메뉴 건너뛰기




Volumn 1827, Issue 8-9, 2013, Pages 871-881

On the antiquity of metalloenzymes and their substrates in bioenergetics

Author keywords

ACS; CODH; Metal sulfide; Methane monooxygenase; Ni Fe hydrogenase

Indexed keywords

ACETYL COENZYME A SYNTHETASE; CARBON MONOXIDE DEHYDROGENASE; ENZYME; METALLOENZYME; METHANE MONOOXYGENASE; METHANETHIOL; NICKEL IRON HYDROGENASE; TRANSITION ELEMENT; UNCLASSIFIED DRUG; METAL;

EID: 84884320609     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2013.02.008     Document Type: Article
Times cited : (123)

References (159)
  • 3
    • 32644453530 scopus 로고    scopus 로고
    • Biogeochemical signatures through time as inferred from whole microbial genomes
    • DOI 10.2475/ajs.305.6-8.467
    • A.L. Zerkle, C.H. House, S.L. Brantley, Biogeochemical signatures through time as inferred from whole microbial genomes, Am. J. Sci. 305 (2005) 467-502. (Pubitemid 43240151)
    • (2005) American Journal of Science , vol.305 , Issue.6-8 SPEC. ISSUE , pp. 467-502
    • Zerkle, A.L.1    House, C.H.2    Brantley, S.L.3
  • 6
    • 84871719406 scopus 로고    scopus 로고
    • Turnstiles and bifurcators: The disequilibrium converting engines that put metabolism on the road
    • E. Branscomb, M.J. Russell, Turnstiles and bifurcators: the disequilibrium converting engines that put metabolism on the road, Biochim. Biophys. Acta Bioenerg. 1827 (2013) 62-78.
    • (2013) Biochim. Biophys. Acta Bioenerg , vol.1827 , pp. 62-78
    • Branscomb, E.1    Russell, M.J.2
  • 10
    • 0028023065 scopus 로고
    • A hydrothermally precipitated catalytic iron sulphide membrane as a first step toward life
    • M.J. Russell, R.M. Daniel, A.J. Hall, J. Sherringham, A hydrothermally precipitated catalytic iron sulphide membrane as a first step toward life, J. Mol. Evol. 39 (1994) 231-243. (Pubitemid 24283339)
    • (1994) Journal of Molecular Evolution , vol.39 , Issue.3 , pp. 231-243
    • Russell, M.J.1    Daniel, R.M.2    Hall, A.J.3    Sherringham, J.A.4
  • 11
    • 0034886919 scopus 로고    scopus 로고
    • Classification and phylogeny of hydrogenases
    • DOI 10.1016/S0168-6445(01)00063-8, PII S0168644501000638
    • P.M. Vignais, B. Billoud, J. Meyer, Classification and phylogeny of hydrogenases, FEMS Microbiol. Rev. 25 (2001) 455-501. (Pubitemid 32778469)
    • (2001) FEMS Microbiology Reviews , vol.25 , Issue.4 , pp. 455-501
    • Vignais, P.M.1    Billoud, B.2    Meyer, J.3
  • 12
    • 70349966236 scopus 로고    scopus 로고
    • Evolutionary formation of new protein folds is linked to metallic cofactor recruitment
    • H.-F. Ji, L. Chen, Y.-Y. Jiang, H.-Y. Zhang, Evolutionary formation of new protein folds is linked to metallic cofactor recruitment, Bioessays 31 (2009) 975-980.
    • (2009) Bioessays , vol.31 , pp. 975-980
    • Ji, H.-F.1    Chen, L.2    Jiang, Y.-Y.3    Zhang, H.-Y.4
  • 14
    • 3242755111 scopus 로고    scopus 로고
    • The rocky roots of the acetyl-CoA pathway
    • DOI 10.1016/j.tibs.2004.05.007, PII S0968000404001276
    • M.J. Russell, W. Martin, The rocky roots of the acetyl coenzyme-A pathway, Trends Biochem. Sci. 24 (2004) 358-363. (Pubitemid 38968752)
    • (2004) Trends in Biochemical Sciences , vol.29 , Issue.7 , pp. 358-363
    • Russell, M.J.1    Martin, W.2
  • 17
    • 84866432793 scopus 로고    scopus 로고
    • The nitrogen cycle in the Archaean; An intricate interplay of enzymatic and abiotic reactions
    • J.W.B. Moir (Ed.) Caister Academic Press, ISBN: 978-1-904455-86-8 (Chapter I)
    • R. van Lis, A.-L. Ducluzeau, W. Nitschke, B. Schoepp-Cothenet, The nitrogen cycle in the Archaean; an intricate interplay of enzymatic and abiotic reactions, in: J.W.B. Moir (Ed.), Nitrogen Cycling in Bacteria: Molecular Analysis, Caister Academic Press, ISBN: 978-1-904455-86-8, 2011, pp. 1-21, (Chapter I).
    • (2011) Nitrogen Cycling in Bacteria: Molecular Analysis , pp. 1-21
    • Van Lis, R.1    Ducluzeau, A.-L.2    Nitschke, W.3    Schoepp-Cothenet, B.4
  • 18
    • 72449155029 scopus 로고    scopus 로고
    • Hydrothermal focusing of chemical and chemiosmotic energy, supported by delivery of catalytic Fe, Ni, Mo/W, Co, S and Se, forced life to emerge
    • W. Nitschke, M.J. Russell, 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 (2009) 481-496.
    • (2009) J. Mol. Evol , vol.69 , pp. 481-496
    • Nitschke, W.1    Russell, M.J.2
  • 19
    • 84555179630 scopus 로고    scopus 로고
    • Redox bifurcations: Mechanisms and importance to life now, and at its origin
    • W. Nitschke, M.J. Russell, Redox bifurcations: mechanisms and importance to life now, and at its origin, Bioessays 34 (2012) 106-109.
    • (2012) Bioessays , vol.34 , pp. 106-109
    • Nitschke, W.1    Russell, M.J.2
  • 20
    • 84859739098 scopus 로고    scopus 로고
    • The ineluctable requirement for the trans-iron elements molybdenum and/or tungsten in the origin of life
    • B. Schoepp-Cothenet, R. van Lis, P. Philippot, A. Magalon, M.J. Russell, W. Nitschke, The ineluctable requirement for the trans-iron elements molybdenum and/or tungsten in the origin of life, Sci. Rep. 2 (2012) 263.
    • (2012) Sci. Rep , vol.2 , pp. 263
    • Schoepp-Cothenet, B.1    Van Lis, R.2    Philippot, P.3    Magalon, A.4    Russell, M.J.5    Nitschke, W.6
  • 22
    • 49249132556 scopus 로고    scopus 로고
    • Enzyme phylogenies as markers for the oxidation state of the environment: The case of respiratory arsenate reductase and related enzymes
    • S. Duval, A.-L. Ducluzeau, W. Nitschke, B. Schoepp-Cothenet, Enzyme phylogenies as markers for the oxidation state of the environment: the case of respiratory arsenate reductase and related enzymes, BMC Evol. Biol. 8 (2008) 206-219.
    • (2008) BMC Evol. Biol , vol.8 , pp. 206-219
    • Duval, S.1    Ducluzeau, A.-L.2    Nitschke, W.3    Schoepp-Cothenet, B.4
  • 23
    • 84862223771 scopus 로고    scopus 로고
    • Evolution and diversification of Group 1 NiFe hydrogenases. Is there a phylogenetic marker for O2-tolerance?
    • M.E. Pandelia, W. Lubitz, W. Nitschke, Evolution and diversification of Group 1 NiFe hydrogenases. Is there a phylogenetic marker for O2-tolerance? Biochim. Biophys. Acta Bioenerg. 1817 (2012) 1565-1575.
    • (2012) Biochim. Biophys. Acta Bioenerg , vol.1817 , pp. 1565-1575
    • Pandelia, M.E.1    Lubitz, W.2    Nitschke, W.3
  • 25
    • 78649496932 scopus 로고    scopus 로고
    • Just like the Universe the emergence of life had high enthalpy and low entropy beginnings
    • W. Nitschke, M.J. Russell, Just like the Universe the emergence of life had high enthalpy and low entropy beginnings, J. Cosmol. 10 (2010) 3200-3216.
    • (2010) J. Cosmol , vol.10 , pp. 3200-3216
    • Nitschke, W.1    Russell, M.J.2
  • 27
    • 0001202417 scopus 로고
    • Evolution of the structure of ferredoxin based on living relics of primitive amino acid sequences
    • R.V. Eck, M.O. Dayhoff, Evolution of the structure of ferredoxin based on living relics of primitive amino acid sequences, Science 152 (1966) 363-366.
