메뉴 건너뛰기




Volumn 171, Issue 8, 2014, Pages 2099-2122

Regulation of mitochondrial bioenergetic function by hydrogen sulfide. Part I. Biochemical and physiological mechanisms

Author keywords

3 mercaptopyruvate sulfurtransferase; bioenergetics; blood vessels; cysteine; cytochrome c oxidase; free radicals; gasotransmitters; mitochondrial electron transport; nitric oxide; superoxide

Indexed keywords

3 MERCAPTOPYRUVATE SULFURTRANSFERASE; 5,10 METHYLENETETRAHYDROFOLATE REDUCTASE (FADH2); ADENOSINE TRIPHOSPHATE; CYSTATHIONINE BETA SYNTHASE; CYSTATHIONINE GAMMA LYASE; CYTOCHROME C OXIDASE; HYDROGEN SULFIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; SULFURTRANSFERASE; UBIQUINOL CYTOCHROME C REDUCTASE; UNCLASSIFIED DRUG; GASOTRANSMITTER;

EID: 84897452490     PISSN: 00071188     EISSN: 14765381     Source Type: Journal    
DOI: 10.1111/bph.12369     Document Type: Review
Times cited : (362)

References (109)
  • 3
    • 77954920936 scopus 로고    scopus 로고
    • Hypoxia in the renal medulla: Implications for hydrogen sulfide signaling
    • Beltowski J, (2010). Hypoxia in the renal medulla: implications for hydrogen sulfide signaling. J Pharmacol Exp Ther 334: 358-363.
    • (2010) J Pharmacol Exp Ther , vol.334 , pp. 358-363
    • Beltowski, J.1
  • 6
    • 79959492292 scopus 로고    scopus 로고
    • Mitochondria and sulfide: A very old story of poisoning, feeding, and signaling?
    • Bouillaud F, Blachier F, (2011). Mitochondria and sulfide: a very old story of poisoning, feeding, and signaling? Antioxid Redox Signal 15: 379-391.
    • (2011) Antioxid Redox Signal , vol.15 , pp. 379-391
    • Bouillaud, F.1    Blachier, F.2
  • 8
    • 84862639554 scopus 로고    scopus 로고
    • Effects of exogenous hydrogen sulphide on calcium signalling, background (TASK) K channel activity and mitochondrial function in chemoreceptor cells
    • Buckler KJ, (2012). Effects of exogenous hydrogen sulphide on calcium signalling, background (TASK) K channel activity and mitochondrial function in chemoreceptor cells. Pflugers Arch 463: 743-754.
    • (2012) Pflugers Arch , vol.463 , pp. 743-754
    • Buckler, K.J.1
  • 9
    • 77950852339 scopus 로고    scopus 로고
    • Novel insights into hydrogen sulfide-mediated cytoprotection
    • Calvert JW, Coetzee WA, Lefer DJ, (2010). Novel insights into hydrogen sulfide-mediated cytoprotection. Antioxid Redox Signal 12: 1203-1217.
    • (2010) Antioxid Redox Signal , vol.12 , pp. 1203-1217
    • Calvert, J.W.1    Coetzee, W.A.2    Lefer, D.J.3
  • 12
    • 84861888611 scopus 로고    scopus 로고
    • Hydrogen sulfide and nitric oxide are mutually dependent in the regulation of angiogenesis and endothelium-dependent vasorelaxation
    • Coletta C, Papapetropoulos A, Erdelyi K, Olah G, Módis K, Panopoulos P, et al. (2012). Hydrogen sulfide and nitric oxide are mutually dependent in the regulation of angiogenesis and endothelium-dependent vasorelaxation. Proc Natl Acad Sci U S A 109: 9161-9166.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 9161-9166
    • Coletta, C.1    Papapetropoulos, A.2    Erdelyi, K.3    Olah, G.4    Módis, K.5    Panopoulos, P.6
  • 13
    • 76049087222 scopus 로고    scopus 로고
    • Using a functional enzyme model to understand the chemistry behind hydrogen sulfide induced hibernation
    • Collman JP, Ghosh S, Dey A, Decréau RA, (2009). Using a functional enzyme model to understand the chemistry behind hydrogen sulfide induced hibernation. Proc Natl Acad Sci U S A 106: 22090-22095.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 22090-22095
    • Collman, J.P.1    Ghosh, S.2    Dey, A.3    Decréau, R.A.4
  • 14
    • 57049151773 scopus 로고    scopus 로고
    • The inhibition of mitochondrial cytochrome oxidase by the gases carbon monoxide, nitric oxide, hydrogen cyanide and hydrogen sulfide: Chemical mechanism and physiological significance
    • Cooper CE, Brown GC, (2008). The inhibition of mitochondrial cytochrome oxidase by the gases carbon monoxide, nitric oxide, hydrogen cyanide and hydrogen sulfide: chemical mechanism and physiological significance. J Bioenerg Biomembr 40: 533-539.
    • (2008) J Bioenerg Biomembr , vol.40 , pp. 533-539
    • Cooper, C.E.1    Brown, G.C.2
  • 15
    • 79959512799 scopus 로고    scopus 로고
    • Chronic exposure to sulfide causes accelerated degradation of cytochrome c oxidase in ethylmalonic encephalopathy
    • Di Meo I, Fagiolari G, Prelle A, Viscomi C, Zeviani M, Tiranti V, (2011). Chronic exposure to sulfide causes accelerated degradation of cytochrome c oxidase in ethylmalonic encephalopathy. Antioxid Redox Signal 15: 353-362.
