39
    • 0020413535 scopus 로고
    • Biosynthesis of vitamin K (menaquinone) in bacteria
    • Bentley, R.; Meganathan, R. Biosynthesis of vitamin K (menaquinone) in bacteria. Microbiol. Rev. 1982, 46, 241-280.
    • (1982) Microbiol. Rev. , vol.46 , pp. 241-280
    • Bentley, R.1    Meganathan, R.2
  • 40
    • 15444345457 scopus 로고
    • Biosynthesis of vitamin K and other natural naphthoquinones
    • Bentley, R. Biosynthesis of vitamin K and other natural naphthoquinones. Pure Appl. Chem. 1975, 41, 47-68.
    • (1975) Pure Appl. Chem. , vol.41 , pp. 47-68
    • Bentley, R.1
  • 41
    • 0017177848 scopus 로고
    • Biosynthesis of bacterial menaquinones: The membrane-associated 1,4-dihydroxy-2-naphthoate octaprenyltransferase of Escherichia coli
    • Shineberg, B.; Young, I. G. Biosynthesis of bacterial menaquinones: the membrane-associated 1,4-dihydroxy-2-naphthoate octaprenyltransferase of Escherichia coli. Biochemistry 1976, 15, 2754-2758.
    • (1976) Biochemistry , vol.15 , pp. 2754-2758
    • Shineberg, B.1    Young, I.G.2
  • 42
    • 0019840644 scopus 로고
    • Biosynthesis of o-succinylbenzoic acid in a men-Escherichia coli mutant requires decarboxylation of L-glutamate at the C-1 position
    • Meganathan, R.; Bentley, R. Biosynthesis of o-succinylbenzoic acid in a men-Escherichia coli mutant requires decarboxylation of L-glutamate at the C-1 position. Biochemistry 1981, 20, 5336-5340.
    • (1981) Biochemistry , vol.20 , pp. 5336-5340
    • Meganathan, R.1    Bentley, R.2
  • 45
  • 46
    • 0021103983 scopus 로고
    • Homology between CAP and Fnr, a regulator of anaerobic respiration in Escherichia coli
    • Shaw, D. J.; Rice, D. W.; Guest, J. R. Homology between CAP and Fnr, a regulator of anaerobic respiration in Escherichia coli. J. Mol. Biol. 1983, 166, 241-247.
    • (1983) J. Mol. Biol. , vol.166 , pp. 241-247
    • Shaw, D.J.1    Rice, D.W.2    Guest, J.R.3
  • 47
    • 0024231821 scopus 로고
    • Differential roles for menaquinone and demethylmenaquinone in anaerobic electron transport of E. coli and their fnr-independent expression
    • Unden G. Differential roles for menaquinone and demethylmenaquinone in anaerobic electron transport of E. coli and their fnr-independent expression. Arch. Microbiol. 1988, 150, 499-503.
    • (1988) Arch. Microbiol. , vol.150 , pp. 499-503
    • Unden, G.1
  • 48
    • 0030899580 scopus 로고    scopus 로고
    • Overlapping promoters modulate Fnr-and ArcA-dependent anaerobic transcriptional activation of the focApfl operon in Escherichia coli
    • Kaiser, M.; Sawers, G. Overlapping promoters modulate Fnr-and ArcA-dependent anaerobic transcriptional activation of the focApfl operon in Escherichia coli. Microbiology 1997, 143, 775-783.
    • (1997) Microbiology , vol.143 , pp. 775-783
    • Kaiser, M.1    Sawers, G.2
  • 49
    • 34147168030 scopus 로고    scopus 로고
    • The redox regulator Fnr is required for fermentative growth and enterotoxin synthesis in bacillus cereus F4430/73
    • and references therein
    • Zigha, A.; Rosenfeld, E.; Schmitt, P.; Duport, C. The redox regulator Fnr is required for fermentative growth and enterotoxin synthesis in bacillus cereus F4430/73. J. Bacteriol. 2007, 189, 2813-2824 and references therein.
    • (2007) J. Bacteriol. , vol.189 , pp. 2813-2824
    • Zigha, A.1    Rosenfeld, E.2    Schmitt, P.3    Duport, C.4
  • 50
    • 0019809335 scopus 로고
    • The dependence on quinone specificity of terminal electron transport of bacteria
    • Hollfinder, R. The dependence on quinone specificity of terminal electron transport of bacteria. Curr. Microbiol. 1981, 6, 155-159.
