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Volumn 31, Issue 1, 2016, Pages 60-72

The role of hydrogen sulfide in evolution and the evolution of hydrogen sulfide in metabolism and signaling

Author keywords

[No Author keywords available]

Indexed keywords

HYDROGEN SULFIDE; OXYGEN;

EID: 84949949016     PISSN: 15489213     EISSN: 15489221     Source Type: Journal    
DOI: 10.1152/physiol.00024.2015     Document Type: Review
Times cited : (205)

References (180)
  • 1
    • 0026614974 scopus 로고
    • Sulfide as an environmental factor and toxicant:Tolerance and adaptations in aquatic organisms
    • Bagarinao T. Sulfide as an environmental factor and toxicant: tolerance and adaptations in aquatic organisms. Aquat Toxicol (Amst) 24: 21-62, 1992
    • (1992) Aquat Toxicol(Amst) , vol.24 , pp. 21-62
    • Bagarinao, T.1
  • 2
    • 0025605321 scopus 로고
    • Oxidative detoxification of sulfide bymitochondria of the California killifish, Fundulus parvipinnisand the speckled sanddab, Citharichthys stigmaeus
    • Bagarinao T, Vetter RD. Oxidative detoxification of sulfide by mitochondria of the California killifish, Fundulus parvipinnis and the speckled sanddab, Citharichthys stigmaeus. J Comp Physiol A 160: 519-527, 1990
    • (1990) J Compphysiol A , vol.160 , pp. 519-527
    • Bagarinao, T.1    Vetter, R.D.2
  • 3
    • 9744276776 scopus 로고    scopus 로고
    • Redox regulation and reaction mechanismof human cystathionine-beta-synthase: A PLP-dependenthemesensor protein
    • Banerjee R, Zou CG. Redox regulation and reaction mechanism of human cystathionine-beta-synthase: a PLP-dependent hemesensor protein. Arch Biochem Biophys 433: 144-156, 2005
    • (2005) Arch Biochem Biophys , vol.433 , pp. 144-156
    • Banerjee, R.1    Zou, C.G.2
  • 4
    • 26944486178 scopus 로고    scopus 로고
    • Late Archean to early Paleoproterozoicglobal tectonics, environmental change and therise of atmospheric oxygen
    • Barley ME, Bekker A, Krapež B. Late Archean to early Paleoproterozoic global tectonics, environmental change and the rise of atmospheric oxygen. Earth Planetary Sci Lett 238: 156-171, 2005
    • (2005) Earth Planetary Sci Lett , vol.238 , pp. 156-171
    • Barley, M.E.1    Bekker, A.2    Krapež, B.3
  • 5
    • 84913585957 scopus 로고    scopus 로고
    • Hydrogen sulfide: Atoxic gas produced by dissimilatory sulfate and sulfur reductionand consumed by microbial oxidation
    • Barton LL, Fardeau ML, Fauque GD. Hydrogen sulfide: a toxic gas produced by dissimilatory sulfate and sulfur reduction and consumed by microbial oxidation. Met Ions Life Sci 14: 237-277, 2014
    • (2014) Met Ions Life Sci , vol.14 , pp. 237-277
    • Barton, L.L.1    Fardeau, M.L.2    Fauque, G.D.3
  • 6
    • 59449093719 scopus 로고    scopus 로고
    • Biochemistry, physiology and biotechnologyof sulfate-reducing bacteria
    • Barton LL, Fauque GD. Biochemistry, physiology and biotechnology of sulfate-reducing bacteria. Adv Appl Microbiol 68: 41-98, 2009
    • (2009) Adv Appl Microbiol , vol.68 , pp. 41-98
    • Barton, L.L.1    Fauque, G.D.2
  • 8
    • 79959492292 scopus 로고    scopus 로고
    • Mitochondria and sulfide: A very oldstory of poisoning, feeding and signaling?
    • Bouillaud F, Blachier F. Mitochondria and sulfide: a very old story of poisoning, feeding and signaling? Antioxid Redox Signal 15: 379-391, 2011
    • (2011) Antioxid Redoxsignal , vol.15 , pp. 379-391
    • Bouillaud, F.1    Blachier, F.2
  • 9
    • 66149189584 scopus 로고    scopus 로고
    • Inorganic nitrogenreduction and stability under simulated hydrothermal conditions
    • Brandes JA, Hazen RM, Yoder HS Jr. Inorganic nitrogen reduction and stability under simulated hydrothermal conditions. Astrobiology 8: 1113-1126, 2008
    • (2008) Astrobiology , vol.8 , pp. 1113-1126
    • Brandes, J.A.1    Hazen, R.M.2    Yoder, H.S.3
  • 10
    • 84871719406 scopus 로고    scopus 로고
    • Turnstiles and bifurcators: The disequilibriumconverting engines that put metabolism on theroad
    • Branscomb E, Russell MJ. Turnstiles and bifurcators: the disequilibrium converting engines that put metabolism on the road. Biochim Biophys Acta 1827: 62-78, 2013
    • (2013) Biochim Biophys Acta , vol.1827 , pp. 62-78
    • Branscomb, E.1    Russell, M.J.2
  • 11
    • 81055127888 scopus 로고    scopus 로고
    • System xc(-) cystine/glutamateantiporter: An update on molecular pharmacology androles within the CNS
    • Bridges RJ, Natale NR, Patel SA. System xc(-) cystine/glutamate antiporter: an update on molecular pharmacology and roles within the CNS. Br J Pharmacol 165: 20-34, 2012
    • (2012) Br J Pharmacol , vol.165 , pp. 20-34
    • Bridges, R.J.1    Natale, N.R.2    Patel, S.A.3
  • 12
    • 58449135158 scopus 로고    scopus 로고
    • The multiple evolutionaryhistories of dioxygen reductases: Implications for theorigin and evolution of aerobic respiration
    • Brochier-Armanet C, Talla E, Gribaldo S. The multiple evolutionary histories of dioxygen reductases: implications for the origin and evolution of aerobic respiration. Mol Biol Evol 26: 285-297, 2009
    • (2009) Mol Biol Evol , vol.26 , pp. 285-297
    • Brochier-Armanet, C.1    Talla, E.2    Gribaldo, S.3
  • 13
    • 0028239826 scopus 로고
    • Evolution ofcytochrome oxidase, an enzyme older than atmospheric oxygen
    • Castresana J, Lubben M, Saraste M, Higgins DG. Evolution of cytochrome oxidase, an enzyme older than atmospheric oxygen. EMBO J 13: 2516-2525, 1994
    • (1994) EMBO J , vol.13 , pp. 2516-2525
    • Castresana, J.1    Lubben, M.2    Saraste, M.3    Higgins, D.G.4
  • 15
    • 66449109703 scopus 로고    scopus 로고
    • H2S biogenesis by human cystathionine gamma-lyase leadsto the novel sulfur metabolites lanthionine and homolanthionineand is responsive to the grade of hyperhomocysteinemia
    • Chiku T, Padovani D, Zhu W, Singh S, Vitvitsky V, Banerjee R. H2S biogenesis by human cystathionine gamma-lyase leads to the novel sulfur metabolites lanthionine and homolanthionine and is responsive to the grade of hyperhomocysteinemia. J Biol Chem 284: 11601-11612, 2009
    • (2009) J Biol Chem , vol.284 , pp. 11601-11612
    • Chiku, T.1    Padovani, D.2    Zhu, W.3    Singh, S.4    Vitvitsky, V.5    Banerjee, R.6
  • 16
    • 3042639896 scopus 로고    scopus 로고
    • Transition metal sulfides and the origins of metabolism
    • Cody GD. Transition metal sulfides and the origins of metabolism. Annu Rev Earth Planet Sci 32: 569-599, 2004
    • (2004) Annu Rev Earth Planet Sci , vol.32 , pp. 569-599
    • Cody, G.D.1
  • 17