    • (2011) Antioxid Redox Signal , vol.15 , pp. 353-362
    • Di Meo, I.1    Fagiolari, G.2    Prelle, A.3    Viscomi, C.4    Zeviani, M.5    Tiranti, V.6
  • 16
    • 0036146130 scopus 로고    scopus 로고
    • Cytochrome oxidase inhibition induced by acute hydrogen sulfide inhalation: Correlation with tissue sulfide concentrations in the rat brain, liver, lung, and nasal epithelium
    • Dorman DC, Moulin FJ, McManus BE, Mahle KC, James RA, Struve MF, (2002). Cytochrome oxidase inhibition induced by acute hydrogen sulfide inhalation: correlation with tissue sulfide concentrations in the rat brain, liver, lung, and nasal epithelium. Toxicol Sci 65: 18-25.
    • (2002) Toxicol Sci , vol.65 , pp. 18-25
    • Dorman, D.C.1    Moulin, F.J.2    McManus, B.E.3    Mahle, K.C.4    James, R.A.5    Struve, M.F.6
  • 17
    • 2942733450 scopus 로고    scopus 로고
    • Respiratory tract toxicity of inhaled hydrogen sulfide in Fischer-344 rats, Sprague-Dawley rats, and B6C3F1 mice following subchronic (90-day) exposure
    • Dorman DC, Struve MF, Gross EA, Brenneman KA, (2004). Respiratory tract toxicity of inhaled hydrogen sulfide in Fischer-344 rats, Sprague-Dawley rats, and B6C3F1 mice following subchronic (90-day) exposure. Toxicol Appl Pharmacol 198: 29-39.
    • (2004) Toxicol Appl Pharmacol , vol.198 , pp. 29-39
    • Dorman, D.C.1    Struve, M.F.2    Gross, E.A.3    Brenneman, K.A.4
  • 19
    • 33745920516 scopus 로고    scopus 로고
    • The emerging roles of hydrogen sulfide in the gastrointestinal tract and liver
    • Fiorucci S, Distrutti E, Cirino G, Wallace JL, (2006). The emerging roles of hydrogen sulfide in the gastrointestinal tract and liver. Gastroenterology 131: 259-271.
    • (2006) Gastroenterology , vol.131 , pp. 259-271
    • Fiorucci, S.1    Distrutti, E.2    Cirino, G.3    Wallace, J.L.4
  • 21
    • 77749271091 scopus 로고    scopus 로고
    • Hydrogen sulfide as a gasotransmitter
    • Gadalla MM, Snyder SH, (2010). Hydrogen sulfide as a gasotransmitter. J Neurochem 113: 14-26.
    • (2010) J Neurochem , vol.113 , pp. 14-26
    • Gadalla, M.M.1    Snyder, S.H.2
  • 22
    • 0027469958 scopus 로고
    • Aspects of life development at deep sea hydrothermal vents
    • Gaill F, (1993). Aspects of life development at deep sea hydrothermal vents. FASEB J 7: 558-565.
    • (1993) FASEB J , vol.7 , pp. 558-565
    • Gaill, F.1
  • 25
    • 0031942895 scopus 로고    scopus 로고
    • Animal adaptations for tolerance and exploitation of poisonous sulfide
    • Grieshaber MK, Volkel S, (1998). Animal adaptations for tolerance and exploitation of poisonous sulfide. Annu Rev Physiol 60: 33-53.
    • (1998) Annu Rev Physiol , vol.60 , pp. 33-53
    • Grieshaber, M.K.1    Volkel, S.2
  • 26
    • 84897385414 scopus 로고    scopus 로고
    • Mitochondrial respiration and cytochrome c inhibition by sulfide in peritoneal macrophages in vitro: Effects of temperature and pH
    • Groeger M, Wagner F, Baumgart K, Huber-Lang M, Knoeferl M, Georgieff M, et al. (2010). Mitochondrial respiration and cytochrome c inhibition by sulfide in peritoneal macrophages in vitro: effects of temperature and pH. Crit Care 14: P6.
    • (2010) Crit Care , vol.14
    • Groeger, M.1    Wagner, F.2    Baumgart, K.3    Huber-Lang, M.4    Knoeferl, M.5    Georgieff, M.6
  • 27
    • 84866615775 scopus 로고    scopus 로고
    • Temperature and cell-type dependency of sulfide effects on mitochondrial respiration
    • Groeger M, Matallo J, McCook O, Wagner F, Wachter U, Bastian O, et al. (2012). Temperature and cell-type dependency of sulfide effects on mitochondrial respiration. Shock 38: 367-374.
    • (2012) Shock , vol.38 , pp. 367-374
    • Groeger, M.1    Matallo, J.2    McCook, O.3    Wagner, F.4    Wachter, U.5    Bastian, O.6
  • 28
    • 0030478259 scopus 로고    scopus 로고
    • Organic sulfur compounds resulting from the interaction of iron sulfide, hydrogen sulfide and carbon dioxide in an anaerobic aqueous environment
    • Heinen W, Lauwers AM, (1996). Organic sulfur compounds resulting from the interaction of iron sulfide, hydrogen sulfide and carbon dioxide in an anaerobic aqueous environment. Orig Life Evol Biosph 26: 131-150.