    • (1981) Curr. Microbiol. , vol.6 , pp. 155-159
    • Hollfinder, R.1
  • 52
    • 0013593621 scopus 로고
    • The function of menaquinone in bacterial electron transport
    • Lenz, G., Ed.; John Wiley & Sons: New York, NY, USA
    • Kröger, A.; Unden, G. The function of menaquinone in bacterial electron transport. In Coenzyme Q; Lenz, G., Ed.; John Wiley & Sons: New York, NY, USA, 1985; pp. 285-300.
    • (1985) Coenzyme Q , pp. 285-300
    • Kröger, A.1    Unden, G.2
  • 53
    • 37549014901 scopus 로고    scopus 로고
    • The validity of mitochondrial dehydrogenases as antimalarial drug targets
    • Vaidya, A. B.; Paintera, H. J.; Morriseya, J. M.; Mathera, M. W. The validity of mitochondrial dehydrogenases as antimalarial drug targets. Trends Parasitol. 2007, 24, 8-9.
    • (2007) Trends Parasitol. , vol.24 , pp. 8-9
    • Vaidya, A.B.1    Paintera, H.J.2    Morriseya, J.M.3    Mathera, M.W.4
  • 54
    • 33847398001 scopus 로고    scopus 로고
    • Specific role of mitochondrial electron transport in blood-stage Plasmodium falciparum
    • Painter, H. J.; Morrisey, J. M.; Mather, M. W.; Vaidya, A. B. Specific role of mitochondrial electron transport in blood-stage Plasmodium falciparum. Nature 2007, 446, 88-91.
    • (2007) Nature , vol.446 , pp. 88-91
    • Painter, H.J.1    Morrisey, J.M.2    Mather, M.W.3    Vaidya, A.B.4
  • 58
    • 27344432975 scopus 로고    scopus 로고
    • Changes in energy metabolism of Mycobacterium tuberculosis in mouse lung and under in vitro conditions affecting aerobic respiration
    • Shi, L.; Sohaskey, C. D.; Kana, B. D.; Dawes, S.; North, R. J.; Mizrahi, V.; Gennaro, M. L. Changes in energy metabolism of Mycobacterium tuberculosis in mouse lung and under in vitro conditions affecting aerobic respiration. Proc. Natl. Acad. Sci. USA 2005, 102, 15629-15634.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 15629-15634
    • Shi, L.1    Sohaskey, C.D.2    Kana, B.D.3    Dawes, S.4    North, R.J.5    Mizrahi, V.6    Gennaro, M.L.7
  • 59
    • 33744957049 scopus 로고    scopus 로고
    • Steady-state kinetics and inhibitory action of antitubercular phenothiazines on Mycobacterium tuberculosis Type-II NADH-menaquinone oxidoreductase (NDH-2)
    • Yano, T.; Li, L. S.; Weinstein, E.; Teh, J. S.; Rubin, H. Steady-state kinetics and inhibitory action of antitubercular phenothiazines on Mycobacterium tuberculosis Type-II NADH-menaquinone oxidoreductase (NDH-2). J. Biol. Chem. 2006, 281, 11456-11463.
    • (2006) J. Biol. Chem. , vol.281 , pp. 11456-11463
    • Yano, T.1    Li, L.S.2    Weinstein, E.3    Teh, J.S.4    Rubin, H.5
  • 60
    • 12244311915 scopus 로고    scopus 로고
    • Acaricide mode of action
    • Dekeyser, M. Acaricide mode of action. Pest Manag. Sci. 2005, 61, 103-110.
    • (2005) Pest Manag. Sci. , vol.61 , pp. 103-110
    • Dekeyser, M.1
  • 61
    • 0033839954 scopus 로고    scopus 로고
    • Mitochondrial complex I: New insights from inhibitor assays
    • Estornell, E. Mitochondrial complex I: new insights from inhibitor assays. Plotoplasma 2000, 213, 11-17.
    • (2000) Plotoplasma , vol.213 , pp. 11-17
    • Estornell, E.1
  • 62
    • 16644398959 scopus 로고    scopus 로고
    • Rotenone-insensitive NADH oxidation in mitochondrial suspension is performed by NADH dehydrogenase of respiratory chain fragments
    • Sharova, I. V.; Vekshin, N. L. Rotenone-insensitive NADH oxidation in mitochondrial suspension is performed by NADH dehydrogenase of respiratory chain fragments. Biofizika 2004, 49, 814-821.