    • 57049151773 scopus 로고    scopus 로고
    • The inhibition of mitochondrial cytochromeoxidase by the gases carbon monoxide, nitric oxide,hydrogen cyanide and hydrogen sulfide: Chemical mechanismand physiological significance
    • Cooper CE, Brown GC. 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
    • (2008) J Bioenerg Biomembr , vol.40 , pp. 533-539
    • Cooper, C.E.1    Brown, G.C.2
  • 21
    • 70349303869 scopus 로고    scopus 로고
    • Predation between prokaryotes andthe origin of eukaryotes
    • Davidov Y, Jurkevitch E. Predation between prokaryotes and the origin of eukaryotes. Bioessays 31: 748-757, 2009
    • (2009) Bioessays , vol.31 , pp. 748-757
    • Davidov, Y.1    Jurkevitch, E.2
  • 22
    • 34447302552 scopus 로고    scopus 로고
    • Mineral interface in extremehabitats: A niche for primitive molecular evolution for theappearance of different forms of life on earth
    • de Souza-Barros F, Vieyra A. Mineral interface in extreme habitats: a niche for primitive molecular evolution for the appearance of different forms of life on earth. Comp Biochem Physiol C Toxicol Pharmacol 146: 10-21, 2007
    • (2007) Compbiochem Physiol C Toxicol Pharmacol , vol.146 , pp. 10-21
    • De Souza-Barros, F.1    Vieyra, A.2
  • 24
    • 84855893273 scopus 로고    scopus 로고
    • Passive loss of hydrogensulfide in biological experiments
    • DeLeon ER, Stoy GF, Olson KR. Passive loss of hydrogen sulfide in biological experiments. Anal Biochem 421: 203-207, 2012
    • (2012) Anal Biochem , vol.421 , pp. 203-207
    • Deleon, E.R.1    Stoy, G.F.2    Olson, K.R.3
  • 25
    • 0032808433 scopus 로고    scopus 로고
    • Chemolithoheterotrophyin a metazoan tissue: Sulfide supports cellularwork in ciliated mussel gills
    • Doeller JE, Gaschen BK, Parrino V 5th, Kraus DW. Chemolithoheterotrophy in a metazoan tissue: sulfide supports cellular work in ciliated mussel gills. J Exp Biol 202: 1953-1961, 1999
    • (1999) J Exp Biol , vol.202 , pp. 1953-1961
    • Doeller, J.E.1    Gaschen, B.K.2    Parrino, V.3    Kraus, D.W.4
  • 26
    • 0035746153 scopus 로고    scopus 로고
    • Chemolithoheterotrophyin a metazoan tissue: Thiosulfate production matchesATP demand in ciliated mussel gills
    • Doeller JE, Grieshaber MK, Kraus DW. Chemolithoheterotrophy in a metazoan tissue: thiosulfate production matches ATP demand in ciliated mussel gills. J Exp Biol 204: 3755-3764, 2001
    • (2001) J Exp Biol , vol.204 , pp. 3755-3764
    • Doeller, J.E.1    Grieshaber, M.K.2    Kraus, D.W.3
  • 28
    • 33645456207 scopus 로고    scopus 로고
    • Eukaryotic evolution, changes andchallenges
    • Embley TM, Martin W. Eukaryotic evolution, changes and challenges. Nature 440: 623-630, 2006
    • (2006) Nature , vol.440 , pp. 623-630
    • Embley, T.M.1    Martin, W.2
  • 30
    • 81755174221 scopus 로고    scopus 로고
    • The reaction ofH2S with oxidized thiols: Generation of persulfides and implicationsto H2S biology
    • Francoleon NE, Carrington SJ, Fukuto JM. The reaction of H2S with oxidized thiols: generation of persulfides and implications to H2S biology. Arch Biochem Biophys 516: 146-153, 2011
    • (2011) Arch Biochem Biophys , vol.516 , pp. 146-153
    • Francoleon, N.E.1    Carrington, S.J.2    Fukuto, J.M.3
  • 31
    • 6344256938 scopus 로고    scopus 로고
    • Seeing green bacteria in a new light:Genomics-enabled studies of the photosynthetic apparatus ingreen sulfur bacteria and filamentous anoxygenic phototrophicbacteria
    • Frigaard NU, Bryant DA. Seeing green bacteria in a new light: genomics-enabled studies of the photosynthetic apparatus in green sulfur bacteria and filamentous anoxygenic phototrophic bacteria. Arch Microbiol 182: 265-276, 2004
    • (2004) Arch Microbiol , vol.182 , pp. 265-276
    • Frigaard, N.U.1    Bryant, D.A.2
  • 32
    • 84857409875 scopus 로고    scopus 로고
    • Hydrogensulfide (H2S) metabolism in mitochondria and its regulatoryrole in energy production
    • Fu M, Zhang W, Wu L, Yang G, Li H, Wang R. Hydrogen sulfide (H2S) metabolism in mitochondria and its regulatory role in energy production. Proc Natl Acad Sci USA 109: 2943-2948, 2012
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 2943-2948
    • Fu, M.1    Zhang, W.2    Wu, L.3    Yang, G.4    Li, H.5    Wang, R.6
  • 33
    • 0035879968 scopus 로고    scopus 로고
    • Oxidation of hydrogen sulfide and methanethiol to thiosulfateby rat tissues: A specialized function of the colonic mucosa
    • Furne J, Springfield J, Koenig T, DeMaster E, Levitt MD. Oxidation of hydrogen sulfide and methanethiol to thiosulfate by rat tissues: a specialized function of the colonic mucosa. Biochem Pharmacol 62: 255-259, 2001
    • (2001) Biochem Pharmacol , vol.62 , pp. 255-259
    • Furne, J.1    Springfield, J.2    Koenig, T.3    Demaster, E.4    Levitt, M.D.5
  • 34
    • 80054025183 scopus 로고    scopus 로고
    • Atmospheric oxygenationcaused by a change in volcanic degassing pressure
    • Gaillard F, Scaillet B, Arndt NT. Atmospheric oxygenation caused by a change in volcanic degassing pressure. Nature 478: 229-232, 2011
    • (2011) Nature , vol.478 , pp. 229-232
    • Gaillard, F.1    Scaillet, B.2    Arndt, N.T.3
  • 37
    • 80052907486 scopus 로고    scopus 로고
    • Mechanisms andevolution of oxidative sulfur metabolism in green sulfur bacteria
    • Gregersen LH, Bryant DA, Frigaard NU. Mechanisms and evolution of oxidative sulfur metabolism in green sulfur bacteria. Front Microbiol 2: 116, 2011
    • (2011) Front Microbiol , vol.2
    • Gregersen, L.H.1    Bryant, D.A.2    Frigaard, N.U.3
  • 39
    • 68249114988 scopus 로고    scopus 로고
    • Evolutionof the haem copper oxidases superfamily: Arooting tale
    • Gribaldo S, Talla E, Brochier-Armanet C. Evolution of the haem copper oxidases superfamily: a rooting tale. Trends Biochem Sci 34: 375-381, 2009
    • (2009) Trends Biochem Sci , vol.34 , pp. 375-381
    • Gribaldo, S.1    Talla, E.2    Brochier-Armanet, C.3
  • 41
    • 0031942895 scopus 로고    scopus 로고
    • Animal adaptations fortolerance and exploitation of poisonous sulfide
    • Grieshaber MK, Völkel S. Animal adaptations for tolerance and exploitation of poisonous sulfide. Annu Rev Physiol 60: 33-53, 1998
    • (1998) Annu Rev Physiol , vol.60 , pp. 33-53
    • Grieshaber, M.K.1    Völkel, S.2
  • 43
    • 77955287882 scopus 로고    scopus 로고
    • Mineral surfaces, geochemicalcomplexities, and the origins of life
    • Hazen RM, Sverjensky DA. Mineral surfaces, geochemical complexities, and the origins of life. Cold Spring Harb Perspect Biol 2: a002162, 2010