    • (1996) Orig Life Evol Biosph , vol.26 , pp. 131-150
    • Heinen, W.1    Lauwers, A.M.2
  • 29
    • 44949214775 scopus 로고    scopus 로고
    • Three enzymatic activities catalyze the oxidation of sulfide to thiosulfate in mammalian and invertebrate mitochondria
    • Hildebrandt TM, Grieshaber MK, (2008). Three enzymatic activities catalyze the oxidation of sulfide to thiosulfate in mammalian and invertebrate mitochondria. FEBS J 275: 3352-3361.
    • (2008) FEBS J , vol.275 , pp. 3352-3361
    • Hildebrandt, T.M.1    Grieshaber, M.K.2
  • 30
    • 0021665682 scopus 로고
    • Interactions of sulphide and other ligands with cytochrome c oxidase. An electron-paramagnetic-resonance study
    • Hill BC, Woon TC, Nicholls P, Peterson J, Greenwood C, Thomson AJ, (1984). Interactions of sulphide and other ligands with cytochrome c oxidase. An electron-paramagnetic-resonance study. Biochem J 224: 591-600.
    • (1984) Biochem J , vol.224 , pp. 591-600
    • Hill, B.C.1    Woon, T.C.2    Nicholls, P.3    Peterson, J.4    Greenwood, C.5    Thomson, A.J.6
  • 32
    • 70350341436 scopus 로고    scopus 로고
    • Detection of exhaled hydrogen sulphide gas in rats exposed to intravenous sodium sulphide
    • Insko MA, Deckwerth TL, Hill P, Toombs CF, Szabo C, (2009). Detection of exhaled hydrogen sulphide gas in rats exposed to intravenous sodium sulphide. Br J Pharmacol 157: 944-951.
    • (2009) Br J Pharmacol , vol.157 , pp. 944-951
    • Insko, M.A.1    Deckwerth, T.L.2    Hill, P.3    Toombs, C.F.4    Szabo, C.5
  • 33
    • 77954579286 scopus 로고    scopus 로고
    • Redox biochemistry of hydrogen sulfide
    • Kabil O, Banerjee R, (2010). Redox biochemistry of hydrogen sulfide. J Biol Chem 285: 21903-21907.
    • (2010) J Biol Chem , vol.285 , pp. 21903-21907
    • Kabil, O.1    Banerjee, R.2
  • 35
    • 77951541709 scopus 로고    scopus 로고
    • Biogeography and biodiversity in sulfide structures of active and inactive vents at deep-sea hydrothermal fields of the Southern Mariana Trough
    • Kato S, Takano Y, Kakegawa T, Oba H, Inoue K, Kobayashi C, et al. (2010). Biogeography and biodiversity in sulfide structures of active and inactive vents at deep-sea hydrothermal fields of the Southern Mariana Trough. Appl Environ Microbiol 76: 2968-2979.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 2968-2979
    • Kato, S.1    Takano, Y.2    Kakegawa, T.3    Oba, H.4    Inoue, K.5    Kobayashi, C.6
  • 37
    • 0025858854 scopus 로고
    • Cytotoxic effects of hydrogen sulfide on pulmonary alveolar macrophages in rats
    • Khan AA, Yong S, Prior MG, Lillie LE, (1991). Cytotoxic effects of hydrogen sulfide on pulmonary alveolar macrophages in rats. J Toxicol Environ Health 33: 57-64.
    • (1991) J Toxicol Environ Health , vol.33 , pp. 57-64
    • Khan, A.A.1    Yong, S.2    Prior, M.G.3    Lillie, L.E.4
  • 38
    • 77950851571 scopus 로고    scopus 로고
    • Hydrogen sulfide: From brain to gut
    • Kimura H, (2010). Hydrogen sulfide: from brain to gut. Antioxid Redox Signal 12: 1111-1123.
    • (2010) Antioxid Redox Signal , vol.12 , pp. 1111-1123
    • Kimura, H.1
  • 39
    • 84884330886 scopus 로고    scopus 로고
    • Production and physiological effects of hydrogen sulfide
    • (in press).
    • Kimura H, (2013). Production and physiological effects of hydrogen sulfide. Antioxid Redox Signal (in press).
    • (2013) Antioxid Redox Signal
    • Kimura, H.1
  • 40
    • 84860761445 scopus 로고    scopus 로고
    • Hydrogen sulfide is a signaling molecule and a cytoprotectant
    • Kimura H, Shibuya N, Kimura Y, (2012). Hydrogen sulfide is a signaling molecule and a cytoprotectant. Antioxid Redox Signal 17: 45-57.
    • (2012) Antioxid Redox Signal , vol.17 , pp. 45-57
    • Kimura, H.1    Shibuya, N.2    Kimura, Y.3
  • 41
    • 53249087745 scopus 로고    scopus 로고
    • Hydrogen sulfide decreases adenosine triphosphate levels in aortic rings and leads to vasorelaxation via metabolic inhibition
    • Kiss L, Deitch EA, Szabo C, (2008). Hydrogen sulfide decreases adenosine triphosphate levels in aortic rings and leads to vasorelaxation via metabolic inhibition. Life Sci 83: 589-594.
    • (2008) Life Sci , vol.83 , pp. 589-594
    • Kiss, L.1    Deitch, E.A.2    Szabo, C.3
  • 42
    • 79952574146 scopus 로고    scopus 로고
    • A suggested pioneer organism for the Wächtershäuser origin of life hypothesis
    • Kundell FA, (2011). A suggested pioneer organism for the Wächtershäuser origin of life hypothesis. Orig Life Evol Biosph 41: 175-198.