    • (2004) Biofizika , vol.49 , pp. 814-821
    • Sharova, I.V.1    Vekshin, N.L.2
  • 63
    • 77950359542 scopus 로고    scopus 로고
    • Acaricides with different modes of action
    • Bai, Y. L. Acaricides with different modes of action. Xiandai Nongyao 2005, 4, 27-30.
    • (2005) Xiandai Nongyao , vol.4 , pp. 27-30
    • Bai, Y.L.1
  • 64
    • 0030087556 scopus 로고    scopus 로고
    • Fenazaquin acaricide specific binding sites in NADH:ubiquinone oxidoreductase and apparently the ATP synthase stalk
    • Wood, E.; Latli, B.; Casida, J. E. Fenazaquin acaricide specific binding sites in NADH:ubiquinone oxidoreductase and apparently the ATP synthase stalk. Pestic. Biochem. Physiol. 1996, 54, 135-145.
    • (1996) Pestic. Biochem. Physiol. , vol.54 , pp. 135-145
    • Wood, E.1    Latli, B.2    Casida, J.E.3
  • 65
    • 77950355843 scopus 로고
    • Electron transport in Paracoccus halodenitrificans and the role of ubiquinone
    • Hochstein, L. I.; Cronin, S. E. Electron transport in Paracoccus halodenitrificans and the role of ubiquinone. NASA Tech. Memo. 1983, 23, 572-577.
    • (1983) NASA Tech. Memo , vol.23 , pp. 572-577
    • Hochstein, L.I.1    Cronin, S.E.2
  • 66
    • 0346729856 scopus 로고    scopus 로고
    • The design and synthesis of novel inhibitors of NADH:ubiquinone oxidoreductase
    • Lindell, S. D.; Ort, O.; Lümmen, P.; Klein, R. The design and synthesis of novel inhibitors of NADH:ubiquinone oxidoreductase. Bioorg. Med. Chem. Lett. 2004, 14, 511-514.
    • (2004) Bioorg. Med. Chem. Lett. , vol.14 , pp. 511-514
    • Lindell, S.D.1    Ort, O.2    Lümmen, P.3    Klein, R.4
  • 67
    • 84987156662 scopus 로고
    • Fungicidal betamethoxyacrylates: From natural products to novel synthetic agricultural fungicides
    • Beautement, K.; Clough, J. M.; de Fraine, P. J.; Godfrey, C. R. A. Fungicidal betamethoxyacrylates: from natural products to novel synthetic agricultural fungicides. Pestic Sci. 1991, 31, 499-519.
    • (1991) Pestic Sci. , vol.31 , pp. 499-519
    • Beautement, K.1    Clough, J.M.2    De Fraine, P.J.3    Godfrey, C.R.A.4
  • 69
    • 0142218976 scopus 로고    scopus 로고
    • Two new epimeric pairs of acetogenins bearing a carbonyl group from Annona cherimolia seeds
    • Son, J. K.; Kim, D. H.; Woo, M. H. Two new epimeric pairs of acetogenins bearing a carbonyl group from Annona cherimolia seeds. J. Nat. Prod. 2003, 66, 1369-1372.
    • (2003) J. Nat. Prod. , vol.66 , pp. 1369-1372
    • Son, J.K.1    Kim, D.H.2    Woo, M.H.3
  • 70
    • 1942447877 scopus 로고    scopus 로고
    • 1 complex: Function in the context of structure
    • 1 complex: Function in the context of structure. Annu. Rev. Physiol. 2004, 66, 689-733.
    • (2004) Annu. Rev. Physiol. , vol.66 , pp. 689-733
    • Crofts, A.R.1
  • 72
    • 4143054902 scopus 로고    scopus 로고
    • Cytochrome bc complexes: A common core of structure and function surrounded by diversity in the outlying provinces
    • Smith, J. L.; Zhang, H.; Yan, J.; Kurisu, G.; Cramer, W. A. Cytochrome bc complexes: a common core of structure and function surrounded by diversity in the outlying provinces. Curr. Opini. Struct. Biol. 2004, 14, 432-439.