    • (1966) Science , vol.152 , pp. 363-366
    • Eck, R.V.1    Dayhoff, M.O.2
  • 28
    • 0015218669 scopus 로고
    • Role of ferredoxins in the origin of life and biological evolution
    • D.O. Hall, R. Cammack, K.K. Rao, Role of ferredoxins in the origin of life and biological evolution, Nature 233 (1971) 136-138.
    • (1971) Nature , vol.233 , pp. 136-138
    • Hall, D.O.1    Cammack, R.2    Rao, K.K.3
  • 29
    • 1542339055 scopus 로고    scopus 로고
    • On the dissipation of thermal and chemical energies on the early Earth: The onsets of hydrothermal convection, chemiosmosis, genetically regulated metabolism and oxygenic photosynthesis
    • R. Ikan (Ed.) Kluwer Academic Publishers, Dordrecht
    • M.J. Russell, A.J. Hall, A. Mellersh, On the dissipation of thermal and chemical energies on the early Earth: the onsets of hydrothermal convection, chemiosmosis, genetically regulated metabolism and oxygenic photosynthesis, in: R. Ikan (Ed.), Natural and Laboratory-Simulated Thermal Geochemical Processes, Kluwer Academic Publishers, Dordrecht, 2003, pp. 325-388.
    • (2003) Natural and Laboratory-Simulated Thermal Geochemical Processes , pp. 325-388
    • Russell, M.J.1    Hall, A.J.2    Mellersh, A.3
  • 30
    • 0037131241 scopus 로고    scopus 로고
    • A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl- CoA synthase
    • DOI 10.1126/science.1075843
    • T.I. Doukov, T.M. Iverson, J. Seravalli, S.W. Ragsdale, C.L. Drennan, A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase, Science 298 (2002) 567-572. (Pubitemid 35215305)
    • (2002) Science , vol.298 , Issue.5593 , pp. 567-572
    • Doukov, T.I.1    Iverson, T.M.2    Seravalli, J.3    Ragsdale, S.W.4    Drennan, C.L.5
  • 31
    • 0242695597 scopus 로고    scopus 로고
    • The active site and catalytic mechanism of NiFe hydrogenases
    • A. Volbeda, J.C. Fontecilla-Camps, The active site and catalytic mechanism of NiFe hydrogenases, Dalton Trans. 2003 (2003) 4030-4038.
    • (2003) Dalton Trans , vol.2003 , pp. 4030-4038
    • Volbeda, A.1    Fontecilla-Camps, J.C.2
  • 32
    • 33845425138 scopus 로고    scopus 로고
    • Catalytic nickel-iron-sulfur clusters: From minerals to enzymes
    • DOI 10.1007/3418-003, Bioorganometallic Chemistry
    • A. Volbeda, J.C. Fontecilla-Camps, Catalytic nickel-iron-sulfur clusters: from minerals to enzymes, in: G. Simmonneaux (Ed.), Topics in Organometallic Chemistry, vol. 17, Springer, Berlin, Germany, 2006, pp. 57-82. (Pubitemid 44889516)
    • (2006) Topics in Organometallic Chemistry , vol.17 , pp. 57-82
    • Volbeda, A.1    Fontecilla-Camps, J.C.2
  • 34
  • 35
    • 0037560872 scopus 로고    scopus 로고
    • Mechanistic studies on the hydroxylation of methane by methane monooxygenase
    • M.-H. Baik, M. Newcomb, R.A. Friesner, S.J. Lippard, Mechanistic studies on the hydroxylation of methane by methane monooxygenase, Chem. Rev. 103 (2003) 2385-2419.
    • (2003) Chem. Rev , vol.103 , pp. 2385-2419
    • Baik, M.-H.1    Newcomb, M.2    Friesner, R.A.3    Lippard, S.J.4
  • 36
    • 33645485151 scopus 로고    scopus 로고
    • The evolutionary significance of the metabolism of tungsten by microorganisms growing at 100 °c
    • J. Wiegel, M.W. Adams (Eds) Taylor and Francis, London and Philadelphia
    • M.W.W. Adams, The evolutionary significance of the metabolism of tungsten by microorganisms growing at 100 °C, in: J. Wiegel, M.W. Adams (Eds.), Thermophiles: the Keys to Molecular Evolution and the Origin of Life? Taylor and Francis, London and Philadelphia, 1998, pp. 325-338.
    • (1998) Thermophiles: The Keys to Molecular Evolution and the Origin of Life? , pp. 325-338
    • Adams, M.W.W.1
  • 38
    • 0036293842 scopus 로고    scopus 로고
    • A novel main-chain anion-binding site in proteins: The nest. A particular combination of phi, psi values in successive residues gives rise to anion-binding sites that occur commonly and are found often at functionally important regions
    • DOI 10.1006/jmbi.2001.5227
    • J.D. Watson, E.J. Milner-White, A novel main-chain anion-binding site in proteins: The Nest. A particular combination of phi, psi values in successive residues gives rise to anion-binding sites that occur commonly and are found often at functionally important regions, J. Mol. Biol. 315 (2002) 171-182. (Pubitemid 34722120)
    • (2002) Journal of Molecular Biology , vol.315 , Issue.2 , pp. 171-182
    • Watson, J.D.1    Milner-White, E.J.2
  • 39
    • 18644380729 scopus 로고    scopus 로고
    • Sites for phosphates and iron-sulfur thiolates in the first membranes: 3 to 6 residue anion-binding motifs (nests)
    • DOI 10.1007/s11084-005-4582-7
    • E.J. Milner-White, M.J. Russell, Sites for phosphates and iron-sulfur thiolates in the first membranes: 3 to 6 residue anion-binding motifs (nests), Orig. Life Evol. Biosph. 35 (2005) 19-27. (Pubitemid 40660308)
    • (2005) Origins of Life and Evolution of the Biosphere , vol.35 , Issue.1 , pp. 19-27
    • Milner-White, E.J.1    Russell, M.J.2
  • 40
    • 39349107507 scopus 로고    scopus 로고
    • Predicting peptide and protein conformations in early evolution
    • E.J. Milner-White, M.J. Russell, Predicting peptide and protein conformations in early evolution, Biol. Direct 3 (2008) 3, http://dx.doi.org/10. 1186/1745-6150-3-3.
    • (2008) Biol. Direct , vol.3 , pp. 3
    • Milner-White, E.J.1    Russell, M.J.2
  • 41
    • 84886096198 scopus 로고    scopus 로고
    • Why are cells powered by proton gradients?
    • N. Lane, Why are cells powered by proton gradients? Nat. Educ. 3 (2010) 18.
    • (2010) Nat. Educ , vol.3 , pp. 18
    • Lane, N.1
  • 42
    • 77950456083 scopus 로고    scopus 로고
    • How did LUCA make a living? Chemiosmosis in the origin of life
    • N. Lane, J.F. Allen, W. Martin, How did LUCA make a living? Chemiosmosis in the origin of life, Bioessays 32 (2010) 271-280.
    • (2010) Bioessays , vol.32 , pp. 271-280
    • Lane, N.1    Allen, J.F.2    Martin, W.3
  • 43
    • 27844507018 scopus 로고    scopus 로고
    • Unusual pathways and enzymes of central carbohydrate metabolism in Archaea
    • DOI 10.1016/j.mib.2005.10.014, PII S1369527405001700, Growth Development
    • B. Siebers, P. Schönheit, Unusual pathways and enzymes of central carbohydrate metabolism in Archaea, Curr. Opin. Microbiol. 8 (2005) 695-705. (Pubitemid 41643038)
    • (2005) Current Opinion in Microbiology , vol.8 , Issue.6 , pp. 695-705
    • Siebers, B.1    Schonheit, P.2
  • 44
    • 77951112274 scopus 로고    scopus 로고
    • Fructose 1,6-bisphosphate aldolase/phosphatase may be an ancestral gluconeogenic enzyme
    • R.F. Say, G. Fuchs, Fructose 1,6-bisphosphate aldolase/phosphatase may be an ancestral gluconeogenic enzyme, Nature 464 (2010) 1077-1081.
    • (2010) Nature , vol.464 , pp. 1077-1081
    • Say, R.F.1    Fuchs, G.2
  • 45
    • 80053227684 scopus 로고    scopus 로고
    • Alternative pathways of carbon dioxide fixation: Insights into the early evolution of life
    • G. Fuchs, Alternative pathways of carbon dioxide fixation: insights into the early evolution of life, Annu. Rev. Microbiol. 65 (2011) 631-658.