    • (2011) Orig Life Evol Biosph , vol.41 , pp. 175-198
    • Kundell, F.A.1
  • 43
    • 77955672171 scopus 로고    scopus 로고
    • Oxidation of hydrogen sulfide remains a priority in mammalian cells and causes reverse electron transfer in colonocytes
    • Lagoutte E, Mimoun S, Andriamihaja M, Chaumontet C, Blachier F, Bouillaud F, (2010). Oxidation of hydrogen sulfide remains a priority in mammalian cells and causes reverse electron transfer in colonocytes. Biochim Biophys Acta 1797: 1500-1511.
    • (2010) Biochim Biophys Acta , vol.1797 , pp. 1500-1511
    • Lagoutte, E.1    Mimoun, S.2    Andriamihaja, M.3    Chaumontet, C.4    Blachier, F.5    Bouillaud, F.6
  • 45
    • 0028184159 scopus 로고
    • Hydrothermal and oceanic pH conditions of possible relevance to the origin of life
    • MacLeod G, McKeown C, Hall AJ, Russell MJ, (1994). Hydrothermal and oceanic pH conditions of possible relevance to the origin of life. Orig Life Evol Biosph 24: 19-41.
    • (1994) Orig Life Evol Biosph , vol.24 , pp. 19-41
    • MacLeod, G.1    McKeown, C.2    Hall, A.J.3    Russell, M.J.4
  • 49
    • 80054015725 scopus 로고    scopus 로고
    • Thioredoxin and dihydrolipoic acid are required for 3-mercaptopyruvate sulfurtransferase to produce hydrogen sulfide
    • Mikami Y, Shibuya N, Kimura Y, Nagahara N, Ogasawara Y, Kimura H, (2011). Thioredoxin and dihydrolipoic acid are required for 3-mercaptopyruvate sulfurtransferase to produce hydrogen sulfide. Biochem J 439: 479-485.
    • (2011) Biochem J , vol.439 , pp. 479-485
    • Mikami, Y.1    Shibuya, N.2    Kimura, Y.3    Nagahara, N.4    Ogasawara, Y.5    Kimura, H.6
  • 50
    • 0032933688 scopus 로고    scopus 로고
    • Hydrogen sulfide poisoning: Clarification of some controversial issues
    • Milby TH, Baselt RC, (1999). Hydrogen sulfide poisoning: clarification of some controversial issues. Am J Ind Med 35: 192-195.
    • (1999) Am J Ind Med , vol.35 , pp. 192-195
    • Milby, T.H.1    Baselt, R.C.2
  • 52
    • 84897466349 scopus 로고    scopus 로고
    • Regulation of mitochondrial function by hydrogen sulfide. Part II Pathophysiological and therapeutic implications
    • Módis K, Coletta C, Papapetropoulos A, Bos EM, Calzia E, van Goor H, et al. (2013a). Regulation of mitochondrial function by hydrogen sulfide. Part II Pathophysiological and therapeutic implications. Br J Pharmacol (in press).
    • (2013) Br J Pharmacol
    • Módis, K.1    Coletta, C.2    Papapetropoulos, A.3    Bos, E.M.4    Calzia, E.5    Van Goor, H.6
  • 53
    • 84873467050 scopus 로고    scopus 로고
    • Intramitochondrial hydrogen sulfide production by 3-mercaptopyruvate sulfurtransferase maintains mitochondrial electron flow and supports cellular bioenergetics
    • Módis K, Coletta C, Erdélyi K, Papapetropoulos A, Szabo C, (2013b). Intramitochondrial hydrogen sulfide production by 3-mercaptopyruvate sulfurtransferase maintains mitochondrial electron flow and supports cellular bioenergetics. FASEB J 27: 601-611.
    • (2013) FASEB J , vol.27 , pp. 601-611
    • Módis, K.1    Coletta, C.2    Erdélyi, K.3    Papapetropoulos, A.4    Szabo, C.5
  • 54
    • 84886728728 scopus 로고    scopus 로고
    • Hydrogen sulfide-mediated stimulation of mitochondrial electron transport involves inhibition of the mitochondrial phosphodiesterase 2A, elevation of cAMP and activation of protein kinase A
    • (in press).
    • Módis K, Panopoluos P, Coletta C, Papapetropoulos A, Szabo C, (2013c). Hydrogen sulfide-mediated stimulation of mitochondrial electron transport involves inhibition of the mitochondrial phosphodiesterase 2A, elevation of cAMP and activation of protein kinase A. Biochem Pharmacol (in press).
    • (2013) Biochem Pharmacol
    • Módis, K.1    Panopoluos, P.2    Coletta, C.3    Papapetropoulos, A.4    Szabo, C.5
  • 55
    • 84876470345 scopus 로고    scopus 로고
    • Oxidative stress suppresses the cellular bioenergetic effect of the 3-mercaptopyruvate sulfurtransferase/hydrogen sulfide pathway
    • Módis K, Asimakopoulou A, Coletta C, Papapetropoulos A, Szabo C, (2013d). Oxidative stress suppresses the cellular bioenergetic effect of the 3-mercaptopyruvate sulfurtransferase/hydrogen sulfide pathway. Biochem Biophys Res Commun 433: 401-407.