    • (2004) Curr. Opini. Struct. Biol. , vol.14 , pp. 432-439
    • Smith, J.L.1    Zhang, H.2    Yan, J.3    Kurisu, G.4    Cramer, W.A.5
  • 74
  • 76
    • 0037022594 scopus 로고    scopus 로고
    • 1 complex with its bound substrate cytochrome c
    • 1 complex with its bound substrate cytochrome c. Proc. Natl. Acad. Sci. USA 2002, 99, 2800-2805.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 2800-2805
    • Lange, C.1    Hunte, C.2
  • 78
    • 0344296085 scopus 로고
    • Inhibition of electron transport by antimycin A, alkyl hydroxy naphthoquinones and metal coordination compounds
    • Tappel, A. L. Inhibition of electron transport by antimycin A, alkyl hydroxy naphthoquinones and metal coordination compounds. Biochem. Pharmacol. 1960, 3, 289-296.
    • (1960) Biochem. Pharmacol. , vol.3 , pp. 289-296
    • Tappel, A.L.1
  • 79
    • 22544467474 scopus 로고    scopus 로고
    • 1 complex: A new crystal structure reveals an altered intramolecular hydrogen-bonding pattern
    • 1 complex: A new crystal structure reveals an altered intramolecular hydrogen-bonding pattern. J. Mol. Biol. 2005, 351, 573-597.
    • (2005) J. Mol. Biol. , vol.351 , pp. 573-597
    • Huang, L.S.1    Cobessi, D.2    Tung, E.Y.3    Berry, E.A.4
  • 80
    • 77950361070 scopus 로고
    • Effect of myxothiazol on the electrogenic redox chain of purple photosynthetic bacteria
    • Kotova, E. A.; Oleskin, A. V.; Samuilov, V. D. Effect of myxothiazol on the electrogenic redox chain of purple photosynthetic bacteria. Photobiochem. Photobiophys. 1983, 6, 211-221.
    • (1983) Photobiochem. Photobiophys , vol.6 , pp. 211-221
    • Kotova, E.A.1    Oleskin, A.V.2    Samuilov, V.D.3
  • 83
    • 64849092441 scopus 로고    scopus 로고
    • Mutations in the mitochondrial cytochrome b of Tetranychus urticae Koch (Acari: Tetranychidae) confer crossresistance between bifenazate and acequinocyl
    • van Nieuwenhuyse, P.; van Leeuwen, T.; Khajehali, J.; Vanholme, B.; Tirry, L. Mutations in the mitochondrial cytochrome b of Tetranychus urticae Koch (Acari: Tetranychidae) confer crossresistance between bifenazate and acequinocyl. Pest. Manag. Sci. 2009, 65, 404-412.
    • (2009) Pest. Manag. Sci. , vol.65 , pp. 404-412
    • Van Nieuwenhuyse, P.1    Van Leeuwen, T.2    Khajehali, J.3    Vanholme, B.4    Tirry, L.5
  • 85
    • 7244255793 scopus 로고    scopus 로고
    • Determination of acequinocyl and hydroxyacequinocyl on fruits and vegetables by HPLC-DAD
    • Caboni, P.; Sarais, G.; Melis, M.; Cabras, M.; Cabras, P. Determination of acequinocyl and hydroxyacequinocyl on fruits and vegetables by HPLC-DAD. J. Agric. Food Chem. 2004, 52, 6700-6702.
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 6700-6702
    • Caboni, P.1    Sarais, G.2    Melis, M.3    Cabras, M.4    Cabras, P.5
  • 86
    • 0014527592 scopus 로고
    • Antiviral and antitumor antibiotics. XIV. Effects of ascochlorin and other respiration inhibitors on multiplication of Newcastle disease virus in cultured cells
    • Takatsuki, A; Tamura, G; Arima, K. Antiviral and antitumor antibiotics. XIV. Effects of ascochlorin and other respiration inhibitors on multiplication of Newcastle disease virus in cultured cells. Appl. Microbiol. 1969, 17, 825-829.
    • (1969) Appl. Microbiol. , vol.17 , pp. 825-829
    • Takatsuki, A.1    Tamura, G.2    Arima, K.3
  • 88
    • 63749090999 scopus 로고    scopus 로고
    • Mitochondrial impacts of insecticidal formate esters in insecticideresistant and insecticide-susceptible Drosophila melanogaster
    • Song, C.; Scharf, M. E. Mitochondrial impacts of insecticidal formate esters in insecticideresistant and insecticide-susceptible Drosophila melanogaster. Pest. Manag. Sci. 2009, 65, 697-703.