    • (2011) Annu. Rev. Microbiol , vol.65 , pp. 631-658
    • Fuchs, G.1
  • 48
    • 0642308250 scopus 로고    scopus 로고
    • The respiratory arsenate reductase from Bacillus selenitireducens strain MLS10
    • DOI 10.1016/S0378-1097(03)00609-8, PII S0378109703006098
    • E. Afkar, J. Lisak, C. Saltikov, P. Basu, R.S. Oremland, J.F. Stolz, The respiratory arsenate reductase from Bacillus selenitireducens strain MLS10, FEMS Microbiol. Lett. 226 (2003) 107-112. (Pubitemid 38444904)
    • (2003) FEMS Microbiology Letters , vol.226 , Issue.1 , pp. 107-112
    • Afkar, E.1    Lisak, J.2    Saltikov, C.3    Basu, P.4    Oremland, R.S.5    Stolz, J.F.6
  • 49
    • 1042265201 scopus 로고    scopus 로고
    • Electrochemical Studies of Arsenite Oxidase: An Unusual Example of a Highly Cooperative Two-Electron Molybdenum Center
    • DOI 10.1021/bi0357154
    • K.R. Hoke, N. Cobb, F.A. Armstrong, R. Hille, Electrochemical studies of arsenite oxidase: an unusual example of a highly cooperative two-electron molybdenum center, Biochemistry 43 (2004) 1667-1674. (Pubitemid 38200573)
    • (2004) Biochemistry , vol.43 , Issue.6 , pp. 1667-1674
    • Hoke, K.R.1    Cobb, N.2    Armstrong, F.A.3    Hille, R.4
  • 50
    • 33947186216 scopus 로고    scopus 로고
    • Alkalilimnicola ehrlichii sp nov, a novel, arsenite-oxidizing haloalkaliphilic gammaproteobacterium capable of chemoautotrophic or heterotrophic growth with nitrate or oxygen as the electron acceptor
    • DOI 10.1099/ijs.0.64576-0
    • S.E. Hoeft, J. Switzer Blum, J.F. Stolz, F.R. Tabita, B. Witte, G.M. King, J.M. Santini, R.S. Oremland, Alkalilimnicola ehrlichii sp. nov., a novel, arsenite-oxidizing haloalkaliphilic gamma proteobacterium capable of chemoautotrophic or heterotrophic growth with nitrate or oxygen as the electron acceptor, Int. J. Syst. Evol. Microbiol. 57 (2007) 504-512. (Pubitemid 46437862)
    • (2007) International Journal of Systematic and Evolutionary Microbiology , vol.57 , Issue.3 , pp. 504-512
    • Hoeft, S.E.1    Blum, J.S.2    Stolz, J.F.3    Tabita, F.R.4    Witte, B.5    King, G.M.6    Santini, J.M.7    Oremland, R.S.8
  • 51
    • 0342758523 scopus 로고    scopus 로고
    • Phosphite oxidation by sulphate reduction
    • B. Schink, M. Friedrich, Phosphite oxidation by sulphate reduction, Nature 406 (2000) 37.
    • (2000) Nature , vol.406 , pp. 37
    • Schink, B.1    Friedrich, M.2
  • 52
    • 84856259383 scopus 로고    scopus 로고
    • Bar-coded pyrosequencing reveals the responses of PBDE-degrading microbial communities to electron donor amendments
    • M. Xu, X. Chen, M. Qiu, X. Zeng, J. Xu, et al., Bar-coded pyrosequencing reveals the responses of PBDE-degrading microbial communities to electron donor amendments, PLoS One 7 (1) (2012) e30439, http://dx.doi.org/10.1371/journal. pone.0030439.
    • (2012) PLoS One , vol.7 , Issue.1
    • Xu, M.1    Chen, X.2    Qiu, M.3    Zeng, X.4    Xu, J.5
  • 53
    • 84871713951 scopus 로고    scopus 로고
    • Microbial metabolism of oxochlorates: A bioenergetic perspective
    • T. Nilsson, M. Rova, A.S. Bäcklund, Microbial metabolism of oxochlorates: a bioenergetic perspective, Biochim. Biophys. Acta Bioenerg. 1827 (2013) 189-197, http://dx.doi.org/10.1016/j.bbabio.2012.06.010.
    • (2013) Biochim. Biophys. Acta Bioenerg , vol.1827 , pp. 189-197
    • Nilsson, T.1    Rova, M.2    Bäcklund, A.S.3
  • 55
    • 0034810541 scopus 로고    scopus 로고
    • Multiple lateral transfers of dissimilatory sulfite reductase genes between major lineages of sulfate-reducing prokaryotes
    • DOI 10.1128/JB.183.20.6028-6035.2001
    • M. Klein, M. Friedrich, A.J. Roger, P. Hugenholtz, S. Fishbain, H. Abicht, L.L. Blackall, D.A. Stahl, M. Wagner, Multiple lateral transfers of dissimilatory sulfite reductase genes between major lineages of sulfate-reducing prokaryotes, J. Bacteriol. 183 (2001) 6028-6035. (Pubitemid 32917422)
    • (2001) Journal of Bacteriology , vol.183 , Issue.20 , pp. 6028-6035
    • Klein, M.1    Friedrich, M.2    Roger, A.J.3    Hugenholtz, P.4    Fishbain, S.5    Abicht, H.6    Blackall, L.L.7    Stahl, D.A.8    Wagner, M.9
  • 56
    • 0037787922 scopus 로고    scopus 로고
    • Single eubacterial origin of eukaryotic sulfide: Quinone oxidoreductase, a mitochondrial enzyme conserved from the early evolution of eukaryotes during anoxic and sulfidic times
    • DOI 10.1093/molbev/msg174
    • U. Theissen, M. Hoffmeister, M. Grieshaber, W. Martin, 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 (2003) 1564-1574. (Pubitemid 37082591)
    • (2003) Molecular Biology and Evolution , vol.20 , Issue.9 , pp. 1564-1574
    • Theissen, U.1    Hoffmeister, M.2    Grieshaber, M.3    Martin, W.4
  • 57
    • 50049103112 scopus 로고    scopus 로고
    • The prokaryotic complex iron-sulfur molybdoenzyme family
    • R.A. Rothery, G.J. Workun, J.H. Weiner, The prokaryotic complex iron-sulfur molybdoenzyme family, Biochim. Biophys. Acta 1778 (2008) 1897-1929.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1897-1929
    • Rothery, R.A.1    Workun, G.J.2    Weiner, J.H.3
  • 58
    • 0036016822 scopus 로고    scopus 로고
    • Molecular analysis of dimethyl sulphide dehydrogenase from Rhodovulum sulfidophilum: Its place in the dimethyl sulphoxide reductase family of microbial molybdopterin-containing enzymes
    • DOI 10.1046/j.1365-2958.2002.02978.x
    • C.A. McDevitt, P. Hugenholtz, G.R. Hanson, A.G. McEwan, Molecular analysis of dimethyl sulphide dehydrogenase from Rhodovulum sulfidophilum: its place in the dimethyl sulphoxide reductase family of microbial molybdopterincontaining enzymes, Mol. Microbiol. 44 (2002) 1575-1587. (Pubitemid 34639434)
    • (2002) Molecular Microbiology , vol.44 , Issue.6 , pp. 1575-1587
    • McDevitt, C.A.1    Hugenholtz, P.2    Hanson, G.R.3    McEwan, A.G.4
  • 59
    • 0034637432 scopus 로고    scopus 로고
    • The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases
    • DOI 10.1016/S0014-5793(00)01867-6, PII S0014579300018676
    • T. Friedrich, D. Scheide, The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases, FEBS Lett. 479 (2000) 1-5. (Pubitemid 30625247)
    • (2000) FEBS Letters , vol.479 , Issue.1-2 , pp. 1-5
    • Friedrich, T.1    Scheide, D.2
  • 60
    • 0037122944 scopus 로고    scopus 로고
    • Quinol: Fumarate oxidoreductases and succinate: Quinone oxidoreductases: Phylogenetic relationships, metal centres and membrane attachment
    • DOI 10.1016/S0005-2728(01)00239-0, PII S0005272801002390
    • R.S. Lemos, A.S. Fernandes, M.M. Pereira, C.M. Gomes, M. Teixeira, Quinol:fumarate oxidoreductases and succinate:quinone oxidoreductases: phylogenetic relationships, metal centres and membrane attachment, Biochim. Biophys. Acta Bioenerg. 1553 (2002) 158-170. (Pubitemid 34137067)
    • (2002) Biochimica et Biophysica Acta - Bioenergetics , vol.1553 , Issue.1-2 , pp. 158-170
    • Lemos, R.S.1    Fernandes, A.S.2    Pereira, M.M.3    Gomes, C.M.4    Teixeira, M.5
  • 61
    • 84871718657 scopus 로고    scopus 로고
    • Amissing link between complex i and group 4 membrane-bound NiFe hydrogenases
    • B.C.Marreiros, A.P. Batista, A.M.S. Duarte,M.M. Pereira, Amissing link between complex I and group 4 membrane-bound NiFe hydrogenases, Biochim. Biophys. Acta Bioenerg. 1827 (2013) 198-209, http://dx.doi.org/10.1016/j.bbabio. 2012.09.012.
