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Volumn 1827, Issue 11-12, 2013, Pages 1392-1406

Multiple Rieske/cytb complexes in a single organism

Author keywords

Bioenergetics; Energy conservation; Energy metabolism; Evolution; Quinone; Rieske cytb complex

Indexed keywords

CYTOCHROME B; IRON SULFUR PROTEIN; MANGANESE OXIDE; METHANOL DEHYDROGENASE; NITRATE REDUCTASE; NITRIC OXIDE REDUCTASE; QUINONE DERIVATIVE; SUCCINATE DEHYDROGENASE (UBIQUINONE);

EID: 84884676081     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2013.03.003     Document Type: Review
Times cited : (17)

References (126)
  • 2
    • 0029030987 scopus 로고
    • New archaebacterial genes coding for redox proteins: Implications for the evolution of aerobic metabolism
    • J. Castresana, M. Lübben, and M. Saraste New archaebacterial genes coding for redox proteins: implications for the evolution of aerobic metabolism J. Mol. Biol. 250 1995 202 210
    • (1995) J. Mol. Biol. , vol.250 , pp. 202-210
    • Castresana, J.1    Lübben, M.2    Saraste, M.3
  • 6
    • 0042318835 scopus 로고    scopus 로고
    • 1 complex of the hyperthermophilic Knallgasbacterium Aquifex aeolicus: Properties and phylogenetic relationships
    • DOI 10.1021/bi034452a
    • M. Schütz, B. Schoepp-Cothenet, E. Lojou, M. Woodstra, D. Lexa, P. Tron, A. Dolla, M.-C. Durand, K.O. Stetter, and F. Baymann The naphthoquinol oxidizing cytochrome bc1 complex of the hyperthermophilic knallgasbacterium Aquifex aeolicus: properties and phylogenetic relationships Biochemistry 42 2003 10800 10808 (Pubitemid 37102120)
    • (2003) Biochemistry , vol.42 , Issue.36 , pp. 10800-10808
    • Schutz, M.1    Schoepp-Cothenet, B.2    Lojou, E.3    Woodstra, M.4    Lexa, D.5    Tron, P.6    Dolla, A.7    Durand, M.-C.8    Stetter, K.O.9    Baymann, F.10
  • 8
    • 84857921513 scopus 로고    scopus 로고
    • Back-reactions, short-circuits, leaks and other energy wasteful reactions in biological electron transfer: Redox tuning to survive life in O2
    • A.W. Rutherford, A. Osyczka, and F. Rappaport Back-reactions, short-circuits, leaks and other energy wasteful reactions in biological electron transfer: redox tuning to survive life in O2 FEBS Lett. 586 2012 603 616
    • (2012) FEBS Lett. , vol.586 , pp. 603-616
    • Rutherford, A.W.1    Osyczka, A.2    Rappaport, F.3
  • 9
    • 0013593621 scopus 로고
    • The function of menaquinone in bacterial electron transport
    • G. Lenaz, John Wiley and Sons Ltd. New York (Chichester [West Sussex])
    • A. Kröger, and G. Unden The function of menaquinone in bacterial electron transport G. Lenaz, Coenzyme Q: Biochemistry, Bioenergetics, and Clinical Applications of Ubiquinone 1985 John Wiley and Sons Ltd. New York 285 300 (Chichester [West Sussex])
    • (1985) Coenzyme Q: Biochemistry, Bioenergetics, and Clinical Applications of Ubiquinone , pp. 285-300
    • Kröger, A.1    Unden, G.2
  • 10
    • 0016751399 scopus 로고
    • Polarographic studies on ubiquinone-10 and rhodoquinone bound with chromatophores from Rhodospirillum rubrum
    • T. Erabi, T. Higuti, T. Kakuno, J. Yamashita, M. Tanaka, and T. Horio Polarographic studies on ubiquinone-10 and rhodoquinone bound with chromatophores from Rhodospirillum rubrum J. Biochem. 78 1975 795 801
    • (1975) J. Biochem. , vol.78 , pp. 795-801
    • Erabi, T.1    Higuti, T.2    Kakuno, T.3    Yamashita, J.4    Tanaka, M.5    Horio, T.6
  • 12
    • 84865978841 scopus 로고    scopus 로고
    • On the function of the various quinone species in Escherichia coli
    • P. Sharma, M.J. Teixeira de Mattos, K.J. Hellingwerf, and M. Bekker On the function of the various quinone species in Escherichia coli FEBS J. 279 2012 3364 3373
    • (2012) FEBS J. , vol.279 , pp. 3364-3373
    • Sharma, P.1    Teixeira De Mattos, M.J.2    Hellingwerf, K.J.3    Bekker, M.4