    • (2009) Pest. Manag. Sci. , vol.65 , pp. 697-703
    • Song, C.1    Scharf, M.E.2
  • 89
    • 21644444034 scopus 로고    scopus 로고
    • Ascochlorin inhibits matrix metalloproteinase-9 expression by suppressing activator protein-1-mediated gene expression through the ERK1/2 signaling pathway
    • Hong, S.; Park, K. K.; Magae, J.; Ando, K.; Lee, T. S.; Kwon, T. K.; Kwak, J. Y. Kim, C. H.; Chang, Y. C. Ascochlorin inhibits matrix metalloproteinase-9 expression by suppressing activator protein-1-mediated gene expression through the ERK1/2 signaling pathway. J. Bio. Chem. 2005, 280, 25202-25209.
    • (2005) J. Bio. Chem. , vol.280 , pp. 25202-25209
    • Hong, S.1    Park, K.K.2    Magae, J.3    Ando, K.4    Lee, T.S.5    Kwon, T.K.6    Kwak, J.Y.7    Kim, C.H.8    Chang, Y.C.9
  • 90
    • 34548538972 scopus 로고    scopus 로고
    • Development of tyrocidine A analogues with improved antibacterial activity
    • Marques, M. A.; Citronb, D. M.; Wang, C. C. Development of tyrocidine A analogues with improved antibacterial activity. Bioorg. Med. Chem. 2007, 15, 6667-6677.
    • (2007) Bioorg. Med. Chem. , vol.15 , pp. 6667-6677
    • Marques, M.A.1    Citronb, D.M.2    Wang, C.C.3
  • 91
    • 0029768884 scopus 로고    scopus 로고
    • The effects of decyl aurachins C and D on the respiratory electron flow of facultative phototrophic bacteria
    • Romagnoli, S.; Oettmeier, W.; Zannoni, D. The effects of decyl aurachins C and D on the respiratory electron flow of facultative phototrophic bacteria. Biochem. Mol. Biol. Int. 1996, 39, 671-678.
    • (1996) Biochem. Mol. Biol. Int. , vol.39 , pp. 671-678
    • Romagnoli, S.1    Oettmeier, W.2    Zannoni, D.3
  • 92
    • 58849094502 scopus 로고    scopus 로고
    • A quinolin antibiotic from Phodococcus erthropolis JCM 6824
    • Kitagawa, W.; Tamura, T. A quinolin antibiotic from Phodococcus erthropolis JCM 6824. J. Antibiot. 2008, 61, 680-682.
    • (2008) J. Antibiot. , vol.61 , pp. 680-682
    • Kitagawa, W.1    Tamura, T.2
  • 93
    • 58849106145 scopus 로고    scopus 로고
    • Three types of antibiotics produced from Phodococcus erthropolis strains
    • Kitagawa, W.; Tamura, T. Three types of antibiotics produced from Phodococcus erthropolis strains. Microbes Environ. 2008, 23, 167-171.
    • (2008) Microbes Environ. , vol.23 , pp. 167-171
    • Kitagawa, W.1    Tamura, T.2
  • 95
    • 0029858218 scopus 로고    scopus 로고
    • Polyalthidin: New prenylated benzopyran inhibitor of the mammalian mitochondrial respiratory chain
    • DOI 10.1021/np960492m
    • Zafra-Polo, M. C.; González, M. C.; Tormo, J. R.; Estornell, E.; Cortes, D. Polyalthidin: New prenylated benzopyran inhibitor of the mammalian mitochondrial respiratory chain. J. Nat. Prod. Chem. 1996, 59, 913-916. (Pubitemid 26365480)
    • (1996) Journal of Natural Products , vol.59 , Issue.10 , pp. 913-916
    • Zafra-Polo, M.C.1    Gonzalez, M.C.2    Tormo, J.R.3    Estornell, E.4    Cortes, D.5
  • 96
    • 68049108475 scopus 로고    scopus 로고
    • Terretonins E and F, inhibitors of the mitochondrial respiratory chain from the marine-derived fungus Aspergillus insuetus
    • López-Gresa, M. P.; Cabedo, N.; González-Mas, M. C.; Ciavatta, M. L.; Avila, C.; Primo, J. Terretonins E and F, inhibitors of the mitochondrial respiratory chain from the marine-derived fungus Aspergillus insuetus. J. Nat. Prod. 2009, 72, 1348-1351.