    • (2013) Biochim. Biophys. Acta Bioenerg , vol.1827 , pp. 198-209
    • Marreiros, B.C.1    Batista, A.P.2    Duarte, A.M.S.3    Pereira, M.M.4
  • 62
    • 0037184270 scopus 로고    scopus 로고
    • Denitrifying genes in bacterial and archaeal genomes
    • L. Philippot, Denitrifying genes in bacterial and archaeal genomes, Biochim. Biophys. Acta Gene Struct. Expr. 1577 (2002) 355-376.
    • (2002) Biochim. Biophys. Acta Gene Struct. Expr , vol.1577 , pp. 355-376
    • Philippot, L.1
  • 63
    • 34447512729 scopus 로고    scopus 로고
    • Volcanic emissions and the early Earth atmosphere
    • DOI 10.1016/j.gca.2007.04.035, PII S0016703707002475
    • R.S. Martin, T.A. Mather, D.M. Pyle, Volcanic emissions and the early Earth atmosphere, Geochim. Cosmochim. Acta 71 (2007) 3673-3685. (Pubitemid 47065183)
    • (2007) Geochimica et Cosmochimica Acta , vol.71 , Issue.15 , pp. 3673-3685
    • Martin, R.S.1    Mather, T.A.2    Pyle, D.M.3
  • 65
    • 21344469473 scopus 로고    scopus 로고
    • Hydrothermal Fe fluxes during the Precambrian: Effect of low oceanic sulfate concentrations and low hydrostatic pressure on the composition of black smokers
    • DOI 10.1016/j.epsl.2005.04.040, PII S0012821X05002918
    • L.R. Kump, W.E. Seyfried, Hydrothermal Fe fluxes during the Precambrian: effect of low oceanic sulfate concentrations and low hydrostatic pressure on the composition of black smokers, Earth Planet. Sci. Lett. 235 (2005) 654-662. (Pubitemid 40912055)
    • (2005) Earth and Planetary Science Letters , vol.235 , Issue.3-4 , pp. 654-662
    • Kump, L.R.1    Seyfried Jr., W.E.2
  • 66
    • 70349733142 scopus 로고    scopus 로고
    • Iron partitioning and hydrogen generation during serpentinization of abyssal peridotites from 15°N on theMid-Atlantic Ridge
    • F. Klein, W. Bach, N. Jöns, T. McCollom, B. Moskowitz, T. Berquó, Iron partitioning and hydrogen generation during serpentinization of abyssal peridotites from 15°N on theMid-Atlantic Ridge, Geochim. Cosmochim. Acta 73 (2009) 6868-6893.
    • (2009) Geochim. Cosmochim. Acta , vol.73 , pp. 6868-6893
    • Klein, F.1    Bach, W.2    Jöns, N.3    McCollom, T.4    Moskowitz, B.5    Berquó, T.6
  • 68
    • 0024254814 scopus 로고
    • Before enzymes and templates: Theory of surface metabolism
    • G. Wächtershäuser, Before enzymes and templates: theory of surface metabolism, Microbiol. Rev. 52 (1988) 452-484.
    • (1988) Microbiol. Rev , vol.52 , pp. 452-484
    • Wächtershäuser, G.1
  • 69
    • 0024899963 scopus 로고
    • In vitro growth of iron sulphide chimneys: Possible culture chambers for origin-of-life experiments
    • M.J. Russell, A.J. Hall, D. Turner, In vitro growth of iron sulphide chimneys: possible culture chambers for origin-of-life experiments, Terra Nova 1 (1989) 238-241.
    • (1989) Terra Nova , vol.1 , pp. 238-241
    • Russell, M.J.1    Hall, A.J.2    Turner, D.3
  • 72
  • 73
    • 0842269839 scopus 로고    scopus 로고
    • Capture of molybdenum in pyrite-forming sediments: Role of ligand-induced reduction by polysulfides
    • DOI 10.1016/S0016-7037(00)00444-7
    • T.P. Vorlicek, M.D. Kahn, Y. Kasuya, G.R. Helz, Capture of molybdenum in pyrite-forming sediments; role of ligand-induced reduction by polysulfides, Geochim. Cosmochim. Acta 68 (2004) 547-556. (Pubitemid 38162485)
    • (2004) Geochimica et Cosmochimica Acta , vol.68 , Issue.3 , pp. 547-556
    • Vorlicek, T.P.1    Kahn, M.D.2    Kasuya, Y.3    Helz, G.R.4
  • 74
    • 79952451539 scopus 로고    scopus 로고
    • U-Th systematics and 230Th ages of carbonate chimneys at the Lost City hydrothermal field
    • K.A. Ludwig, C.C. Shen, D.S. Kelley, H. Cheng, R.L. Edwards, U-Th systematics and 230Th ages of carbonate chimneys at the Lost City hydrothermal field, Geochim. Cosmochim. Acta 75 (2011) 1869-1888.
    • (2011) Geochim. Cosmochim. Acta , vol.75 , pp. 1869-1888
    • Ludwig, K.A.1    Shen, C.C.2    Kelley, D.S.3    Cheng, H.4    Edwards, R.L.5
  • 76
    • 80054087048 scopus 로고    scopus 로고
    • Abioticmethane flux fromthe Chimaera seep and Tekirova ophiolites (Turkey): Understanding gas exhalation from low temperature serpentinization and implications for Mars
    • G. Etiope,M. Schoell,H.Hosgormez,Abioticmethane flux fromthe Chimaera seep and Tekirova ophiolites (Turkey): understanding gas exhalation from low temperature serpentinization and implications for Mars, Earth Planet. Sci. Lett. 310 (2011) 96-104.
    • (2011) Earth Planet. Sci. Lett , vol.310 , pp. 96-104
    • Etiope, G.1    Schoell, M.2    Hosgormez, H.3
  • 80
    • 45749153355 scopus 로고    scopus 로고
    • Abiotic ammonium formation in the presence of Ni-Fe metals and alloys and its implications for the Hadean nitrogen cycle
    • A. Smirnov, D. Hausner, R. Laffers, D.R. Strongin, M.A.A. Schoonen, Abiotic ammonium formation in the presence of Ni-Fe metals and alloys and its implications for the Hadean nitrogen cycle, Geochem. Trans. 9 (2008) 5, http://dx.doi.org/10.1186/ 1467-4866-9-5.
    • (2008) Geochem. Trans , vol.9 , pp. 5
    • Smirnov, A.1    Hausner, D.2    Laffers, R.3    Strongin, D.R.4    Schoonen, M.A.A.5
  • 81
    • 0000526144 scopus 로고
    • Mineral theories of the origin of life and an iron sulphide example
    • A.G. Cairns-Smith, A.J. Hall, M.J. Russell, Mineral theories of the origin of life and an iron sulphide example, Orig. Life Evol. Biosph. 22 (1992) 161-180.
    • (1992) Orig. Life Evol. Biosph , vol.22 , pp. 161-180
    • Cairns-Smith, A.G.1    Hall, A.J.2    Russell, M.J.3
  • 82
    • 0038322915 scopus 로고    scopus 로고
    • High Archean climatic temperature inferred from oxygen isotope geochemistry of cherts in the 3.5 Ga Swaziland Supergroup, South Africa
    • DOI 10.1130/0016-7606(2003)115 <0566:HACTIF>2.0.CO;2
    • L.P. Knauth, D.R. Lowe, High Archean climatic temperature inferred from oxygen isotope geochemistry of cherts in the 3.5 Ga Swaziland Supergroup, South Africa, Geol. Soc. Am. Bull. 115 (2003) 566-580. (Pubitemid 36650380)
    • (2003) Bulletin of the Geological Society of America , vol.115 , Issue.5 , pp. 566-580
    • Knauth, L.P.1    Lowe, D.R.2
  • 85
    • 0037735248 scopus 로고    scopus 로고
    • Crystals and life
    • DOI 10.1002/hlca.200390135
    • G.O. Arrhenius, Crystals and life, Helv. Chim. Acta 86 (2003) 1569-1586. (Pubitemid 36735720)
    • (2003) Helvetica Chimica Acta , vol.86 , Issue.5 , pp. 1569-1586
    • Arrhenius, G.O.1
  • 86
    • 33947112786 scopus 로고    scopus 로고
    • 3
    • DOI 10.1016/j.gca.2007.01.002, PII S0016703707000166
    • N.H. de Leeuw, T.G. Cooper, Surface simulation studies of the hydration of white rust Fe(OH)2, goethite a-FeO(OH) and hematite a-Fe2O3, Geochim. Cosmochim. Acta 71 (2007) 1655-1673. (Pubitemid 46395092)
    • (2007) Geochimica et Cosmochimica Acta , vol.71 , Issue.7 , pp. 1655-1673
    • De Leeuw, N.H.1    Cooper, T.G.2
  • 88
    • 72149118443 scopus 로고    scopus 로고
    • Elevated concentrations of formate, acetate and dissolved organic carbon found at the Lost City hydrothermal field
    • S.Q. Lang, D.A. Butterfield, M. Schulte, D.S. Kelley, M.D. Lilley, Elevated concentrations of formate, acetate and dissolved organic carbon found at the Lost City hydrothermal field, Geochim. Cosmochim. Acta 74 (2010) 941-952.