  • 13
    • 0014303481 scopus 로고
    • Effect of anaerobiosis on the concentrations of demethylmenaquinone, menaquinone and ubiquinone in Escherichia freundii, Proteus mirabilis and Aeromonas punctata
    • G. Whistance, and D. Threlfall Effect of anaerobiosis on the concentrations of demethylmenaquinone, menaquinone and ubiquinone in Escherichia freundii, Proteus mirabilis and Aeromonas punctata Biochem. J. 108 1968 3
    • (1968) Biochem. J. , vol.108 , pp. 3
    • Whistance, G.1    Threlfall, D.2
  • 14
    • 77957276541 scopus 로고    scopus 로고
    • Aquifex aeolicus membrane hydrogenase for hydrogen biooxidation: Role of lipids and physiological partners in enzyme stability and activity
    • P. Infossi, E. Lojou, J.-P. Chauvin, G. Herbette, M. Brugna, and M.-T. Giudici-Orticoni Aquifex aeolicus membrane hydrogenase for hydrogen biooxidation: role of lipids and physiological partners in enzyme stability and activity Int. J. Hydrogen Energy 35 2010 10778 10789
    • (2010) Int. J. Hydrogen Energy , vol.35 , pp. 10778-10789
    • Infossi, P.1    Lojou, E.2    Chauvin, J.-P.3    Herbette, G.4    Brugna, M.5    Giudici-Orticoni, M.-T.6
  • 15
    • 34250346936 scopus 로고    scopus 로고
    • Biochemical studies of Klebsiella pneumoniae NifL reduction using reconstituted partial anaerobic respiratory chains of Wolinella succinogenes
    • DOI 10.1074/jbc.M609826200
    • R. Thummer, O. Klimmek, and R.A. Schmitz Biochemical studies of Klebsiella pneumoniae NifL reduction using reconstituted partial anaerobic respiratory chains of Wolinella succinogenes J. Biol. Chem. 282 2007 12517 12526 (Pubitemid 47100626)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.17 , pp. 12517-12526
    • Thummer, R.1    Klimmek, O.2    Schmitz, R.A.3
  • 16
    • 0021827070 scopus 로고
    • Structure of thermoplasmaquinone from Thermoplasma acidophilum
    • DOI 10.1016/0378-1097(85)90209-5
    • M.D. Collins Structure of thermoplasmaquinone from Thermoplasma acidophilum FEMS Microbiol. Lett. 28 1985 21 23 (Pubitemid 15013540)
    • (1985) FEMS Microbiology Letters , vol.28 , Issue.1 , pp. 21-23
    • Collins, M.D.1
  • 17
    • 84947532410 scopus 로고
    • Quinones from archaebacteria, II. Different types of quinones from sulphur-dependent archaebacteria
    • S. Thurl, W. Witke, I. Buhrow, and W. Schäfer Quinones from archaebacteria, II. Different types of quinones from sulphur-dependent archaebacteria Biol. Chem. Hoppe Seyler 367 1986 7
    • (1986) Biol. Chem. Hoppe Seyler , vol.367 , pp. 7
    • Thurl, S.1    Witke, W.2    Buhrow, I.3    Schäfer, W.4
  • 18
    • 0023202759 scopus 로고
    • 2-methylthio- 1,4-naphtoquinone, a unique sulfur-containing quinone from a thermophilic hydrogen-oxidizing bacterium, Hydrogenobacter thermophilus
    • M. Ishii, T. Kawasumi, Y. Igarashi, T. Kodama, and Y. Minoda 2-Methylthio-1,4-naphthoquinone, a unique sulfur-containing quinone from a thermophilic hydrogen-oxidizing bacterium, Hydrogenobacter thermophilus J. Bacteriol. 169 1987 2380 2384 (Pubitemid 17104291)
    • (1987) Journal of Bacteriology , vol.169 , Issue.6 , pp. 2380-2384
    • Ishil, M.1    Kawasumi, T.2    Igarashi, Y.3
  • 19
    • 0032502711 scopus 로고    scopus 로고
    • Alteration of the midpoint potential and catalytic activity of the Rieske iron-sulfur protein by changes of amino acids forming hydrogen bonds to the iron-sulfur cluster
    • DOI 10.1074/jbc.273.15.9085
    • E. Denke, T. Merbitz-Zahradnik, O.M. Hatzfeld, C.H. Snyder, T.A. Link, and B.L. Trumpower Alteration of the midpoint potential and catalytic activity of the Rieske iron-sulfur protein by changes of amino acids forming hydrogen bonds to the iron-sulfur cluster J. Biol. Chem. 273 1998 9085 9093 (Pubitemid 28176197)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.15 , pp. 9085-9093