    • (2013) Biochem Biophys Res Commun , vol.433 , pp. 401-407
    • Módis, K.1    Asimakopoulou, A.2    Coletta, C.3    Papapetropoulos, A.4    Szabo, C.5
  • 56
    • 84879179357 scopus 로고    scopus 로고
    • Hydrogen sulfide in cell signaling, signal transduction, cellular bioenergetics and physiology in C. Elegans
    • Módis K, Wolanska K, Wozdek R, (2013e). Hydrogen sulfide in cell signaling, signal transduction, cellular bioenergetics and physiology in C. elegans. Gen Physiol Biophys 32: 1-22.
    • (2013) Gen Physiol Biophys , vol.32 , pp. 1-22
    • Módis, K.1    Wolanska, K.2    Wozdek, R.3
  • 59
    • 84879682497 scopus 로고    scopus 로고
    • Regulation of mercaptopyruvate sulfurtransferase activity via intrasubunit and intersubunit redox-sensing switches
    • (in press).
    • Nagahara N, (2013). Regulation of mercaptopyruvate sulfurtransferase activity via intrasubunit and intersubunit redox-sensing switches. Antioxid Redox Signal (in press).
    • (2013) Antioxid Redox Signal
    • Nagahara, N.1
  • 60
    • 27144442871 scopus 로고    scopus 로고
    • Post-translational regulation of mercaptopyruvate sulfurtransferase via a low redox potential cysteine-sulfenate in the maintenance of redox homeostasis
    • Nagahara N, Katayama A, (2005). Post-translational regulation of mercaptopyruvate sulfurtransferase via a low redox potential cysteine-sulfenate in the maintenance of redox homeostasis. J Biol Chem 280: 34569-34576.
    • (2005) J Biol Chem , vol.280 , pp. 34569-34576
    • Nagahara, N.1    Katayama, A.2
  • 61
    • 84857623740 scopus 로고    scopus 로고
    • Is novel signal transducer sulfur oxide involved in the redox cycle of persulfide at the catalytic site cysteine in a stable reaction intermediate of mercaptopyruvate sulfurtransferase?
    • Nagahara N, Nirasawa T, Yoshii T, Niimura Y, (2012). Is novel signal transducer sulfur oxide involved in the redox cycle of persulfide at the catalytic site cysteine in a stable reaction intermediate of mercaptopyruvate sulfurtransferase? Antioxid Redox Signal 16: 747-753.
    • (2012) Antioxid Redox Signal , vol.16 , pp. 747-753
    • Nagahara, N.1    Nirasawa, T.2    Yoshii, T.3    Niimura, Y.4
  • 63
    • 0016742498 scopus 로고
    • The effect of sulphide on cytochrome aa3. Isosteric and allosteric shifts of the reduced alpha-peak
    • Nicholls P, (1975). The effect of sulphide on cytochrome aa3. Isosteric and allosteric shifts of the reduced alpha-peak. Biochim Biophys Acta 396: 24-35.
    • (1975) Biochim Biophys Acta , vol.396 , pp. 24-35
    • Nicholls, P.1
  • 64
    • 0019879881 scopus 로고
    • Oxidation of sulphide by cytochrome aa3
    • Nicholls P, Kim JK, (1981). Oxidation of sulphide by cytochrome aa3. Biochim Biophys Acta 637: 312-320.
    • (1981) Biochim Biophys Acta , vol.637 , pp. 312-320
    • Nicholls, P.1    Kim, J.K.2
  • 65
    • 0020149565 scopus 로고
    • Sulphide as an inhibitor and electron donor for the cytochrome c oxidase system
    • Nicholls P, Kim JK, (1982). Sulphide as an inhibitor and electron donor for the cytochrome c oxidase system. Can J Biochem 60: 613-623.
    • (1982) Can J Biochem , vol.60 , pp. 613-623
    • Nicholls, P.1    Kim, J.K.2
  • 68
    • 0242469070 scopus 로고    scopus 로고
    • The effect of antibiotics and bismuth on fecal hydrogen sulfide and sulfate-reducing bacteria in the rat
    • Ohge H, Furne JK, Springfield J, Sueda T, Madoff RD, Levitt MD, (2003). The effect of antibiotics and bismuth on fecal hydrogen sulfide and sulfate-reducing bacteria in the rat. FEMS Microbiol Lett 228: 137-142.
    • (2003) FEMS Microbiol Lett , vol.228 , pp. 137-142
    • Ohge, H.1    Furne, J.K.2    Springfield, J.3    Sueda, T.4    Madoff, R.D.5    Levitt, M.D.6
  • 69
    • 84860758991 scopus 로고    scopus 로고
    • A practical look at the chemistry and biology of hydrogen sulfide
    • Olson KR, (2012). A practical look at the chemistry and biology of hydrogen sulfide. Antioxid Redox Signal 17: 32-44.
    • (2012) Antioxid Redox Signal , vol.17 , pp. 32-44
    • Olson, K.R.1
  • 70
    • 84881497241 scopus 로고    scopus 로고
    • Hydrogen sulfide as an oxygen sensor
    • Olson KR, (2013). Hydrogen sulfide as an oxygen sensor. Clin Chem Lab Med 51: 623-632.
    • (2013) Clin Chem Lab Med , vol.51 , pp. 623-632
    • Olson, K.R.1
  • 71
    • 77950801465 scopus 로고    scopus 로고
    • Hydrogen sulfide and oxygen sensing in the cardiovascular system
    • Olson KR, Whitfield NL, (2010). Hydrogen sulfide and oxygen sensing in the cardiovascular system. Antioxid Redox Signal 12: 1219-1234.