    • (2010) Cold Spring Harb Perspect Biol , vol.2
    • Hazen, R.M.1    Sverjensky, D.A.2
  • 44
    • 0033551085 scopus 로고    scopus 로고
    • Noninvasive measurementof anatomic structure and intraluminal oxygenationin the gastrointestinal tract of living micewith spatial and spectral EPR imaging
    • He G, Shankar RA, Chzhan M, Samouilov A, Kuppusamy P, Zweier JL. Noninvasive measurement of anatomic structure and intraluminal oxygenation in the gastrointestinal tract of living mice with spatial and spectral EPR imaging. Proc Natl Acad Sci USA 96: 4586-4591, 1999
    • (1999) Proc Natlacad Sci USA , vol.96 , pp. 4586-4591
    • He, G.1    Shankar, R.A.2    Chzhan, M.3    Samouilov, A.4    Kuppusamy, P.5    Zweier, J.L.6
  • 45
    • 79960563168 scopus 로고    scopus 로고
    • Modulation of sulfide oxidationand toxicity in rat mitochondria by dehydroascorbicacid
    • Hildebrandt TM. Modulation of sulfide oxidation and toxicity in rat mitochondria by dehydroascorbic acid. Biochim Biophys Acta 1807: 1206-1213, 2011
    • (2011) Biochim Biophys Acta , vol.1807 , pp. 1206-1213
    • Hildebrandt, T.M.1
  • 46
    • 52649125410 scopus 로고    scopus 로고
    • Grieshaber MK. Redox regulationof mitochondrial sulfide oxidation in the lugworm,Arenicola marina
    • Hildebrandt TM, Grieshaber MK. Redox regulation of mitochondrial sulfide oxidation in the lugworm, Arenicola marina. J Exp Biol 211: 2617-2623, 2008
    • (2008) J Exp Biol , vol.211 , pp. 2617-2623
    • Hildebrandt, T.M.1
  • 47
    • 44949214775 scopus 로고    scopus 로고
    • Three enzymaticactivities catalyze the oxidation of sulfideto thiosulfate in mammalian and invertebrate mitochondria
    • Hildebrandt TM, Grieshaber MK. Three enzymatic activities catalyze the oxidation of sulfide to thiosulfate in mammalian and invertebrate mitochondria. FEBS J 275: 3352-3361, 2008
    • (2008) FEBS J , vol.275 , pp. 3352-3361
    • Hildebrandt, T.M.1    Grieshaber, M.K.2
  • 48
    • 33644824666 scopus 로고    scopus 로고
    • Biogeochemistry of dihydrogen(H2)
    • Hoehler TM. Biogeochemistry of dihydrogen (H2). Met Ions Biol Syst 43: 9-48, 2005
    • (2005) Met Ions Biol Syst , vol.43 , pp. 9-48
    • Hoehler, T.M.1
  • 50
    • 33747790905 scopus 로고    scopus 로고
    • The oxygenation of the atmosphereand oceans
    • Holland HD. The oxygenation of the atmosphere and oceans. Philos Trans R Soc Lond B Biol Sci 361: 903-915, 2006
    • (2006) Philos Trans R Soc Lond B Biol Sci , vol.361 , pp. 903-915
    • Holland, H.D.1
  • 51
    • 44449133098 scopus 로고    scopus 로고
    • Formation of Zn-and Fe-sulfidesnear hydrothermal vents at the Eastern LauSpreading Center: Implications for sulfide bioavailabilityto chemoautotrophs
    • Hsu-Kim H, Mullaugh KM, Tsang JJ, Yucel M, Luther GW, 3rd. Formation of Zn-and Fe-sulfides near hydrothermal vents at the Eastern Lau Spreading Center: implications for sulfide bioavailability to chemoautotrophs. Geochem Trans 9: 6, 2008
    • (2008) Geochem Trans , vol.9
    • Hsu-Kim, H.1    Mullaugh, K.M.2    Tsang, J.J.3    Yucel, M.4    Luther, G.W.5
  • 53
    • 33646772901 scopus 로고    scopus 로고
    • The nutritional relationship linkingsulfur to nitrogen in living organisms
    • Ingenbleek Y. The nutritional relationship linking sulfur to nitrogen in living organisms. J Nutr 136: 1641S-1651S, 2006
    • (2006) J Nutr , vol.136 , pp. 1641S-1651S
    • Ingenbleek, Y.1
  • 54
    • 84879839976 scopus 로고    scopus 로고
    • Nutritional essentialityof sulfur in health and disease
    • Ingenbleek Y, Kimura H. Nutritional essentiality of sulfur in health and disease. Nutr Rev 71: 413-432, 2013
    • (2013) Nutr Rev , vol.71 , pp. 413-432
    • Ingenbleek, Y.1    Kimura, H.2
  • 55
    • 11144334622 scopus 로고    scopus 로고
    • Strategies adopted bythe mudskipper Boleophthalmus boddaerti tosurvive sulfide exposure in normoxia or hypoxia
    • Ip YK, Kuah SS, Chew SF. Strategies adopted by the mudskipper Boleophthalmus boddaerti to survive sulfide exposure in normoxia or hypoxia. Physiol Biochem Zool 77: 824-837, 2004
    • (2004) Physiol Biochem Zool , vol.77 , pp. 824-837
    • Ip, Y.K.1    Kuah, S.S.2    Chew, S.F.3
  • 56
    • 84867522886 scopus 로고    scopus 로고
    • Human sulfide:Quinone oxidoreductase catalyzes the firststep in hydrogen sulfide metabolism and producesa sulfane sulfur metabolite
    • Jackson MR, Melideo SL, Jorns MS. Human sulfide: quinone oxidoreductase catalyzes the first step in hydrogen sulfide metabolism and produces a sulfane sulfur metabolite. Biochemistry 51: 6804-6815, 2012
    • (2012) Biochemistry , vol.51 , pp. 6804-6815
    • Jackson, M.R.1    Melideo, S.L.2    Jorns, M.S.3
  • 57
    • 77956049607 scopus 로고    scopus 로고
    • Elucidatingthe catalytic mechanism of sulfite oxidizingenzymes using structural, spectroscopic, andkinetic analyses
    • Johnson-Winters K, Tollin G, Enemark JH. Elucidating the catalytic mechanism of sulfite oxidizing enzymes using structural, spectroscopic, and kinetic analyses. Biochemistry 49: 7242-7254, 2010
    • (2010) Biochemistry , vol.49 , pp. 7242-7254
    • Johnson-Winters, K.1    Tollin, G.2    Enemark, J.H.3
  • 58
    • 79959530805 scopus 로고    scopus 로고
    • The quantitativesignificance of the transsulfuration enzymesfor H2S production in murine tissues
    • Kabil O, Vitvitsky V, Xie P, Banerjee R. The quantitative significance of the transsulfuration enzymes for H2S production in murine tissues. Antioxid Redox Signal 15: 363-372, 2011
    • (2011) Antioxid Redox Signal , vol.15 , pp. 363-372
    • Kabil, O.1    Vitvitsky, V.2    Xie, P.3    Banerjee, R.4
  • 59
    • 3042651344 scopus 로고    scopus 로고
    • Endogenous production of hydrogensulfide in mammals
    • Kamoun P. Endogenous production of hydrogen sulfide in mammals. Amino Acids 26: 243-254, 2004
    • (2004) Amino Acids , vol.26 , pp. 243-254
    • Kamoun, P.1
  • 60
    • 0037998250 scopus 로고    scopus 로고
    • Formation of carbonyl sulfide by the reaction ofcarbon monoxide and inorganic polysulfides
    • Kamyshny A Jr, Goifman A, Rizkov D, Lev O. Formation of carbonyl sulfide by the reaction of carbon monoxide and inorganic polysulfides. Environ Sci Technol 37: 1865-1872, 2003
    • (2003) Environsci Technol , vol.37 , pp. 1865-1872
    • Kamyshny, A.1    Goifman, A.2    Rizkov, D.3    Lev, O.4
  • 61
    • 0027914959 scopus 로고
    • Earth’s early atmosphere
    • Kasting JF. Earth’s early atmosphere. Science 259: 920-926, 1993
    • (1993) Science , vol.259 , pp. 920-926
    • Kasting, J.F.1
  • 63
    • 0028184401 scopus 로고