    • (2009) J. Nat. Prod. , vol.72 , pp. 1348-1351
    • López-Gresa, M.P.1    Cabedo, N.2    González-Mas, M.C.3    Ciavatta, M.L.4    Avila, C.5    Primo, J.6
  • 97
    • 34548118698 scopus 로고    scopus 로고
    • Discovery of 1,4-didydroxy-2-naphthoate prenyltransferase inhibitors: New drug leads for multidrug-resistant gram-positive pathogens
    • DOI 10.1021/jm070638m
    • Kurosu, M.; Narayanasamy, P.; Biswas, K.; Dhiman, R.; Crick, D. C. Discovery of 1,4-dihydroxy-2-naphthoate prenyltransferase inhibitors: New drug leads for multidrug-resistant Gram-positive pathogens. J. Med. Chem. 2007, 50, 3973-3975. (Pubitemid 47301729)
    • (2007) Journal of Medicinal Chemistry , vol.50 , Issue.17 , pp. 3973-3975
    • Kurosu, M.1    Narayanasamy, P.2    Biswas, K.3    Dhiman, R.4    Crick, D.C.5
  • 98
    • 0029976980 scopus 로고    scopus 로고
    • An in vitro model for sequential study of shiftdown of Mycobacterium tuberculosis through two stages of nonreplicating persistence
    • Wayne, L. G.; Hayes, L. G. An in vitro model for sequential study of shiftdown of Mycobacterium tuberculosis through two stages of nonreplicating persistence. Infect. Immun. 1996, 64, 2062-2069.
    • (1996) Infect. Immun. , vol.64 , pp. 2062-2069
    • Wayne, L.G.1    Hayes, L.G.2
  • 99
    • 0018757805 scopus 로고
    • Antigenic differences between extracts of actively replicating and synchronized resting cells of Mycobacterium tuberculosis
    • Wayne, L. G.; Sramek, H. A. Antigenic differences between extracts of actively replicating and synchronized resting cells of Mycobacterium tuberculosis. Infect. Immun. 1979, 24, 363-370.
    • (1979) Infect. Immun. , vol.24 , pp. 363-370
    • Wayne, L.G.1    Sramek, H.A.2
  • 100
    • 0028603583 scopus 로고
    • Metronidazole is bactericidal to dormant cells of Mycobacterium tuberculosis
    • Wayne, L. G.; Sramek, H. A. Metronidazole is bactericidal to dormant cells of Mycobacterium tuberculosis. Antimicrob. Agents Chemother. 1994, 13, 908-912.
    • (1994) Antimicrob. Agents Chemother. , vol.13 , pp. 908-912
    • Wayne, L.G.1    Sramek, H.A.2
  • 101
    • 65349189521 scopus 로고    scopus 로고
    • MenA is a promising drug target for developing novel lead molecules to combat Mycobacterium tuberculosis
    • Kurosu, M.; Crick, D. C. MenA is a promising drug target for developing novel lead molecules to combat Mycobacterium tuberculosis. Med. Chem. 2009, 5, 197-207.
    • (2009) Med. Chem. , vol.5 , pp. 197-207
    • Kurosu, M.1    Crick, D.C.2
  • 103
    • 55249100482 scopus 로고    scopus 로고
    • Mechanism-based inhibitors of MenE, an acyl-CoA synthetase involved in bacterial menaquinone biosynthesis
    • Lu, X.; Zhang, H.; Tonge, P. J.; Tan, D. S. Mechanism-based inhibitors of MenE, an acyl-CoA synthetase involved in bacterial menaquinone biosynthesis. Bioorg. Med. Chem. Lett. 2008, 18, 5963-5966.
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , pp. 5963-5966
    • Lu, X.1    Zhang, H.2    Tonge, P.J.3    Tan, D.S.4
  • 104
    • 77950365062 scopus 로고    scopus 로고
    • Enzymatic activity in the crotonase superfamily: The mechanism of the reactions catalyzed by 1,4-dihydroxynaphthoyl-CoA synthase (MenB) and 2-ketocyclohexanecarboxyl-CoA hydrolase (BadI)
    • Boston, MA, USA, 19-23 August
    • Zhang, H.; Tonge, P. J. Enzymatic activity in the crotonase superfamily: The mechanism of the reactions catalyzed by 1,4-dihydroxynaphthoyl-CoA synthase (MenB) and 2-ketocyclohexanecarboxyl-CoA hydrolase (BadI). In 234th ACS National Meeting, Boston, MA, USA, 19-23 August 2007.