    • (2010) Antioxid Redox Signal , vol.12 , pp. 1219-1234
    • Olson, K.R.1    Whitfield, N.L.2
  • 73
    • 84879411608 scopus 로고    scopus 로고
    • Linking geology, fluid chemistry, and microbial activity of basalt- and ultramafic-hosted deep-sea hydrothermal vent environments
    • Perner M, Hansen M, Seifert R, Strauss H, Koschinsky A, Petersen S, (2013). Linking geology, fluid chemistry, and microbial activity of basalt- and ultramafic-hosted deep-sea hydrothermal vent environments. Geobiology 11: 340-355.
    • (2013) Geobiology , vol.11 , pp. 340-355
    • Perner, M.1    Hansen, M.2    Seifert, R.3    Strauss, H.4    Koschinsky, A.5    Petersen, S.6
  • 74
    • 0017353388 scopus 로고
    • The effect of inhibitors on the oxygen kinetics of cytochrome c oxidase
    • Petersen LC, (1977). The effect of inhibitors on the oxygen kinetics of cytochrome c oxidase. Biochim Biophys Acta 460: 299-307.
    • (1977) Biochim Biophys Acta , vol.460 , pp. 299-307
    • Petersen, L.C.1
  • 75
    • 0022554531 scopus 로고
    • Hydrogen sulfide oxidation is coupled to oxidative phosphorylation in mitochondria of Solemya reidi
    • Powell MA, Somero GN, (1986). Hydrogen sulfide oxidation is coupled to oxidative phosphorylation in mitochondria of Solemya reidi. Science 233: 563-566.
    • (1986) Science , vol.233 , pp. 563-566
    • Powell, M.A.1    Somero, G.N.2
  • 76
    • 77958110849 scopus 로고    scopus 로고
    • Development of hydrogen sulfide-based therapeutics for cardiovascular disease
    • Predmore BL, Lefer DJ, (2010). Development of hydrogen sulfide-based therapeutics for cardiovascular disease. J Cardiovasc Transl Res 3: 487-498.
    • (2010) J Cardiovasc Transl Res , vol.3 , pp. 487-498
    • Predmore, B.L.1    Lefer, D.J.2
  • 79
    • 1542572798 scopus 로고    scopus 로고
    • Metabolic integration during the evolutionary origin of mitochondria
    • Searcy DG, (2003). Metabolic integration during the evolutionary origin of mitochondria. Cell Res 13: 229-238.
    • (2003) Cell Res , vol.13 , pp. 229-238
    • Searcy, D.G.1
  • 81
    • 84864408372 scopus 로고    scopus 로고
    • Screening of genes related to sulfide metabolism in Urechis unicinctus (Echiura, Urechidae) using suppression subtractive hybridization and cDNA microarray analysis
    • Shi X, Shao M, Zhang L, Ma Y, Zhang Z, (2012). Screening of genes related to sulfide metabolism in Urechis unicinctus (Echiura, Urechidae) using suppression subtractive hybridization and cDNA microarray analysis. Comp Biochem Physiol Part D Genomics Proteomics 7: 254-259.
    • (2012) Comp Biochem Physiol Part D Genomics Proteomics , vol.7 , pp. 254-259
    • Shi, X.1    Shao, M.2    Zhang, L.3    Ma, Y.4    Zhang, Z.5
  • 82
    • 70449686289 scopus 로고    scopus 로고
    • Vascular endothelium expresses 3-mercaptopyruvate sulfurtransferase and produces hydrogen sulfide
    • Shibuya N, Mikami Y, Kimura Y, Nagahara N, Kimura H, (2009a). Vascular endothelium expresses 3-mercaptopyruvate sulfurtransferase and produces hydrogen sulfide. J Biochem 146: 623-626.
    • (2009) J Biochem , vol.146 , pp. 623-626
    • Shibuya, N.1    Mikami, Y.2    Kimura, Y.3    Nagahara, N.4    Kimura, H.5
  • 83
    • 60749088329 scopus 로고    scopus 로고
    • 3-Mercaptopyruvate sulfurtransferase produces hydrogen sulfide and bound sulfane sulfur in the brain
    • Shibuya N, Tanaka M, Yoshida M, Ogasawara Y, Togawa T, Ishii K, et al. (2009b). 3-Mercaptopyruvate sulfurtransferase produces hydrogen sulfide and bound sulfane sulfur in the brain. Antioxid Redox Signal 11: 703-714.
    • (2009) Antioxid Redox Signal , vol.11 , pp. 703-714
    • Shibuya, N.1    Tanaka, M.2    Yoshida, M.3    Ogasawara, Y.4    Togawa, T.5    Ishii, K.6
  • 84
    • 84868322708 scopus 로고    scopus 로고
    • 2S is required for hypoxic sensing by carotid body glomus cells'
    • 2S is required for hypoxic sensing by carotid body glomus cells'. Am J Physiol Cell Physiol 303: C911-C912.
    • (2012) Am J Physiol Cell Physiol , vol.303
    • Smith, K.A.1    Yuan, J.X.2
  • 85
    • 0034962142 scopus 로고    scopus 로고
    • Neurotoxicological effects associated with short-term exposure of Sprague-Dawley rats to hydrogen sulfide
    • Struve MF, Brisbois JN, James RA, Marshall MW, Dorman DC, (2001). Neurotoxicological effects associated with short-term exposure of Sprague-Dawley rats to hydrogen sulfide. Neurotoxicology 22: 375-385.