    • Formation of amide bonds without a condensationagent and implications for origin oflife
    • Keller M, Blochl E, Wachtershauser G, Stetter KO. Formation of amide bonds without a condensation agent and implications for origin of life. Nature 368: 836-838, 1994
    • (1994) Nature , vol.368 , pp. 836-838
    • Keller, M.1    Blochl, E.2    Wachtershauser, G.3    Stetter, K.O.4
  • 64
    • 0036436134 scopus 로고    scopus 로고
    • Volcanoes, fluids,and life at mid-ocean ridge spreading centers
    • Kelly DS, Baross JA, Delaney JR. Volcanoes, fluids, and life at mid-ocean ridge spreading centers. Annu Rev Earth Planet Sci 30: 385-489, 2002
    • (2002) Annu Rev Earth Planet Sci , vol.30 , pp. 385-489
    • Kelly, D.S.1    Baross, J.A.2    Delaney, J.R.3
  • 66
    • 84911880650 scopus 로고    scopus 로고
    • Hydrogen sulfide and polysulfides asbiological mediators
    • Kimura H. Hydrogen sulfide and polysulfides as biological mediators. Molecules 19: 16146-16157, 2014
    • (2014) Molecules , vol.19 , pp. 16146-16157
    • Kimura, H.1
  • 67
    • 84921904030 scopus 로고    scopus 로고
    • Signaling molecules: Hydrogen sulfideand polysulfide
    • Kimura H. Signaling molecules: hydrogen sulfide and polysulfide. Antioxid Redox Signal 22: 362-376, 2015
    • (2015) Antioxid Redox Signal , vol.22 , pp. 362-376
    • Kimura, H.1
  • 68
    • 84921910957 scopus 로고    scopus 로고
    • Signaling of hydrogen sulfide andpolysulfides
    • Kimura H. Signaling of hydrogen sulfide and polysulfides. Antioxid Redox Signal 22: 347-349, 2015
    • (2015) Antioxid Redox Signal , vol.22 , pp. 347-349
    • Kimura, H.1
  • 69
    • 84878764595 scopus 로고    scopus 로고
    • Polysulfides are possible H2S-derivedsignaling molecules in rat brain
    • Kimura Y, Mikami Y, Osumi K, Tsugane M, Oka JI, Kimura H. Polysulfides are possible H2S-derived signaling molecules in rat brain. FASEB J 27: 2451-2457, 2013
    • (2013) FASEB J , vol.27 , pp. 2451-2457
    • Kimura, Y.1    Mikami, Y.2    Osumi, K.3    Tsugane, M.4    Oka, J.I.5    Kimura, H.6
  • 71
    • 38349105591 scopus 로고    scopus 로고
    • The rise of atmospheric oxygen
    • Kump LR. The rise of atmospheric oxygen. Nature 451: 277-278, 2008
    • (2008) Nature , vol.451 , pp. 277-278
    • Kump, L.R.1
  • 72
    • 0034443285 scopus 로고    scopus 로고
    • Origin and evolutionof the mitochondrial proteome
    • Kurland CG, Andersson SG. Origin and evolution of the mitochondrial proteome. Microbiol Mol Biol Rev 64: 786-820, 2000
    • (2000) Microbiol Molbiol Rev , vol.64 , pp. 786-820
    • Kurland, C.G.1    Ersson, S.G.2
  • 73
    • 77955672171 scopus 로고    scopus 로고
    • Oxidation ofhydrogen sulfide remains a priority in mammaliancells and causes reverse electron transfer incolonocytes
    • Lagoutte E, Mimoun S, Andriamihaja M, Chaumontet C, Blachier F, Bouillaud F. Oxidation of hydrogen sulfide remains a priority in mammalian cells and causes reverse electron transfer in colonocytes. Biochim Biophys Acta 1797: 1500-1511, 2010
    • (2010) Biochim Biophys Acta , vol.1797 , pp. 1500-1511
    • Lagoutte, E.1    Mimoun, S.2    Riamihaja, M.3    Chaumontet, C.4    Blachier, F.5    Bouillaud, F.6
  • 75
    • 84881513267 scopus 로고    scopus 로고
    • Chemical foundations ofhydrogen sulfide biology
    • Li Q, Lancaster JR Jr. Chemical foundations of hydrogen sulfide biology. Nitric Oxide 35: 21-34, 2013
    • (2013) Nitric Oxide , vol.35 , pp. 21-34
    • Li, Q.1    Lancaster, J.R.2
  • 76
    • 84908391944 scopus 로고    scopus 로고
    • Organization of the human mitochondrialhydrogen sulfide oxidation pathway
    • Libiad M, Yadav PK, Vitvitsky V, Martinov M, Banerjee R. Organization of the human mitochondrial hydrogen sulfide oxidation pathway. J Biol Chem 289: 30901-30910, 2014
    • (2014) Jbiol Chem , vol.289 , pp. 30901-30910
    • Libiad, M.1    Yadav, P.K.2    Vitvitsky, V.3    Martinov, M.4    Banerjee, R.5
  • 77
    • 84930667997 scopus 로고    scopus 로고
    • Chemicalprobes for molecular imaging and detection ofhydrogen sulfide and reactive sulfur species inbiological systems
    • Lin VS, Chen W, Xian M, Chang CJ. Chemical probes for molecular imaging and detection of hydrogen sulfide and reactive sulfur species in biological systems. Chem Soc Rev 44: 4596-4618, 2015
    • (2015) Chem Soc Rev , vol.44 , pp. 4596-4618
    • Lin, V.S.1    Chen, W.2    Xian, M.3    Chang, C.J.4
  • 78
    • 84885466734 scopus 로고    scopus 로고
    • Hydrogen sulfide signaling in the gastrointestinaltract
    • Linden DR. Hydrogen sulfide signaling in the gastrointestinal tract. Antioxid Redox Signal 20: 818-830, 2014
    • (2014) Antioxid Redox Signal , vol.20 , pp. 818-830
    • Linden, D.R.1
  • 79
    • 84894261996 scopus 로고    scopus 로고
    • The rise ofoxygen in Earth’s early ocean and atmosphere
    • Lyons TW, Reinhard CT, Planavsky NJ. The rise of oxygen in Earth’s early ocean and atmosphere. Nature 506: 307-315, 2014
    • (2014) Nature , vol.506 , pp. 307-315
    • Lyons, T.W.1    Reinhard, C.T.2    Planavsky, N.J.3
  • 80
    • 77951225834 scopus 로고    scopus 로고
    • A newstructure-based classification of sulfide:Quinoneoxidoreductases
    • Marcia M, Ermler U, Peng G, Michel H. A new structure-based classification of sulfide:quinone oxidoreductases. Proteins 78: 1073-1083, 2010
    • (2010) Proteins , vol.78 , pp. 1073-1083
    • Marcia, M.1    Ermler, U.2    Peng, G.3    Michel, H.4
  • 81
    • 0030035039 scopus 로고    scopus 로고
    • Archaeal-eubacterial mergers in theorigin of Eukarya: Phylogenetic classification oflife
    • Margulis L. Archaeal-eubacterial mergers in the origin of Eukarya: phylogenetic classification of life. Proc Natl Acad Sci USA 93: 1071-1076, 1996
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1071-1076
    • Margulis, L.1
  • 83
    • 35148861695 scopus 로고    scopus 로고
    • On the origin of biochemistryat an alkaline hydrothermal vent
    • Martin W, Russell MJ. On the origin of biochemistry at an alkaline hydrothermal vent. Philos Trans R Soc Lond B Biol Sci 362: 1887-1925, 2007
    • (2007) Philostrans R Soc Lond B Biol Sci , vol.362 , pp. 1887-1925
    • Martin, W.1    Russell, M.J.2
  • 84
    • 0037471691 scopus 로고    scopus 로고
    • On the origins of cells: Ahypothesis for the evolutionary transitions fromabiotic geochemistry to chemoautotrophic prokaryotes,and from prokaryotes to nucleatedcells
    • Martin W, Russell MJ. On the origins of cells: a hypothesis for the evolutionary transitions from abiotic geochemistry to chemoautotrophic prokaryotes, and from prokaryotes to nucleated cells. Philos Trans R Soc Lond B Biol Sci 358: 59-83, 2003