    • Denke, E.1    Merbitz-Zahradnik, T.2    Hatzfeld, O.M.3    Snyder, C.H.4    Link, T.A.5    Trumpower, B.L.6
  • 23
    • 0019490792 scopus 로고
    • Distribution of isoprenoid quinone structural types in bacteria and their taxonomic implication
    • M.D. Collins, and D. Jones Distribution of isoprenoid quinone structural types in bacteria and their taxonomic implication Microbiol. Rev. 45 1981 9
    • (1981) Microbiol. Rev. , vol.45 , pp. 9
    • Collins, M.D.1    Jones, D.2
  • 24
    • 0021682230 scopus 로고
    • Quinones of phototrophic purple bacteria
    • DOI 10.1016/0378-1097(84)90052-1
    • J.F. Imhoff Quinones of phototrophic purple bacteria FEMS Microbiol. Lett. 25 1984 85 89 (Pubitemid 15217305)
    • (1984) FEMS Microbiology Letters , vol.25 , Issue.1 , pp. 85-89
    • Imhoff, J.F.1
  • 26
    • 0014409302 scopus 로고
    • Roles of ubiquinone-10 and rhodoquinone in photosynthetic formation of adenosine triphosphate by chromatophores from Rhodospirillum rubrum
    • S. Okayama, N. Yamamoto, K. Nishikawa, and T. Horio Roles of ubiquinone-10 and rhodoquinone in photosynthetic formation of adenosine triphosphate by chromatophores from Rhodospirillum rubrum J. Biol. Chem. 243 1968 2995 2999
    • (1968) J. Biol. Chem. , vol.243 , pp. 2995-2999
    • Okayama, S.1    Yamamoto, N.2    Nishikawa, K.3    Horio, T.4
  • 27
    • 33846326537 scopus 로고    scopus 로고
    • 1 complexes in the strict acidophilic chemolithoautotrophic bacterium Acidithiobacillus ferrooxidans suggests a model for their respective roles in iron or sulfur oxidation
    • DOI 10.1099/mic.0.2006/000067-0
    • P. Bruscella, C. Appia-Ayme, G. Levican, J. Ratouchniak, E. Jedlicki, D.S. Holmes, and V. Bonnefoy Differential expression of two bc1 complexes in the strict acidophilic chemolithoautotrophic bacterium Acidithiobacillus ferrooxidans suggests a model for their respective roles in iron or sulfur oxidation Microbiology 153 2007 102 110 (Pubitemid 46111825)
    • (2007) Microbiology , vol.153 , Issue.1 , pp. 102-110
    • Bruscella, P.1    Appia-Ayme, C.2    Levican, G.3    Ratouchniak, J.4    Jedlicki, E.5    Holmes, D.S.6    Bonnefoy, V.7
  • 29
    • 0035085306 scopus 로고    scopus 로고
    • Respiratory enzymes from Sulfolobus acidocaldarius
    • DOI 10.1016/S0076-6879(01)31071-6
    • G. Schafer, R. Moll, and C.L. Schmidt Respiratory enzymes from Sulfolobus acidocaldarius Methods Enzymol. 331 2001 369 410 (Pubitemid 32242361)
    • (2001) Methods in Enzymology , vol.331 , pp. 369-410
    • Schafer, G.1    Moll, R.2    Schmidt, C.L.3
  • 30
    • 0040984441 scopus 로고    scopus 로고
    • On the origin of respiration: Electron transport proteins from archaea to man
    • DOI 10.1016/0168-6445(96)00010-1
    • G. Schafer, W. Purschke, and C.L. Schmidt On the origin of respiration: electron transport proteins from archaea to man FEMS Microbiol. Rev. 18 1996 173 188 (Pubitemid 26184691)
    • (1996) FEMS Microbiology Reviews , vol.18 , Issue.2-3 , pp. 173-188
    • Schafer, G.1    Purschke, W.2    Schmidt, C.L.3
  • 32
    • 13444260030 scopus 로고    scopus 로고
    • Respiratory gene clusters of Metallosphaera sedula - Differential expression and transcriptional organization
    • DOI 10.1099/mic.0.27515-0
    • U. Kappler, L.I. Sly, and A.G. McEwan Respiratory gene clusters of Metallosphaera sedula - differential expression and transcriptional organization Microbiology 151 2005 35 43 (Pubitemid 40207667)
    • (2005) Microbiology , vol.151 , Issue.1 , pp. 35-43
    • Kappler, U.1    Sly, L.I.2    McEwan, A.G.3
  • 34
    • 79952996497 scopus 로고    scopus 로고
    • Seasonal dynamics of anammox bacteria in estuarial sediment of the Mai Po Nature Reserve revealed by analyzing the 16S rRNA and hydrazine oxidoreductase (hzo) genes