    • (2001) Neurotoxicology , vol.22 , pp. 375-385
    • Struve, M.F.1    Brisbois, J.N.2    James, R.A.3    Marshall, M.W.4    Dorman, D.C.5
  • 86
    • 84860437228 scopus 로고    scopus 로고
    • Hydrogen sulfide decreases the levels of ROS by inhibiting mitochondrial Complex IV and increasing SOD activities in cardiomyocytes under ischemia/reperfusion
    • Sun WH, Liu F, Chen Y, Zhu YC, (2012). Hydrogen sulfide decreases the levels of ROS by inhibiting mitochondrial Complex IV and increasing SOD activities in cardiomyocytes under ischemia/reperfusion. Biochem Biophys Res Commun 421: 164-169.
    • (2012) Biochem Biophys Res Commun , vol.421 , pp. 164-169
    • Sun, W.H.1    Liu, F.2    Chen, Y.3    Zhu, Y.C.4
  • 87
    • 84857869999 scopus 로고    scopus 로고
    • Life and death of deep-sea vents: Bacterial diversity and ecosystem succession on inactive hydrothermal sulfides
    • Sylvan JB, Toner BM, Edwards KJ, (2012). Life and death of deep-sea vents: bacterial diversity and ecosystem succession on inactive hydrothermal sulfides. Mbio 3: e00279-e00211.
    • (2012) Mbio , vol.3
    • Sylvan, J.B.1    Toner, B.M.2    Edwards, K.J.3
  • 88
    • 35748959038 scopus 로고    scopus 로고
    • Hydrogen sulphide and its therapeutic potential
    • Szabo C, (2007). Hydrogen sulphide and its therapeutic potential. Nat Rev Drug Discov 6: 917-935.
    • (2007) Nat Rev Drug Discov , vol.6 , pp. 917-935
    • Szabo, C.1
  • 91
    • 84155171245 scopus 로고    scopus 로고
    • Identification of agents that reduce renal hypoxia-reoxygenation injury using cell-based screening: Purine nucleosides are alternative energy sources in LLC-PK1 cells during hypoxia
    • Szoleczky P, Módis K, Nagy N, Dóri Tóth Z, DeWitt D, Szabo C, et al. (2012). Identification of agents that reduce renal hypoxia-reoxygenation injury using cell-based screening: purine nucleosides are alternative energy sources in LLC-PK1 cells during hypoxia. Arch Biochem Biophys 517: 53-70.
    • (2012) Arch Biochem Biophys , vol.517 , pp. 53-70
    • Szoleczky, P.1    Módis, K.2    Nagy, N.3    Dóri Tóth, Z.4    Dewitt, D.5    Szabo, C.6
  • 93
    • 79953175962 scopus 로고    scopus 로고
    • 2S by 3-mercaptopyruvate sulphurtransferase
    • 2S by 3-mercaptopyruvate sulphurtransferase. J Biochem 149: 357-359.
    • (2011) J Biochem , vol.149 , pp. 357-359
    • Tanizawa, K.1
  • 94
    • 84881101982 scopus 로고    scopus 로고
    • Oxygen-sensitive mitochondrial accumulation of cystathione β-synthase mediated by Lon protease
    • Teng H, Wu B, Zhao K, Yang G, Wu L, Wang R, (2013). Oxygen-sensitive mitochondrial accumulation of cystathione β-synthase mediated by Lon protease. Proc Natl Acad Sci U S A 110: 12679-12684.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 12679-12684
    • Teng, H.1    Wu, B.2    Zhao, K.3    Yang, G.4    Wu, L.5    Wang, R.6
  • 95
    • 0037723099 scopus 로고    scopus 로고
    • Cytotoxic mechanisms of hydrosulfide anion and cyanide anion in primary rat hepatocyte cultures
    • Thompson RW, Valentine HL, Valentine WM, (2003). Cytotoxic mechanisms of hydrosulfide anion and cyanide anion in primary rat hepatocyte cultures. Toxicology 188: 149-159.
    • (2003) Toxicology , vol.188 , pp. 149-159
    • Thompson, R.W.1    Valentine, H.L.2    Valentine, W.M.3
  • 96
    • 77952057690 scopus 로고    scopus 로고
    • Detection of exhaled hydrogen sulphide gas in healthy human volunteers during intravenous administration of sodium sulphide
    • Toombs CF, Insko MA, Wintner EA, Deckwerth TL, Usansky H, Jamil K, et al. (2010). Detection of exhaled hydrogen sulphide gas in healthy human volunteers during intravenous administration of sodium sulphide. Br J Clin Pharmacol 69: 626-636.
    • (2010) Br J Clin Pharmacol , vol.69 , pp. 626-636
    • Toombs, C.F.1    Insko, M.A.2    Wintner, E.A.3    Deckwerth, T.L.4    Usansky, H.5    Jamil, K.6
  • 98
    • 0030068577 scopus 로고    scopus 로고
    • Mitochondrial sulfide oxidation in Arenicola marina
    • Volkel S, Grieshaber M, (1997). Mitochondrial sulfide oxidation in Arenicola marina. Eur J Biochem 235: 231-237.
    • (1997) Eur J Biochem , vol.235 , pp. 231-237
    • Volkel, S.1    Grieshaber, M.2
  • 99
    • 41149146946 scopus 로고    scopus 로고
    • Inhaled hydrogen sulfide: A rapidly reversible inhibitor of cardiac and metabolic function in the mouse
    • Volpato GP, Searles R, Yu B, Scherrer-Crosbie M, Bloch KD, Ichinose F, et al. (2008). Inhaled hydrogen sulfide: a rapidly reversible inhibitor of cardiac and metabolic function in the mouse. Anesthesiology 108: 659-668.