    • (2003) Philos Trans R Soc Lond B Biol Sci , vol.358 , pp. 59-83
    • Martin, W.1    Russell, M.J.2
  • 85
    • 79959647506 scopus 로고    scopus 로고
    • Early evolution without a tree of life
    • Martin WF. Early evolution without a tree of life. Biol Direct 6: 36, 2011
    • (2011) Biol Direct , vol.6
    • Martin, W.F.1
  • 86
    • 84857143067 scopus 로고    scopus 로고
    • Hydrogen, metals, bifurcating electrons,and proton gradients: The early evolutionof biological energy conservation
    • Martin WF. Hydrogen, metals, bifurcating electrons, and proton gradients: the early evolution of biological energy conservation. FEBS Lett 586: 485-493, 2012
    • (2012) FEBS Lett , vol.586 , pp. 485-493
    • Martin, W.F.1
  • 87
    • 84901832887 scopus 로고    scopus 로고
    • Evolution. Energyat life’s origin
    • Martin WF, Sousa FL, Lane N. Evolution. Energy at life’s origin. Science 344: 1092-1093, 2014
    • (2014) Science , vol.344 , pp. 1092-1093
    • Martin, W.F.1    Sousa, F.L.2    Lane, N.3
  • 89
    • 84861920985 scopus 로고    scopus 로고
    • Peptide andRNA contributions to iron-sulphur chemical gardensas life’s first inorganic compartments, catalysts,capacitors and condensers
    • McGlynn SE, Kanik I, Russell MJ. Peptide and RNA contributions to iron-sulphur chemical gardens as life’s first inorganic compartments, catalysts, capacitors and condensers. Philos Trans A Math Phys Eng Sci 370: 3007-3022, 2012
    • (2012) Philos Trans Amath Phys Eng Sci , vol.370 , pp. 3007-3022
    • McGlynn, S.E.1    Kanik, I.2    Russell, M.J.3
  • 90
    • 84904668283 scopus 로고    scopus 로고
    • Biosynthesisof a central intermediate in hydrogen sulfide metabolismby a novel human sulfurtransferase andits yeast ortholog
    • Melideo SL, Jackson MR, Jorns MS. Biosynthesis of a central intermediate in hydrogen sulfide metabolism by a novel human sulfurtransferase and its yeast ortholog. Biochemistry 53: 4739-4753, 2014
    • (2014) Biochemistry , vol.53 , pp. 4739-4753
    • Melideo, S.L.1    Jackson, M.R.2    Jorns, M.S.3
  • 91
    • 77952253378 scopus 로고    scopus 로고
    • Anaerobic animals from anancient, anoxic ecological niche
    • Mentel M, Martin W. Anaerobic animals from an ancient, anoxic ecological niche. BMC Biol 8: 32, 2010
    • (2010) BMC Biol , vol.8
    • Mentel, M.1    Martin, W.2
  • 94
    • 80054015725 scopus 로고    scopus 로고
    • Thioredoxin and dihydrolipoicacid are required for 3-mercaptopyruvatesulfurtransferase to produce hydrogensulfide
    • Mikami Y, Shibuya N, Kimura Y, Nagahara N, Ogasawara Y, Kimura H. Thioredoxin and dihydrolipoic acid are required for 3-mercaptopyruvate sulfurtransferase to produce hydrogen sulfide. Biochem J 439: 479-485, 2011
    • (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
  • 97
    • 80053338536 scopus 로고    scopus 로고
    • HIF-1 and SKN-1coordinate the transcriptional response to hydrogensulfide in Caenorhabditis elegans
    • Miller DL, Budde MW, Roth MB. HIF-1 and SKN-1 coordinate the transcriptional response to hydrogen sulfide in Caenorhabditis elegans. PLos One 6: e25476, 2011
    • (2011) Plos One , vol.6
    • Miller, D.L.1    Budde, M.W.2    Roth, M.B.3
  • 98
    • 37049243502 scopus 로고
    • A production of amino acids underpossible primitive earth conditions
    • Miller SL. A production of amino acids under possible primitive earth conditions. Science 117: 528-529, 1953
    • (1953) Science , vol.117 , pp. 528-529
    • Miller, S.L.1
  • 99
    • 84934905709 scopus 로고    scopus 로고
    • Biogenesisof reactive sulfur species for signaling by hydrogensulfide oxidation pathways
    • Mishanina TV, Libiad M, Banerjee R. Biogenesis of reactive sulfur species for signaling by hydrogen sulfide oxidation pathways. Nat Chem Biol 11: 457-464, 2015
    • (2015) Nat Chem Biol , vol.11 , pp. 457-464
    • Mishanina, T.V.1    Libiad, M.2    Banerjee, R.3
  • 100
    • 84876470345 scopus 로고    scopus 로고
    • Oxidative stress suppressesthe cellular bioenergetic effect of the3-mercaptopyruvate sulfurtransferase/hydrogensulfide pathway
    • Modis K, Asimakopoulou A, Coletta C, Papapetropoulos A, Szabo C. Oxidative stress suppresses the cellular bioenergetic effect of the 3-mercaptopyruvate sulfurtransferase/hydrogen sulfide pathway. Biochem Biophys Res Commun 433: 401-407, 2013
    • (2013) Biochem Biophys Res Commun , vol.433 , pp. 401-407
    • Modis, K.1    Asimakopoulou, A.2    Coletta, C.3    Papapetropoulos, A.4    Szabo, C.5
  • 102
    • 84873467050 scopus 로고    scopus 로고
    • Intramitochondrial hydrogen sulfideproduction by 3-mercaptopyruvate sulfurtransferasemaintains mitochondrial electron flow andsupports cellular bioenergetics
    • Modis K, Coletta C, Erdelyi K, Papapetropoulos A, Szabo C. Intramitochondrial hydrogen sulfide production by 3-mercaptopyruvate sulfurtransferase maintains mitochondrial electron flow and supports cellular bioenergetics. FASEB J 27: 601-611, 2013
    • (2013) FASEB J , vol.27 , pp. 601-611
    • Modis, K.1    Coletta, C.2    Erdelyi, K.3    Papapetropoulos, A.4    Szabo, C.5
  • 103
    • 84886728728 scopus 로고    scopus 로고
    • Hydrogen sulfide-mediatedstimulation of mitochondrial electron transportinvolves inhibition of the mitochondrial phosphodiesterase2A, elevation of cAMP and activationof protein kinase A
    • Modis K, Panopoulos P, Coletta C, Papapetropoulos A, Szabo C. 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 86: 1311-1319, 2013
    • (2013) Biochem Pharmacol , vol.86 , pp. 1311-1319
    • Modis, K.1    Panopoulos, P.2    Coletta, C.3    Papapetropoulos, A.4    Szabo, C.5
  • 104
    • 78049446734 scopus 로고    scopus 로고
    • Ligand fieldtheory and the origin of life as an emergent featureof the periodic table of elements
    • Morowitz HJ, Srinivasan V, Smith E. Ligand field theory and the origin of life as an emergent feature of the periodic table of elements. Biol Bull 219: 1-6, 2010
    • (2010) Biol Bull , vol.219 , pp. 1-6
    • Morowitz, H.J.1    Srinivasan, V.2    Smith, E.3
  • 105
    • 33646349748 scopus 로고    scopus 로고
    • Trafficking in persulfides: Deliveringsulfur in biosynthetic pathways
    • Mueller EG. Trafficking in persulfides: delivering sulfur in biosynthetic pathways. Nat Chem Biol 2: 185-194, 2006
    • (2006) Nat Chem Biol , vol.2 , pp. 185-194
    • Mueller, E.G.1
  • 107
    • 0031666759 scopus 로고    scopus 로고