    • (2007) In 234th ACS National Meeting
    • Zhang, H.1    Tonge, P.J.2
  • 105
    • 77950351720 scopus 로고    scopus 로고
    • Inhibition of 1,4-dihydroxynaphthoyl-CoA synthase (MenB), an enzyme drug target bacterial menaquinone biosynthesis pathway
    • Philadelphia, PA, USA, 17-21 August
    • Li, X.; Zhang, H.; Tonge, P. J. Inhibition of 1,4-dihydroxynaphthoyl-CoA synthase (MenB), an enzyme drug target bacterial menaquinone biosynthesis pathway. In 236th ACS National Meeting, Philadelphia, PA, USA, 17-21 August 2008.
    • (2008) In 236th ACS National Meeting
    • Li, X.1    Zhang, H.2    Tonge, P.J.3
  • 106
    • 77950360402 scopus 로고    scopus 로고
    • Mechanistic studies of MenD, 2-succinyl-5-enoylpyruvyl-6-hydroxy-3- cyclohexene-1-carboxylic acid synthase from Staphylococcus aureus
    • Salt Lake City, UT, USA, 22-26 March
    • Xu, H.; Graham, M.; Karelis, J.; Walker, S. G.; Peter J. Tonge, P. J. Mechanistic studies of MenD, 2-succinyl-5-enoylpyruvyl-6-hydroxy-3-cyclohexene- 1-carboxylic acid synthase from Staphylococcus aureus. In 237th ACS National Meeting, Salt Lake City, UT, USA, 22-26 March 2009.
    • (2009) In 237th ACS National Meeting
    • Xu, H.1    Graham, M.2    Karelis, J.3    Walker, S.G.4    Peter, J.5    Tonge, P.J.6
  • 107
    • 0017811949 scopus 로고
    • Stereobiochemical aspects of warfarin isomers for inhibition of enzymatic alkylation of menaquinone-0 to menaquinone-4 in chick liver
    • Hossein, D. G. Stereobiochemical aspects of warfarin isomers for inhibition of enzymatic alkylation of menaquinone-0 to menaquinone-4 in chick liver. Int. J. Vitam. Nutr. Res. 1978, 48, 131-135.
    • (1978) Int. J. Vitam. Nutr. Res. , vol.48 , pp. 131-135
    • Hossein, D.G.1
  • 109
    • 13744260022 scopus 로고    scopus 로고
    • TB-a new target, a new drug
    • Cole, S. T.; Alzari, P. M. TB-a new target, a new drug. Science 2005, 307, 214-215.
    • (2005) Science , vol.307 , pp. 214-215
    • Cole, S.T.1    Alzari, P.M.2
  • 110
    • 67651202584 scopus 로고    scopus 로고
    • Unique roles of DosT and DosS in DosR regulon induction and Mycobacterium tuberculosis dormancy
    • Honaker, R. W.; Leistikow, R. L.; Bartek, I. L.; Voskuil, M. I. Unique roles of DosT and DosS in DosR regulon induction and Mycobacterium tuberculosis dormancy. Infect. Immun. 2009, 77, 3258-3263.
    • (2009) Infect. Immun. , vol.77 , pp. 3258-3263
    • Honaker, R.W.1    Leistikow, R.L.2    Bartek, I.L.3    Voskuil, M.I.4
  • 111
    • 0015798511 scopus 로고
    • Physiological effects of menaquinone deficiency in Bacillus subtilis
    • Farrand, S. K.; Taber, H. W. Physiological effects of menaquinone deficiency in Bacillus subtilis. J. Bacteriol. 1973, 115, 1035-1044.
    • (1973) J. Bacteriol. , vol.115 , pp. 1035-1044
    • Farrand, S.K.1    Taber, H.W.2
  • 112
    • 0025647235 scopus 로고
    • Menaquinone is an obligatory component of the chain catalyzing succinate respiration in Bacillus subtilis
    • Lemma, E.; Unden, G.; Kröger, A. Menaquinone is an obligatory component of the chain catalyzing succinate respiration in Bacillus subtilis. Arch. Microbiol. 1990, 155, 62-67.
    • (1990) Arch. Microbiol. , vol.155 , pp. 62-67
    • Lemma, E.1    Unden, G.2    Kröger, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.