    • (2008) Anesthesiology , vol.108 , pp. 659-668
    • Volpato, G.P.1    Searles, R.2    Yu, B.3    Scherrer-Crosbie, M.4    Bloch, K.D.5    Ichinose, F.6
  • 100
    • 84859464714 scopus 로고    scopus 로고
    • Novel structural arrangement of nematode cystathionine β-synthases: Characterization of Caenorhabditis elegans CBS-1
    • Vozdek R, Hnízda A, Krijt J, Kostrouchová M, Kožich V, (2012). Novel structural arrangement of nematode cystathionine β-synthases: characterization of Caenorhabditis elegans CBS-1. Biochem J 443: 535-547.
    • (2012) Biochem J , vol.443 , pp. 535-547
    • Vozdek, R.1    Hnízda, A.2    Krijt, J.3    Kostrouchová, M.4    Kožich, V.5
  • 101
    • 70350452015 scopus 로고    scopus 로고
    • Bench-to-bedside review: Hydrogen sulfide - The third gaseous transmitter: Applications for critical care
    • Wagner F, Asfar P, Calzia E, Radermacher P, Szabo C, (2009). Bench-to-bedside review: hydrogen sulfide-the third gaseous transmitter: applications for critical care. Crit Care 13: 213.
    • (2009) Crit Care , vol.13 , pp. 213
    • Wagner, F.1    Asfar, P.2    Calzia, E.3    Radermacher, P.4    Szabo, C.5
  • 102
    • 84860117196 scopus 로고    scopus 로고
    • Physiological implications of hydrogen sulfide: A whiff exploration that blossomed
    • Wang R, (2012). Physiological implications of hydrogen sulfide: a whiff exploration that blossomed. Physiol Rev 92: 791-896.
    • (2012) Physiol Rev , vol.92 , pp. 791-896
    • Wang, R.1
  • 103
    • 2042432480 scopus 로고
    • Cytochrome oxidase from beef heart mitochondria
    • Estabrook R.W. Pullman M.E. (eds). Academic Press: New York
    • Wharton DC, Tzagoloff A, (1967). Cytochrome oxidase from beef heart mitochondria. In:, Estabrook RW, Pullman ME, (eds). Methods in Enzymology, Vol. 10. Academic Press: New York, pp. 245-250.
    • (1967) Methods in Enzymology , vol.10 , pp. 245-250
    • Wharton, D.C.1    Tzagoloff, A.2
  • 104
    • 78650485623 scopus 로고    scopus 로고
    • Hydrogen sulfide and inflammation: The good, the bad, the ugly and the promising
    • Whiteman M, Winyard PG, (2011). Hydrogen sulfide and inflammation: the good, the bad, the ugly and the promising. Expert Rev Clin Pharmacol 4: 13-32.
    • (2011) Expert Rev Clin Pharmacol , vol.4 , pp. 13-32
    • Whiteman, M.1    Winyard, P.G.2
  • 105
    • 80052373686 scopus 로고    scopus 로고
    • Emerging role of hydrogen sulfide in health and disease: Critical appraisal of biomarkers and pharmacological tools
    • Whiteman M, Le Trionnaire S, Chopra M, Fox B, Whatmore J, (2011). Emerging role of hydrogen sulfide in health and disease: critical appraisal of biomarkers and pharmacological tools. Clin Sci (Lond) 121: 459-488.
    • (2011) Clin Sci (Lond) , vol.121 , pp. 459-488
    • Whiteman, M.1    Le Trionnaire, S.2    Chopra, M.3    Fox, B.4    Whatmore, J.5
  • 106
    • 77952859292 scopus 로고    scopus 로고
    • A monobromobimane-based assay to measure the pharmacokinetic profile of reactive sulphide species in blood
    • Wintner EA, Deckwerth TL, Langston W, Bengtsson A, Leviten D, Hill P, et al. (2010). A monobromobimane-based assay to measure the pharmacokinetic profile of reactive sulphide species in blood. Br J Pharmacol 160: 941-957.
    • (2010) Br J Pharmacol , vol.160 , pp. 941-957
    • Wintner, E.A.1    Deckwerth, T.L.2    Langston, W.3    Bengtsson, A.4    Leviten, D.5    Hill, P.6
  • 107
    • 79954517258 scopus 로고    scopus 로고
    • Myocardial and lung injuries induced by hydrogen sulfide and the effectiveness of oxygen therapy in rats
    • Wu N, Du X, Wang D, Hao F, (2011). Myocardial and lung injuries induced by hydrogen sulfide and the effectiveness of oxygen therapy in rats. Clin Toxicol (Phila) 49: 161-166.
    • (2011) Clin Toxicol (Phila) , vol.49 , pp. 161-166
    • Wu, N.1    Du, X.2    Wang, D.3    Hao, F.4
  • 109
    • 0035030625 scopus 로고    scopus 로고
    • Sulfide oxidation coupled to ATP synthesis in chicken liver mitochondria
    • Yong R, Searcy DG, (2001). Sulfide oxidation coupled to ATP synthesis in chicken liver mitochondria. Comp Biochem Physiol B Biochem Mol Biol 129: 129-137.
    • (2001) Comp Biochem Physiol B Biochem Mol Biol , vol.129 , pp. 129-137
    • Yong, R.1    Searcy, D.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.