    • Tissueand subcellular distribution of mercaptopyruvatesulfurtransferase in the rat: Confocal laser fluorescenceand immunoelectron microscopic studiescombined with biochemical analysis
    • Nagahara N, Ito T, Kitamura H, Nishino T. Tissue and subcellular distribution of mercaptopyruvate sulfurtransferase in the rat: confocal laser fluorescence and immunoelectron microscopic studies combined with biochemical analysis. Histochem Cell Biol 110: 243-250, 1998
    • (1998) Histochemcell Biol , vol.110 , pp. 243-250
    • Nagahara, N.1    Ito, T.2    Kitamura, H.3    Nishino, T.4
  • 108
    • 27144442871 scopus 로고    scopus 로고
    • Post-translational regulationof mercaptopyruvate sulfurtransferase viaa low redox potential cysteine-sulfenate in themaintenance of redox homeostasis
    • Nagahara N, Katayama A. 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
    • (2005) J Biol Chem , vol.280 , pp. 34569-34576
    • Nagahara, N.1    Katayama, A.2
  • 109
    • 33847335589 scopus 로고    scopus 로고
    • Thioredoxin-dependent enzymatic activation ofmercaptopyruvate sulfurtransferase. An intersubunitdisulfide bond serves as a redox switchfor activation
    • Nagahara N, Yoshii T, Abe Y, Matsumura T. Thioredoxin-dependent enzymatic activation of mercaptopyruvate sulfurtransferase. An intersubunit disulfide bond serves as a redox switch for activation. J Biol Chem 282: 1561-1569, 2007
    • (2007) J Biol Chem , vol.282 , pp. 1561-1569
    • Nagahara, N.1    Yoshii, T.2    Abe, Y.3    Matsumura, T.4
  • 110
    • 84923586690 scopus 로고    scopus 로고
    • Mechanistic chemical perspective of hydrogensulfide signaling
    • Nagy P. Mechanistic chemical perspective of hydrogen sulfide signaling. Methods Enzymol 554: 3-29, 2015
    • (2015) Methods Enzymol , vol.554 , pp. 3-29
    • Nagy, P.1
  • 114
    • 72449155029 scopus 로고    scopus 로고
    • Hydrothermal focusingof chemical and chemiosmotic energy, supportedby delivery of catalytic Fe, Ni, Mo/W, Co,S and Se, forced life to emerge
    • Nitschke W, Russell MJ. Hydrothermal focusing of chemical and chemiosmotic energy, supported by delivery of catalytic Fe, Ni, Mo/W, Co, S and Se, forced life to emerge. J Mol Evol 69: 481-496, 2009
    • (2009) J Mol Evol , vol.69 , pp. 481-496
    • Nitschke, W.1    Russell, M.J.2
  • 115
    • 84555179630 scopus 로고    scopus 로고
    • Redox bifurcations:Mechanisms and importance to life now, and atits origin: A widespread means of energy conversionin biology unfolds
    • Nitschke W, Russell MJ. Redox bifurcations: mechanisms and importance to life now, and at its origin: a widespread means of energy conversion in biology unfolds. Bioessays 34: 106-109, 2012
    • (2012) Bioessays , vol.34 , pp. 106-109
    • Nitschke, W.1    Russell, M.J.2
  • 116
    • 84882392351 scopus 로고    scopus 로고
    • Reactivity landscape ofpyruvate under simulated hydrothermal ventconditions
    • Novikov Y, Copley SD. Reactivity landscape of pyruvate under simulated hydrothermal vent conditions. Proc Natl Acad Sci USA 110: 13283-13288, 2013
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 13283-13288
    • Novikov, Y.1    Copley, S.D.2
  • 117
    • 84921915828 scopus 로고    scopus 로고
    • Hydrogen sulfide as an oxygen sensor
    • Olson KR. Hydrogen sulfide as an oxygen sensor. Antioxid Redox Signal 22: 377-397, 2015
    • (2015) Antioxid Redox Signal , vol.22 , pp. 377-397
    • Olson, K.R.1
  • 118
    • 84875249385 scopus 로고    scopus 로고
    • A theoretical examination of hydrogensulfide metabolism and its potential in autocrine/paracrine oxygen sensing
    • Olson KR. A theoretical examination of hydrogen sulfide metabolism and its potential in autocrine/ paracrine oxygen sensing. Respir Physiol Neurobiol 186: 173-179, 2013
    • (2013) Respir Physiol Neurobiol , vol.186 , pp. 173-179
    • Olson, K.R.1
  • 119
    • 17644375486 scopus 로고    scopus 로고
    • Vascular actions of hydrogen sulfide innon-mammalian vertebrates
    • Olson KR. Vascular actions of hydrogen sulfide in non-mammalian vertebrates. Antioxid Redox Signal 7: 804-812, 2005
    • (2005) Antioxid Redox Signal , vol.7 , pp. 804-812
    • Olson, K.R.1
  • 121
    • 84905247104 scopus 로고    scopus 로고
    • Controversies andconundrums in hydrogen sulfide biology
    • Olson KR, DeLeon ER, Liu F. Controversies and conundrums in hydrogen sulfide biology. Nitric Oxide 41: 11-26, 2014
    • (2014) Nitricoxide , vol.41 , pp. 11-26
    • Olson, K.R.1    Deleon, E.R.2    Liu, F.3
  • 123
    • 84887430297 scopus 로고    scopus 로고
    • Chlorosome antennacomplexes from green photosynthetic bacteria
    • Orf GS, Blankenship RE. Chlorosome antenna complexes from green photosynthetic bacteria. Photosynth Res 116: 315-331, 2013
    • (2013) Photosynth Res , vol.116 , pp. 315-331
    • Orf, G.S.1    Blankenship, R.E.2
  • 125
    • 84934892111 scopus 로고    scopus 로고
    • Persulfides: Current knowledge and challengesin chemistry and chemical biology
    • Park CM, Weerasinghe L, Day JJ, Fukuto JM, Xian M. Persulfides: current knowledge and challenges in chemistry and chemical biology. Mol Biosyst 11: 1775-1785, 2015
    • (2015) Molbiosyst , vol.11 , pp. 1775-1785
    • Park, C.M.1    Weerasinghe, L.2    Day, J.J.3    Fukuto, J.M.4    Xian, M.5
  • 126
    • 79956061759 scopus 로고    scopus 로고
    • Prebiotic synthesisof methionine and other sulfur-containing organiccompounds on the primitive Earth: Acontemporary reassessment based on an unpublished1958 Stanley Miller experiment
    • Parker ET, Cleaves HJ, Callahan MP, Dworkin JP, Glavin DP, Lazcano A, Bada JL. Prebiotic synthesis of methionine and other sulfur-containing organic compounds on the primitive Earth: a contemporary reassessment based on an unpublished 1958 Stanley Miller experiment. Orig Life Evol Biosph 41: 201-212, 2011
    • (2011) Orig Lifeevol Biosph , vol.41 , pp. 201-212
    • Parker, E.T.1    Cleaves, H.J.2    Callahan, M.P.3    Dworkin, J.P.4    Glavin, D.P.5    Lazcano, A.6    Bada, J.L.7
  • 128
    • 0033867969 scopus 로고    scopus 로고
    • ATP productionfrom the oxidation of sulfide in gill mitochondriaof the ribbed mussel Geukensia demissa
    • Parrino V, Kraus DW, Doeller JE. ATP production from the oxidation of sulfide in gill mitochondria of the ribbed mussel Geukensia demissa. J Exp Biol 203: 2209-2218, 2000
    • (2000) J Expbiol , vol.203 , pp. 2209-2218
    • Parrino, V.1    Kraus, D.W.2    Doeller, J.E.3
  • 129
    • 0017353388 scopus 로고
    • The effect of inhibitors on theoxygenkinetics of cytochrome c oxidase
    • Petersen CL. The effect of inhibitors on theoxygen kinetics of cytochrome c oxidase. Biochim Biophys Acta 460: 299-307, 1977