    • (2010) Geochim. Cosmochim. Acta , vol.74 , pp. 941-952
    • Lang, S.Q.1    Butterfield, D.A.2    Schulte, M.3    Kelley, D.S.4    Lilley, M.D.5
  • 89
    • 78649499060 scopus 로고    scopus 로고
    • High production and fluxes of H2 and CH4 and evidence of abiotic hydrocarbon synthesis by serpentinization in ultramafic-hosted hydrothermal systems on theMid-Atlantic Ridge
    • P. Rona, C. Devey, J. Dyment, B. Murton (Eds.) AGU Geophysical Monograph 188American Geophysical Union,Washington DC
    • J.L. Charlou, J.P. Donval, C. Konn, H. Ondreas, Y. Fouquet, P. Jean-Baptiste, E. Fourré, High production and fluxes of H2 and CH4 and evidence of abiotic hydrocarbon synthesis by serpentinization in ultramafic-hosted hydrothermal systems on theMid-Atlantic Ridge, in: P. Rona, C. Devey, J. Dyment, B. Murton (Eds.), Diversity of Hydrothermal Systems on Slow Spreading Ocean Ridges, AGU Geophysical Monograph 188American Geophysical Union,Washington DC, 2010.
    • (2010) Diversity of Hydrothermal Systems on Slow Spreading Ocean Ridges
    • Charlou, J.L.1    Donval, J.P.2    Konn, C.3    Ondreas, H.4    Fouquet, Y.5    Jean-Baptiste, P.6    Fourré, E.7
  • 90
    • 79960018592 scopus 로고    scopus 로고
    • Diffuse flow hydrothermal fluids from 9° 50' N East Pacific Rise: Origin, evolution and biogeochemical controls
    • W.S. Wilcock, et al., (Eds.) The subseafloor biosphere at mid-ocean ridges AGU, Washington, D. C
    • K.L. Von Damm, M.D. Lilley, Diffuse flow hydrothermal fluids from 9° 50' N East Pacific Rise: Origin, evolution and biogeochemical controls, in: W.S. Wilcock, et al., (Eds.), The subseafloor biosphere at mid-ocean ridges, Geophys. Monogr. Ser., vol. 144, AGU, Washington, D. C, 2004, pp. 245-268, http://dx.doi.org/10.1029/ 144GM16.
    • (2004) Geophys. Monogr. Ser , vol.144 , pp. 245-268
    • Von Damm, K.L.1    Lilley, M.D.2
  • 91
    • 50349087072 scopus 로고    scopus 로고
    • Hydrothermal venting at pressure-temperature conditions above the critical point of seawater, 58S on the mid-Atlantic ridge
    • A. Koschinsky, D. Garbe-Schonberg, S. Sander, K. Schmidt, H. Gennerich, H. Strauss, Hydrothermal venting at pressure-temperature conditions above the critical point of seawater, 58S on the mid-Atlantic ridge, Geology 36 (2008) 615-618.
    • (2008) Geology , vol.36 , pp. 615-618
    • Koschinsky, A.1    Garbe-Schonberg, D.2    Sander, S.3    Schmidt, K.4    Gennerich, H.5    Strauss, H.6
  • 92
    • 0034089852 scopus 로고    scopus 로고
    • Molybdenum(VI) speciation in sulfidic waters: Stability and lability of thiomolybdates
    • DOI 10.1016/S0016-7037(99)00423-8, PII S0016703799004238
    • B.E. Erickson, G.R. Helz, Molybdenum (VI) speciation in sulfidic waters: stability and lability of thiomolybdates, Geochim. Cosmochim. Acta 64 (2000) 1149-1158. (Pubitemid 30239468)
    • (2000) Geochimica et Cosmochimica Acta , vol.64 , Issue.7 , pp. 1149-1158
    • Erickson, B.E.1    Helz, G.R.2
  • 95
    • 0003337751 scopus 로고    scopus 로고
    • The emergence of life from fes bubbles at alkaline hot springs in an acid ocean
    • J.Wiegel, M.W. Adams (Eds.) Taylor and Francis, London and Philadelphia
    • M.J. Russell, D.E. Daia, A.J. Hall, The emergence of life from FeS bubbles at alkaline hot springs in an acid ocean, in: J.Wiegel, M.W. Adams (Eds.), Thermophiles: The Keys to Molecular Evolution and the Origin of Life? Taylor and Francis, London and Philadelphia, 1998, pp. 77-126.
    • (1998) Thermophiles: The Keys to Molecular Evolution and the Origin of Life? , pp. 77-126
    • Russell, M.J.1    Daia, D.E.2    Hall, A.J.3
  • 96
    • 33847763196 scopus 로고    scopus 로고
    • Chemistry of iron sulfides
    • DOI 10.1021/cr0503658
    • D. Rickard, G.W. Luther, Chemistry of iron sulfides, Chem. Rev. 107 (2007) 514-562. (Pubitemid 46381032)
    • (2007) Chemical Reviews , vol.107 , Issue.2 , pp. 514-562
    • Rickard, D.1    Luther III, G.W.2
  • 98
    • 79961060286 scopus 로고    scopus 로고
    • Magnetic ordering in tetragonal FeS: Evidence for strong itinerant spin fluctuations
    • K.D. Kwon, K. Refson, S. Bone, R. Qiao, W-l. Yang, Z. Liu, G. Sposito, Magnetic ordering in tetragonal FeS: evidence for strong itinerant spin fluctuations, Phys. Rev. B 83 (2011) 064402.
    • (2011) Phys. Rev. B , vol.83 , pp. 064402
    • Kwon, K.D.1    Refson, K.2    Bone, S.3    Qiao, R.4    Yang, W.-L.5    Liu, Z.6    Sposito, G.7
  • 99
    • 84864856789 scopus 로고    scopus 로고
    • Water confined between sheets of mackinawite FeS minerals
    • C. Wittekindt, D. Marx, Water confined between sheets of mackinawite FeS minerals, J. Chem. Phys. 137 (2012) 054710.
    • (2012) J. Chem. Phys , vol.137 , pp. 054710
    • Wittekindt, C.1    Marx, D.2
  • 100
    • 0014546747 scopus 로고
    • Nickelian mackinawite from Vlakfontein, Transvaal
    • D.J. Vaughan, Nickelian mackinawite from Vlakfontein, Transvaal, Am. Mineral. 54 (1969) 1190-1193.
    • (1969) Am. Mineral , vol.54 , pp. 1190-1193
    • Vaughan, D.J.1
  • 101
    • 0022182351 scopus 로고
    • The crystal chemistry of iron-nickel thiospinels
    • D.J. Vaughan, J.R. Craig, The crystal chemistry of iron-nickel thiospinels, Am. Mineral. 70 (1985) 1036-1043.
    • (1985) Am. Mineral , vol.70 , pp. 1036-1043
    • Vaughan, D.J.1    Craig, J.R.2
  • 102
    • 26444476901 scopus 로고
    • Nickelian mackinawite from Vlakfontein
    • A.H. Clark, Nickelian mackinawite from Vlakfontein, Transvaal: a discussion, Am. Mineral. 55 (1970) 1802-1807.
    • (1970) Transvaal: A Discussion, Am. Mineral , vol.55 , pp. 1802-1807
    • Clark, A.H.1
  • 103
    • 0000636891 scopus 로고
    • Greigite, the thio-spinel of iron; A new mineral
    • B.J. Skinner, R.C. Erd, F.S. Grimaldi, Greigite, the thio-spinel of iron; a new mineral, Am. Mineral. 49 (1964) 543-555.