    • (1977) Biochimbiophys Acta , vol.460 , pp. 299-307
    • Petersen, C.L.1
  • 130
    • 33646471591 scopus 로고    scopus 로고
    • The chemistry of life’s origin: A carbonaceousmeteorite perspective
    • Pizzarello S. The chemistry of life’s origin: a carbonaceous meteorite perspective. Acc Chem Res 39: 231-237, 2006
    • (2006) Acc Chem Res , vol.39 , pp. 231-237
    • Pizzarello, S.1
  • 131
    • 77957283679 scopus 로고    scopus 로고
    • The organic composition ofcarbonaceous meteorites: The evolutionary storyahead of biochemistry
    • Pizzarello S, Shock E. The organic composition of carbonaceous meteorites: the evolutionary story ahead of biochemistry. Cold Spring Harb Perspect Biol 2: a002105, 2010
    • (2010) Cold Spring Harb Perspectbiol , vol.2
    • Pizzarello, S.1    Shock, E.2
  • 133
    • 84924594298 scopus 로고    scopus 로고
    • Thecardioprotective actions of hydrogen sulfide inacute myocardial infarction and heart failure
    • Polhemus DJ, Calvert JW, Butler J, Lefer DJ. The cardioprotective actions of hydrogen sulfide in acute myocardial infarction and heart failure. Scientifica (Cairo) 2014: 768607, 2014
    • (2014) Scientifica(Cairo) , vol.2014
    • Polhemus, D.J.1    Calvert, J.W.2    Butler, J.3    Lefer, D.J.4
  • 134
    • 84906267368 scopus 로고    scopus 로고
    • Stable sulfur andoxygen isotope fractionation of anoxic sulfideoxidation by two different enzymatic pathways
    • Poser A, Vogt C, Knoller K, Ahlheim J, Weiss H, Kleinsteuber S, Richnow HH. Stable sulfur and oxygen isotope fractionation of anoxic sulfide oxidation by two different enzymatic pathways. Environ Sci Technol 48: 9094-9102, 2014
    • (2014) Environ Sci Technol , vol.48 , pp. 9094-9102
    • Poser, A.1    Vogt, C.2    Knoller, K.3    Ahlheim, J.4    Weiss, H.5    Kleinsteuber, S.6    Richnow, H.H.7
  • 135
    • 0022554531 scopus 로고
    • Hydrogen sulfide oxidationis coupled to oxidative phosphorylation inmitochondria of Solemya reidi
    • Powell MA, Somero GN. Hydrogen sulfide oxidation is coupled to oxidative phosphorylation in mitochondria of Solemya reidi. Science 233: 563-566, 1986
    • (1986) Science , vol.233 , pp. 563-566
    • Powell, M.A.1    Somero, G.N.2
  • 136
    • 79960547649 scopus 로고    scopus 로고
    • Prebiological evolution and the metabolicorigins of life
    • Pratt AJ. Prebiological evolution and the metabolic origins of life. Artif Life 17: 203-217, 2011
    • (2011) Artif Life , vol.17 , pp. 203-217
    • Pratt, A.J.1
  • 137
    • 34047274576 scopus 로고    scopus 로고
    • Lipid domain boundaries asprebiotic catalysts of peptide bond formation
    • Raine DJ, Norris V. Lipid domain boundaries as prebiotic catalysts of peptide bond formation. J Theor Biol 246: 176-185, 2007
    • (2007) Jtheor Biol , vol.246 , pp. 176-185
    • Raine, D.J.1    Norris, V.2
  • 138
    • 84900487381 scopus 로고    scopus 로고
    • The iron biogeochemicalcycle past and present
    • Raiswell R, Canfield DE. The iron biogeochemical cycle past and present. Geochem Perspect 1: 1-220, 2012
    • (2012) Geochem Perspect , vol.1 , pp. 1-220
    • Raiswell, R.1    Canfield, D.E.2
  • 139
    • 38049009377 scopus 로고    scopus 로고
    • The origin of theoxygen-evolving complex
    • Raymond J, Blankenship RE. The origin of the oxygen-evolving complex. Coord Chem Rev 252: 377-383, 2008
    • (2008) Coord Chem Rev , vol.252 , pp. 377-383
    • Raymond, J.1    Blankenship, R.E.2
  • 140
    • 33847763196 scopus 로고    scopus 로고
    • Chemistry of iron sulfides
    • Rickard D, Luther GW 3rd Chemistry of iron sulfides. Chem Rev 107: 514-562, 2007
    • (2007) Chem Rev , vol.107 , pp. 514-562
    • Rickard, D.1    Luther, G.W.2
  • 141
    • 84858437435 scopus 로고    scopus 로고
    • On the evolutionaryecology of symbioses between chemosyntheticbacteria and bivalves
    • Roeselers G, Newton IL. On the evolutionary ecology of symbioses between chemosynthetic bacteria and bivalves. Appl Microbiol Biotechnol 94: 1-10, 2012
    • (2012) Appl Microbiol Biotechnol , vol.94 , pp. 1-10
    • Roeselers, G.1    Newton, I.L.2
  • 142
    • 36549077770 scopus 로고    scopus 로고
    • The alkaline solution to the emergenceof life: Energy, entropy and early evolution
    • Russell MJ. The alkaline solution to the emergence of life: energy, entropy and early evolution. Acta Biotheor 55: 133-179, 2007
    • (2007) Acta Biotheor , vol.55 , pp. 133-179
    • Russell, M.J.1
  • 144
    • 0030875872 scopus 로고    scopus 로고
    • The emergence of life fromiron monosulphide bubbles at a submarine hydrothermalredox and pH front
    • Russell MJ, Hall AJ. The emergence of life from iron monosulphide bubbles at a submarine hydrothermal redox and pH front. J Geol Soc London 154: 377-402, 1997
    • (1997) J Geol Soc London , vol.154 , pp. 377-402
    • Russell, M.J.1    Hall, A.J.2
  • 145
    • 78349292586 scopus 로고    scopus 로고
    • Serpentinization asa source of energy at the origin of life
    • Russell MJ, Hall AJ, Martin W. Serpentinization as a source of energy at the origin of life. Geobiology 8: 355-371, 2010
    • (2010) Geobiology , vol.8 , pp. 355-371
    • Russell, M.J.1    Hall, A.J.2    Martin, W.3
  • 147
    • 0000565510 scopus 로고
    • Long-wavelength ultravioletphotoproduction of amino acids on the primitiveEarth
    • Sagan C, Khare BN. Long-wavelength ultraviolet photoproduction of amino acids on the primitive Earth. Science 173: 417-420, 1971
    • (1971) Science , vol.173 , pp. 417-420
    • Sagan, C.1    Khare, B.N.2
  • 148
    • 77953651658 scopus 로고    scopus 로고
    • Inorganicsulfur oxidizing system in green sulfur bacteria
    • Sakurai H, Ogawa T, Shiga M, Inoue K. Inorganic sulfur oxidizing system in green sulfur bacteria. Photosynth Res 104: 163-176, 2010
    • (2010) Photosynth Res , vol.104 , pp. 163-176
    • Sakurai, H.1    Ogawa, T.2    Shiga, M.3    Inoue, K.4
  • 149
    • 84896983974 scopus 로고    scopus 로고
    • Geological evidence of oxygenicphotosynthesis and the biotic response to the2400-2200 ma “great oxidation event”
    • Schopf JW. Geological evidence of oxygenic photosynthesis and the biotic response to the 2400-2200 ma “great oxidation event”. Biochemistry (Mosc) 79: 165-177, 2014
    • (2014) Biochemistry(Mosc) , vol.79 , pp. 165-177
    • Schopf, J.W.1
  • 151
    • 1542572798 scopus 로고    scopus 로고
    • Metabolic integration during the evolutionaryorigin of mitochondria
    • Searcy DG. Metabolic integration during the evolutionary origin of mitochondria. Cell Res 13: 229-238, 2003
    • (2003) Cell Res , vol.13 , pp. 229-238
    • Searcy, D.G.1
  • 159
    • 3142729014 scopus 로고    scopus 로고
    • Sulfur amino acid metabolism:Pathways for production and removal of homocysteineand cysteine
    • Stipanuk MH. Sulfur amino acid metabolism: pathways for production and removal of homocysteine and cysteine. Annu Rev Nutr 24: 539-577, 2004
    • (2004) Annu Rev Nutr , vol.24 , pp. 539-577
    • Stipanuk, M.H.1
  • 160
    • 79953715220 scopus 로고    scopus 로고
    • Dealing with methionine/homocysteine sulfur: Cysteine metabolism to taurineand inorganic sulfur
    • Stipanuk MH, Ueki I. Dealing with methionine/ homocysteine sulfur: cysteine metabolism to taurine and inorganic sulfur. J Inherit Metab Dis 34: 17-32, 2011
    • (2011) J Inherit Metab Dis , vol.34 , pp. 17-32
    • Stipanuk, M.H.1    Ueki, I.2
  • 162
    • 26844461420 scopus 로고    scopus 로고
    • Ammonia formation by the reductionof nitrite/nitrate by FeS: Ammonia formationunder acidic conditions
    • Summers DP. Ammonia formation by the reduction of nitrite/nitrate by FeS: ammonia formation under acidic conditions. Orig Life Evol Biosph 35: 299-312, 2005
    • (2005) Orig Life Evol Biosph , vol.35 , pp. 299-312
    • Summers, D.P.1
  • 163
  • 164
    • 84907598666 scopus 로고    scopus 로고
    • AP39,a novel mitochondria-targeted hydrogen sulfidedonor, stimulates cellular bioenergetics, exertscytoprotective effects and protects against theloss of mitochondrial DNA integrity in oxidativelystressed endothelial cells in vitro
    • Szczesny B, Modis K, Yanagi K, Coletta C, Le TS, Perry A, Wood ME, Whiteman M, Szabo C. AP39, a novel mitochondria-targeted hydrogen sulfide donor, stimulates cellular bioenergetics, exerts cytoprotective effects and protects against the loss of mitochondrial DNA integrity in oxidatively stressed endothelial cells in vitro. Nitric Oxide 41: 120-130, 2014
    • (2014) Nitric Oxide , vol.41 , pp. 120-130
    • Szczesny, B.1    Modis, K.2    Yanagi, K.3    Coletta, C.4    Le, T.S.5    Perry, A.6    Wood, M.E.7    Whiteman, M.8    Szabo, C.9
  • 165
    • 78449299224 scopus 로고    scopus 로고
    • Mosaic origin of themitochondrial proteome
    • Szklarczyk R, Huynen MA. Mosaic origin of the mitochondrial proteome. Proteomics 10: 4012-4024, 2010
    • (2010) Proteomics , vol.10 , pp. 4012-4024
    • Szklarczyk, R.1    Huynen, M.A.2
  • 166
    • 84881101982 scopus 로고    scopus 로고
    • Oxygen-sensitive mitochondrial accumulation ofcystathionine beta-synthase mediated by Lonprotease
    • Teng H, Wu B, Zhao K, Yang G, Wu L, Wang R. Oxygen-sensitive mitochondrial accumulation of cystathionine beta-synthase mediated by Lon protease. Proc Natl Acad Sci USA 110: 12679-12684, 2013
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 12679-12684
    • Teng, H.1    Wu, B.2    Zhao, K.3    Yang, G.4    Wu, L.5    Wang, R.6
  • 167
    • 0037787922 scopus 로고    scopus 로고
    • Single eubacterial origin of eukaryotic sulfide:Quinone oxidoreductase, a mitochondrial enzymeconserved from the early evolution ofeukaryotes during anoxic and sulfidic times
    • 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 20: 1564-1574, 2003
    • (2003) Molbiol Evol , vol.20 , pp. 1564-1574
    • Theissen, U.1    Hoffmeister, M.2    Grieshaber, M.3    Martin, W.4
  • 168
    • 79953712285 scopus 로고    scopus 로고
    • Sulfur signaling: Is the agent sulfide orsulfane?
    • Toohey JI. Sulfur signaling: is the agent sulfide or sulfane? Anal Biochem 413: 1-7, 2011
    • (2011) Anal Biochem , vol.413 , pp. 1-7
    • Toohey, J.I.1
  • 169
    • 84906657542 scopus 로고    scopus 로고
    • Thiosulfoxide (Sulfane) sulfur:New chemistry and new regulatory roles inbiology
    • Toohey JI, Cooper AJ. Thiosulfoxide (sulfane) sulfur: new chemistry and new regulatory roles in biology. Molecules 19: 12789-12813, 2014
    • (2014) Molecules , vol.19 , pp. 12789-12813
    • Toohey, J.I.1    Cooper, A.J.2
  • 170
    • 84925484963 scopus 로고    scopus 로고
    • Kinetic andthermodynamic studies on the disulfide-bond reducingpotential of hydrogen sulfide
    • Vasas A, Doka E, Fabian I, Nagy P. Kinetic and thermodynamic studies on the disulfide-bond reducing potential of hydrogen sulfide. Nitric Oxide 46: 93-101, 2015
    • (2015) Nitric Oxide , vol.46 , pp. 93-101
    • Vasas, A.1    Doka, E.2    Fabian, I.3    Nagy, P.4
  • 171
    • 1842365519 scopus 로고    scopus 로고
    • Sulphide oxidation andoxidative phosphorylation in the mitochondria ofthe lugworm Arenicola marina
    • Völkel S, Grieshaber MK. Sulphide oxidation and oxidative phosphorylation in the mitochondria of the lugworm Arenicola marina. J Exp Biol 200: 83-92, 1997
    • (1997) J Exp Biol , vol.200 , pp. 83-92
    • Völkel, S.1    Grieshaber, M.K.2
  • 172
    • 0024254814 scopus 로고
    • Before enzymes and templates:Theory of surface metabolism
    • Wächtershäuser G. Before enzymes and templates: theory of surface metabolism. Microbiol Rev 52: 452-484, 1988
    • (1988) Microbiolrev , vol.52 , pp. 452-484
    • Wächtershäuser, G.1
  • 173
    • 34249713769 scopus 로고    scopus 로고
    • On the chemistry and evolutionof the pioneer organism
    • Wächtershäuser G. On the chemistry and evolution of the pioneer organism. Chem Biodivers 4: 584-602, 2007
    • (2007) Chem Biodivers , vol.4 , pp. 584-602
    • Wächtershäuser, G.1
  • 175
    • 84880277784 scopus 로고    scopus 로고
    • The biological chemistry of hydrogenperoxide
    • Winterbourn CC. The biological chemistry of hydrogen peroxide. Methods Enzymol 528: 3-25, 2013
    • (2013) Methods Enzymol , vol.528 , pp. 3-25
    • Winterbourn, C.C.1
  • 176
    • 84880050232 scopus 로고    scopus 로고
    • Structure and kinetic analysis of H2Sproduction by human mercaptopyruvate sulfurtransferase
    • Yadav PK, Yamada K, Chiku T, Koutmos M, Banerjee R. Structure and kinetic analysis of H2S production by human mercaptopyruvate sulfurtransferase. J Biol Chem 288: 20002-20013, 2013
    • (2013) J Biol Chem , vol.288 , pp. 20002-20013
    • Yadav, P.K.1    Yamada, K.2    Chiku, T.3    Koutmos, M.4    Banerjee, R.5
  • 177
    • 0035030625 scopus 로고    scopus 로고
    • Sulfide oxidation coupled toATP synthesis in chicken liver mitochondria
    • Yong R, Searcy DG. Sulfide oxidation coupled to ATP synthesis in chicken liver mitochondria. Comp Biochem Physiol B Biochem Mol Biol 129: 129-137, 2001
    • (2001) Comp Biochem Physiol B Biochem Mol Biol , vol.129 , pp. 129-137
    • Yong, R.1    Searcy, D.G.2


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