    • (1964) Am. Mineral , vol.49 , pp. 543-555
    • Skinner, B.J.1    Erd, R.C.2    Grimaldi, F.S.3
  • 104
    • 0027811323 scopus 로고
    • Adsorption and coprecipitation of divalent metals with mackinawite (FeS)
    • DOI 10.1016/0016-7037(93)90145-M
    • J.W. Morse, T. Arakaki, Adsorption and coprecipitation of divalent metals with mackinawite (FeS), Geochim. Cosmochim. Acta 57 (1993) 3635-3640. (Pubitemid 24418327)
    • (1993) Geochimica et Cosmochimica Acta , vol.57 , Issue.15 , pp. 3635-3640
    • Morse, J.W.1    Arakaki, T.2
  • 106
    • 0030620774 scopus 로고    scopus 로고
    • Activated acetic acid by carbon fixation on (Fe,Ni) S under primordial conditions
    • C. Huber, G. Wächtershäuser, Activated acetic acid by carbon fixation on (Fe, Ni) S under primordial conditions, Science 276 (1997) 245-247.
    • (1997) Science , vol.276 , pp. 245-247
    • Huber, C.1    Wächtershäuser, G.2
  • 107
    • 0037450456 scopus 로고    scopus 로고
    • Primordial reductive amination revisited
    • DOI 10.1016/S0040-4039(02)02863-0, PII S0040403902028630
    • C. Huber, G.Wächtershäuser, Primordial reductive amination revisited, Tetrahedron Lett. 44 (2003) 1695-1697. (Pubitemid 36170115)
    • (2003) Tetrahedron Letters , vol.44 , Issue.8 , pp. 1695-1697
    • Huber, C.1    Wachtershauser, G.2
  • 108
    • 0032584573 scopus 로고    scopus 로고
    • Peptides by activation of amino acids on (Fe,Ni)S surfaces: Implications for the origin of life
    • C. Huber, G. Wächtershäuser, Peptides by activation of amino acids on (Fe, Ni)S surfaces: implications for the origin of life, Science 281 (1998) 670-672.
    • (1998) Science , vol.281 , pp. 670-672
    • Huber, C.1    Wächtershäuser, G.2
  • 109
    • 0043023785 scopus 로고    scopus 로고
    • A possible primordial peptide cycle
    • DOI 10.1126/science.1086501
    • C. Huber, W. Eisenreich, S. Hecht, G. Wächtershäuser, A possible primordial peptide cycle, Science 301 (2003) 938-940. (Pubitemid 36994799)
    • (2003) Science , vol.301 , Issue.5635 , pp. 938-940
    • Huber, C.1    Eisenreich, W.2    Hecht, S.3    Wachtershauser, G.4
  • 110
    • 84861920985 scopus 로고    scopus 로고
    • Peptide and RNA contributions to iron-sulphur chemical gardens as life's first inorganic compartments, catalysts, capacitors and condensers
    • S.E. McGlynn, I. Kanik, M.J. Russell, Peptide and RNA contributions to iron-sulphur chemical gardens as life's first inorganic compartments, catalysts, capacitors and condensers, Philos. Trans. R. Soc. Lond. A Phys. Sci. 370 (2012) 1-16.
    • (2012) Philos. Trans. R. Soc. Lond. A Phys. Sci , vol.370 , pp. 1-16
    • McGlynn, S.E.1    Kanik, I.2    Russell, M.J.3
  • 111
    • 11144296361 scopus 로고    scopus 로고
    • A perspective on the role of minerals in prebiotic synthesis
    • M.A. Schoonen, A. Smirnov, C. Cohn, A perspective on the role of minerals in prebiotic synthesis, Ambio 33 (2004) 539-551. (Pubitemid 40033402)
    • (2004) Ambio , vol.33 , Issue.8 , pp. 539-551
    • Schoonen, M.1    Smirnov, A.2    Cohn, C.3
  • 112
    • 84867191616 scopus 로고    scopus 로고
    • Anaerobic methane oxidation in metalliferous hydrothermal sediments: Influence on carbon flux and decoupling from sulfate reduction
    • S.D. Wankel, M.M. Adams, D.T. Johnston, C.M. Hansel, S.B. Joye, P.R. Girguis, Anaerobic methane oxidation in metalliferous hydrothermal sediments: influence on carbon flux and decoupling from sulfate reduction, Environ. Microbiol. 14 (2012) 2726-2740.
    • (2012) Environ. Microbiol , vol.14 , pp. 2726-2740
    • Wankel, S.D.1    Adams, M.M.2    Johnston, D.T.3    Hansel, C.M.4    Joye, S.B.5    Girguis, P.R.6
  • 113
    • 34547541483 scopus 로고    scopus 로고
    • Green rust formation from the bioreduction of γ-FeOOH (Lepidocrocite): Comparison of several Shewanella species
    • DOI 10.1080/01490450701459333, PII 780799033
    • E.J. O'Loughlin, P. Larese-Casanova, M. Scherer, R. Cook, Green rust formation from the bioreduction of γ-FeOOH (lepidocrocite): comparison of several Shewanella species, Geomicrobiol. J. 24 (2007) 211-230. (Pubitemid 47180055)
    • (2007) Geomicrobiology Journal , vol.24 , Issue.3-4 , pp. 211-230
    • O'Loughlin, E.J.1    Larese-Casanova, P.2    Scherer, M.3    Cook, R.4
  • 114
    • 67650430046 scopus 로고    scopus 로고
    • Manganese- and iron-dependent marine methane oxidation
    • E.J. Beal, C.H. House, V.J. Orphan, Manganese- and iron-dependent marine methane oxidation, Science 325 (2009) 184-187.
    • (2009) Science , vol.325 , pp. 184-187
    • Beal, E.J.1    House, C.H.2    Orphan, V.J.3
  • 116
    • 0027593997 scopus 로고
    • The oxidation of ferrous hydroxide in chloride-containing aqueous media and Pourbaix diagrams of green rust one
    • P. Refait, J.M.R. Génin, The oxidation of ferrous hydroxide in chloride-containing aqueous media and Pourbaix diagrams of green rust one, Corros. Sci. 34 (1993) 797-819.
    • (1993) Corros. Sci , vol.34 , pp. 797-819
    • Refait, P.1    Génin, J.M.R.2
  • 117
    • 26444613316 scopus 로고    scopus 로고
    • In situ Mössbauer spectroscopy: Evidence for green rust (fougerite) in a gleysol and its mineralogical transformations with time and depth
    • DOI 10.1016/j.gca.2005.03.042, PII S0016703705003030
    • F. Feder, F. Trolard, G. Klingelhöfer, G. Bourrié, In situ Mössbauer spectroscopy: evidence for green rust (fougerite) in a gleysol and its mineralogical transformations with time and depth, Geochim. Cosmochim. Acta 69 (2005) 4463-4483. (Pubitemid 41430782)
    • (2005) Geochimica et Cosmochimica Acta , vol.69 , Issue.18 , pp. 4463-4483
    • Feder, F.1    Trolard, F.2    Klingelhofer, G.3    Bourrie, G.4
  • 118
  • 119
    • 33845750085 scopus 로고    scopus 로고
    • Ordering in FeII-III hydroxysalt green rusts from XRD and Mössbauer analysis (chloride, carbonate, sulphate, oxalate⋯); About the structure of hydrotalcite-like compounds
    • J.-M.R. Génin, M. Abdelmoula, R. Aissa, C. Ruby, Ordering in FeII-III hydroxysalt green rusts from XRD and Mössbauer analysis (chloride, carbonate, sulphate, oxalate⋯); about the structure of hydrotalcite-like compounds, Hyperfine Interact. 166 (2006) 391-396.
    • (2006) Hyperfine Interact , vol.166 , pp. 391-396
    • Génin, J.-M.R.1    Abdelmoula, M.2    Aissa, R.3    Ruby, C.4
  • 120
    • 33745212338 scopus 로고    scopus 로고
    • II-III oxyhydroxycarbonate fougerite
    • DOI 10.1016/j.crte.2006.04.005, PII S163107130600085X
    • J.-M.R. Génin, M. Abdelmoula, C. Ruby, C. Upadhyay, Speciation of iron; characterisation and structure of green rusts and FeII-III oxyhydroxycarbonate fougerite, C.R. Geosci. 338 (2006) 402-419. (Pubitemid 43947835)
    • (2006) Comptes Rendus - Geoscience , vol.338 , Issue.6-7 , pp. 402-419
    • Genin, J.-M.R.1    Abdelmoula, M.2    Ruby, C.3    Upadhyay, C.4
  • 121
    • 33745208120 scopus 로고    scopus 로고
    • h-pH Pourbaix diagrams
    • DOI 10.1016/j.crte.2006.04.004, PII S1631071306000848
    • J.-M.R. Génin, C. Ruby, A. Géhin, Ph. Refait, Synthesis of green rust by oxidation of Fe(OH)2, their products of oxidation and reduction of ferric oxyhydroxides; Eh-pH Pourbaix diagrams, C.R. Geosci. 338 (2006) 433-446. (Pubitemid 43947834)
    • (2006) Comptes Rendus - Geoscience , vol.338 , Issue.6-7 , pp. 433-446
    • Genin, J.-M.R.1    Ruby, C.2    Gehin, A.3    Refait, P.4
  • 122
    • 48049099209 scopus 로고    scopus 로고
    • Carbonate and sulphate green rusts - Mechanisms of oxidation and reduction
    • H. Antony, L. Legrand, A. Chaussé, Carbonate and sulphate green rusts - mechanisms of oxidation and reduction, Electrochim. Acta 53 (2008) 7146-7156.
    • (2008) Electrochim. Acta , vol.53 , pp. 7146-7156
    • Antony, H.1    Legrand, L.2    Chaussé, A.3
  • 123
    • 72449206024 scopus 로고    scopus 로고
    • Oxidation modes and thermodynamics of FeII-III oxyhydroxycarbonate green rust: Dissolution-precipitation versus in situ deprotonation
    • C. Ruby, M. Abdelmoula, S. Naille, A. Renard, V. Khare, G. Ona-Nguema, G. Morin, J.-M.R. Génin, Oxidation modes and thermodynamics of FeII-III oxyhydroxycarbonate green rust: dissolution-precipitation versus in situ deprotonation, Geochim. Cosmochim. Acta 74 (2010) 953-966.
    • (2010) Geochim. Cosmochim. Acta , vol.74 , pp. 953-966
    • Ruby, C.1    Abdelmoula, M.2    Naille, S.3    Renard, A.4    Khare, V.5    Ona-Nguema, G.6    Morin, G.7    Génin, J.-M.R.8
  • 125
    • 0015889802 scopus 로고
    • Comment to concept on role of nitrate fermentation and nitrate respiration in an evolutionary pathway of energy metabolism
    • F. Egami, Comment to concept on role of nitrate fermentation and nitrate respiration in an evolutionary pathway of energy metabolism, Z. Allg. Mikrobiol. 13 (1973) 177-181.
    • (1973) Z. Allg. Mikrobiol , vol.13 , pp. 177-181
    • Egami, F.1
  • 126
    • 0028193680 scopus 로고
    • Evaluation of the free energy of formation of Fe(II)-Fe(III) hydroxide-sulphate (green rust) and its reduction of nitrite
    • DOI 10.1016/0016-7037(94)90131-7
    • H.C.B. Hansen, O.K. Borggaard, J. Sørensen, Evaluation of the free energy of formation of Fe(II)-Fe(III) hydroxide-sulphate (green rust) and its reduction of nitrite, Geochim. Cosmochim. Acta 58 (1994) 2599-2608. (Pubitemid 24428437)
    • (1994) Geochimica et Cosmochimica Acta , vol.58 , Issue.12 , pp. 2599-2608
    • Hansen, H.C.B.1    Borggaard, O.K.2    Sorensen, J.3
  • 127
    • 0034745586 scopus 로고    scopus 로고
    • Kinetics of nitrate reduction by green rusts - Effects of interlayer anion and Fe(II):Fe(III) ratio
    • H.C.B. Hansen, S. Guldberg, M. Erbs, C. Bender Koch, Kinetics of nitrate reduction by green rusts - effects of interlayer anion and Fe(II):Fe(III) ratio, Appl. Clay Sci. 18 (2001) 81-91.
    • (2001) Appl. Clay Sci , vol.18 , pp. 81-91
    • Hansen, H.C.B.1    Guldberg, S.2    Erbs, M.3    Bender Koch, C.4
  • 129
    • 84871722568 scopus 로고    scopus 로고
    • Abiotic and microbial interactions during anaerobic transformations of Fe(II) and NO- x
    • F. Picardal, Abiotic and microbial interactions during anaerobic transformations of Fe(II) and NO- x, Front. Microbiol. 3 (2012), http://dx.doi.org/10.3389/fmicb. 2012.00112.
    • (2012) Front. Microbiol , vol.3
    • Picardal, F.1
  • 130
    • 84864509821 scopus 로고    scopus 로고
    • Co-localization of particulate methane monooxygenase and cd1 nitrite reductase in the denitrifying methanotroph 'Candidatus Methylomirabilis oxyfera'
    • M.L. Wu, T.A. Alen, E.G. Donselaar, M. Strous, M.S. Jetten, L. Niftrik, Co-localization of particulate methane monooxygenase and cd1 nitrite reductase in the denitrifying methanotroph 'Candidatus Methylomirabilis oxyfera', FEMS Microbiol. Lett. 334 (2012) 49-56.
    • (2012) FEMS Microbiol. Lett , vol.334 , pp. 49-56
    • Wu, M.L.1    Alen, T.A.2    Donselaar, E.G.3    Strous, M.4    Jetten, M.S.5    Niftrik, L.6
  • 131
    • 0033627381 scopus 로고    scopus 로고
    • Conversion of methane to methanol on diiron and dicopper enzyme models of methane monooxygenase: A theoretical study on a concerted reaction pathway
    • DOI 10.1246/bcsj.73.815
    • K. Yoshizawa, A. Suzuki, Y. Shiota, T. Yamabe, Conversion of methane to methanol on di-iron and dicopper enzyme models of methane monooxygenase: a theoretical study on a concerted reaction pathway, Bull. Chem. Soc. Jpn. 73 (2000) 815-827. (Pubitemid 30235607)
    • (2000) Bulletin of the Chemical Society of Japan , vol.73 , Issue.4 , pp. 815-827
    • Yoshizawa, K.1    Suzuki, A.2    Shiota, Y.3    Yamabe, T.4
  • 132
    • 33746266964 scopus 로고    scopus 로고
    • a, spin. A golden tetrad for understanding metalloenzyme energetics and reaction pathways
    • DOI 10.1007/s00775-006-0136-3
    • L. Noodleman, W.-G. Han, Structure, redox, pKa, spin. A golden tetrad for understanding metalloenzyme energetics and reaction pathways, J. Biol. Inorg. Chem. 11 (2006) 674-694. (Pubitemid 44100463)
    • (2006) Journal of Biological Inorganic Chemistry , vol.11 , Issue.6 , pp. 674-694
    • Noodleman, L.1    Han, W.-G.2
  • 133
    • 39149140682 scopus 로고    scopus 로고
    • Structural model studies for the high-valent intermediate Q of methane monooxygenase from broken-symmetry density functional calculations
    • W.-G. Han, L. Noodleman, Structural model studies for the high-valent intermediate Q of methane monooxygenase from broken-symmetry density functional calculations, Inorg. Chim. Acta 361 (2008) 973-986.
    • (2008) Inorg. Chim. Acta , vol.361 , pp. 973-986
    • Han, W.-G.1    Noodleman, L.2
  • 134
    • 78649521267 scopus 로고    scopus 로고
    • Speculation on quantum mechanics and the operation of life giving catalysts
    • N. Haydon, S.E. McGlynn, O. Robus, Speculation on quantum mechanics and the operation of life giving catalysts, Orig. Life Evol. Biosph. 41 (2011) 35-50.
    • (2011) Orig. Life Evol. Biosph , vol.41 , pp. 35-50
    • Haydon, N.1    McGlynn, S.E.2    Robus, O.3
  • 135
    • 0017148721 scopus 로고
    • Possible molecular mechanisms of the protonmotive function of cytochrome systems
    • P. Mitchell, Possible molecular mechanisms of the protonmotive function of cytochrome systems, J. Theor. Biol. 62 (1976) 327-367.
    • (1976) J. Theor. Biol , vol.62 , pp. 327-367
    • Mitchell, P.1
  • 136
    • 0015506505 scopus 로고
    • Oxidoreduction of cytochrome b in the presence of antimycin
    • M.K. Wikström, J.A. Berden, Oxidoreduction of cytochrome b in the presence of antimycin, Biochim. Biophys. Acta 283 (1972) 403-420.
    • (1972) Biochim. Biophys. Acta , vol.283 , pp. 403-420
    • Wikström, M.K.1    Berden, J.A.2
  • 137
    • 84871712835 scopus 로고    scopus 로고
    • Energy conservation via electron bifurcating ferredoxin reduction and proton/Na+ translocating ferredoxin oxidation
    • W. Buckel, R.K. Thauer, Energy conservation via electron bifurcating ferredoxin reduction and proton/Na+ translocating ferredoxin oxidation, Biochim. Biophys. Acta Bioenerg. 1827 (2012) 94-113.
    • (2012) Biochim. Biophys. Acta Bioenerg , vol.1827 , pp. 94-113
    • Buckel, W.1    Thauer, R.K.2
  • 139
    • 0021669234 scopus 로고
    • Quantitative polyphosphate-induced "prebiotic" peptide formation in H2O by addition of certain azoles and ions
    • J. Rabinowitz, A. Hampaï, Quantitative polyphosphate-induced "prebiotic" peptide formation in H2O by addition of certain azoles and ions, J. Mol. Evol. 21 (1985) 199-201.
    • (1985) J. Mol. Evol , vol.21 , pp. 199-201
    • Rabinowitz, J.1    Hampaï, A.2
  • 140
    • 0014688015 scopus 로고
    • Peptide formation in the presence of linear or cyclic polyphosphates
    • J. Rabinowitz, R. Flores, R. Krebsback, G. Rogers, Peptide formation in the presence of linear or cyclic polyphosphates, Nature 224 (1969) 795-796.
    • (1969) Nature , vol.224 , pp. 795-796
    • Rabinowitz, J.1    Flores, R.2    Krebsback, R.3    Rogers, G.4
  • 141
    • 5044231756 scopus 로고    scopus 로고
    • Carbonyl sulfide-mediated prebiotic formation of peptides
    • DOI 10.1126/science.1102722
    • L. Leman, L. Orgel, M.R. Ghadiri, Carbonyl sulfide-mediated prebiotic formation of peptides, Science 306 (2004) 283-286. (Pubitemid 39336874)
    • (2004) Science , vol.306 , Issue.5694 , pp. 283-286
    • Leman, L.1    Orgel, L.2    Ghadiri, M.R.3
  • 142
    • 0000406389 scopus 로고    scopus 로고
    • Amino terminal Cu(II) and Ni(II) binding ATCUN motif of proteins and peptides
    • C. Harford, B. Sarkar, Amino terminal Cu(II) and Ni(II) binding ATCUN motif of proteins and peptides, Acc. Chem. Res. 30 (1999) 123-130.
    • (1999) Acc. Chem. Res , vol.30 , pp. 123-130
    • Harford, C.1    Sarkar, B.2
  • 143
    • 33947336002 scopus 로고
    • Metal ion exchange of square-planar nickel(II) tetraglycine with polydentate amines
    • N.W.H. Ma, D.A. White, R.B. Martin, Metal ion exchange of square-planar nickel(II) tetraglycine with polydentate amines, Inorg. Chem. 6 (1967) 1632-1636.
    • (1967) Inorg. Chem , vol.6 , pp. 1632-1636
    • Ma, N.W.H.1    White, D.A.2    Martin, R.B.3
  • 144
    • 0742321266 scopus 로고    scopus 로고
    • Sulfite induced autoxidation of Ni(II) and Co(II) tetraglycine complexes. Spectrophotometric and rotating ring-disc voltammetric studies
    • M.V. Alipázaga, D. Lowinsohn, M. Bertotti, N. Coichev, Sulfite induced autoxidation of Ni(II) and Co(II) tetraglycine complexes. Spectrophotometric and rotating ring-disc voltammetric studies, Dalton Trans. 2004 (2004) 267-272.
    • (2004) Dalton Trans , vol.2004 , pp. 267-272
    • Alipázaga, M.V.1    Lowinsohn, D.2    Bertotti, M.3    Coichev, N.4
  • 145
  • 146
    • 0000245848 scopus 로고    scopus 로고
    • Complexation of Molybdenum by Siderophores: Synthesis and Structure of the Double-Helical cis-Dioxomolybdenum(VI) Complex of a Bis(catecholamide) Siderophore Analogue
    • A.-K. Duhme, Z. Dauter, R.C. Hider, S. Pohl, Complexation of molybdenum by siderophores: synthesis and structure of the double-helical cisdioxomolybdenum( VI) complex of a bis(catecholamide) siderophore analogue, Inorg. Chem. 35 (1996) 3059-3061. (Pubitemid 126451851)
    • (1996) Inorganic Chemistry , vol.35 , Issue.10 , pp. 3059-3061
    • Duhme, A.-K.1    Dauter, Z.2    Hider, R.C.3    Pohl, S.4
  • 147
    • 0000482996 scopus 로고    scopus 로고
    • Coordination Chemistry of the Amonabactins, Bis(catecholate) Siderophores from Aeromonas hydrophila
    • J.R. Telford, K.N. Raymond, Coordination chemistry of the amonabactins, bis(catecholate) siderophores from Aeromonas hydrophila, Inorg. Chem. 37 (1998) 4578-4583. (Pubitemid 128483093)
    • (1998) Inorganic Chemistry , vol.37 , Issue.18 , pp. 4578-4583
    • Telford, J.R.1    Raymond, K.N.2
  • 149
    • 70349619626 scopus 로고    scopus 로고
    • Role of the siderophore azotobactin in the bacterial acquisition of nitrogenase metal cofactors
    • T. Wichard, J.-P. Bellenger, F.M.M. Morel, A.M.L. Kraepiel, Role of the siderophore azotobactin in the bacterial acquisition of nitrogenase metal cofactors, Environ. Sci. Technol. 43 (2009) 7218-7224.
    • (2009) Environ. Sci. Technol , vol.43 , pp. 7218-7224
    • Wichard, T.1    Bellenger, J.-P.2    Morel, F.M.M.3    Kraepiel, A.M.L.4
  • 150
    • 0033543133 scopus 로고    scopus 로고
    • Determination of nonligand amino acids critical to 4Fe-4S2+/+ assembly in ferredoxin maquettes
    • S.E. Mulholland, B.R. Gibney, F. Rabanal, P. Leslie Dutton, Determination of nonligand amino acids critical to 4Fe-4S2+/+ assembly in ferredoxin maquettes, Biochemistry 38 (1999) 10442-10448.
    • (1999) Biochemistry , vol.38 , pp. 10442-10448
    • Mulholland, S.E.1    Gibney, B.R.2    Rabanal, F.3    Leslie Dutton, P.4
  • 152
    • 0020766701 scopus 로고
    • Synthetic routes to iron-sulphur clusters from the common percursor Fe(SC2H5)42+
    • K. Hagen, A. Watson, R. Holm, Synthetic routes to iron-sulphur clusters from the common precursor Fe(SC2H5)42+, J. Am. Chem. Soc. 105 (1983) 3905-3913.
    • (1983) J. Am. Chem. Soc , vol.105 , pp. 3905-3913
    • Hagen, K.1    Watson, A.2    Holm, R.3
  • 153
    • 0001531848 scopus 로고    scopus 로고
    • Protein control of redox potentials of iron-sulfur proteins
    • P.J. Stephens, D.R. Jollie, A. Warshel, Protein control of redox potentials of iron- sulfur proteins, Chem. Rev. 96 (1996) 2491-2513. (Pubitemid 126641110)
    • (1996) Chemical Reviews , vol.96 , Issue.7 , pp. 2491-2513
    • Stephens, P.J.1    Jollie, D.R.2    Warshel, A.3
  • 155
    • 0029738940 scopus 로고    scopus 로고
    • Novel zinc-binding center in thermoacidophilic archeal ferredoxins
    • T. Fujii, Y. Hata, T. Wakagi, N. Tanaka, T. Oshima, Novel zinc-binding center in thermoacidophilic archeal ferredoxins, Nat. Struct. Biol. 3 (1996) 834.
    • (1996) Nat. Struct. Biol , vol.3 , pp. 834
    • Fujii, T.1    Hata, Y.2    Wakagi, T.3    Tanaka, N.4    Oshima, T.5
  • 156
    • 84868676076 scopus 로고    scopus 로고
    • Interactions of iron-sulfur clusters with small peptides: Insights into early evolution
    • R.P. Hong Enriquez, T.N. Do, Interactions of iron-sulfur clusters with small peptides: insights into early evolution, Comput. Biol. Chem. 41 (2012) 58-61.
    • (2012) Comput. Biol. Chem , vol.41 , pp. 58-61
    • Hong Enriquez, R.P.1    Do, T.N.2
  • 159
    • 0030868605 scopus 로고    scopus 로고
    • Iron-sulfur clusters: Nature's modular, multipurpose structures
    • DOI 10.1126/science.277.5326.653
    • H. Beinert, R.H.Holm, E.Münck, Iron-sulfur clusters:Nature's modular, multipurpose structures, Science 277 (1997) 653-659. (Pubitemid 27373905)
    • (1997) Science , vol.277 , Issue.5326 , pp. 653-659
    • Beinert, H.1    Holm, R.H.2    Munck, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.