    • M. Li, H. Cao, Y.G. Hong, and J.D. Gu Seasonal dynamics of anammox bacteria in estuarial sediment of the Mai Po Nature Reserve revealed by analyzing the 16S rRNA and hydrazine oxidoreductase (hzo) genes Microbes Environ. 26 2011 15 22
    • (2011) Microbes Environ. , vol.26 , pp. 15-22
    • Li, M.1    Cao, H.2    Hong, Y.G.3    Gu, J.D.4
  • 37
    • 84555194881 scopus 로고    scopus 로고
    • Complete genome of Leptospirillum ferriphilum ML-04 provides insight into its physiology and environmental adaptation
    • S. Mi, J. Song, J. Lin, Y. Che, H. Zheng, and J. Lin Complete genome of Leptospirillum ferriphilum ML-04 provides insight into its physiology and environmental adaptation J. Microbiol. 49 2011 890 901
    • (2011) J. Microbiol. , vol.49 , pp. 890-901
    • Mi, S.1    Song, J.2    Lin, J.3    Che, Y.4    Zheng, H.5    Lin, J.6
  • 38
    • 84855283899 scopus 로고    scopus 로고
    • Complete genome of Candidatus Chloracidobacterium thermophilum, a chlorophyll-based photoheterotroph belonging to the phylum Acidobacteria
    • A.M. Garcia Costas, Z. Liu, L.P. Tomsho, S.C. Schuster, D.M. Ward, and D.A. Bryant Complete genome of Candidatus Chloracidobacterium thermophilum, a chlorophyll-based photoheterotroph belonging to the phylum Acidobacteria Environ. Microbiol. 14 2012 177 190
    • (2012) Environ. Microbiol. , vol.14 , pp. 177-190
    • Garcia Costas, A.M.1    Liu, Z.2    Tomsho, L.P.3    Schuster, S.C.4    Ward, D.M.5    Bryant, D.A.6
  • 42
    • 70350454746 scopus 로고    scopus 로고
    • Multiple Rieske proteins enable short- and long-term light adaptation of Synechocystis sp. PCC 6803
    • Y. Tsunoyama, G. Bernát, N.G. Dyczmons, D. Schneider, and M. Rögner Multiple Rieske proteins enable short- and long-term light adaptation of Synechocystis sp. PCC 6803 J. Biol. Chem. 284 2009 27875 27883
    • (2009) J. Biol. Chem. , vol.284 , pp. 27875-27883
    • Tsunoyama, Y.1    Bernát, G.2    Dyczmons, N.G.3    Schneider, D.4    Rögner, M.5
  • 43
    • 21244461968 scopus 로고    scopus 로고
    • 1-complex of Rubrivivax gelatinosus
    • DOI 10.1111/j.1365-2958.2005.04685.x
    • S. Ouchane, W. Nitschke, P. Bianco, A. Vermeglio, and C. Astier Multiple Rieske genes in prokaryotes: exchangeable Rieske subunits in the cytochrome bc1-complex of Rubrivivax gelatinosus Mol. Microbiol. 57 2005 261 275 (Pubitemid 40896613)
    • (2005) Molecular Microbiology , vol.57 , Issue.1 , pp. 261-275
    • Ouchane, S.1    Nitschke, W.2    Bianco, P.3    Vermeglio, A.4    Astier, C.5
  • 44
    • 78751664531 scopus 로고    scopus 로고
    • Characterization of two cytochrome b6 proteins from the cyanobacterium Gloeobacter violaceus PCC 7421
    • C. Dreher, R. Hielscher, A. Prodöhl, P. Hellwig, and D. Schneider Characterization of two cytochrome b6 proteins from the cyanobacterium Gloeobacter violaceus PCC 7421 J. Bioenerg. Biomembr. 42 2010 517 526
    • (2010) J. Bioenerg. Biomembr. , vol.42 , pp. 517-526
    • Dreher, C.1    Hielscher, R.2    Prodöhl, A.3    Hellwig, P.4    Schneider, D.5
  • 45
    • 0037056056 scopus 로고    scopus 로고
    • 1 complex?
    • DOI 10.1016/S0005-2728(02)00251-7, PII S0005272802002517
    • G. Brasseur, P. Bruscella, V. Bonnefoy, and D. Lemesle-Meunier The bc(1) complex of the iron-grown acidophilic chemolithotrophic bacterium Acidithiobacillus ferrooxidans functions in the reverse but not in the forward direction. Is there a second bc(1) complex? Biochim. Biophys. Acta 1555 2002 37 43 (Pubitemid 35246002)
    • (2002) Biochimica et Biophysica Acta - Bioenergetics , vol.1555 , Issue.1-3 , pp. 37-43
    • Brasseur, G.1    Bruscella, P.2    Bonnefoy, V.3    Lemesle-Meunier, D.4
  • 46
    • 0033546326 scopus 로고    scopus 로고
    • Redox components of cytochrome bc-type enzymes in acidophilic prokaryotes. I. Characterization of the cytochrome bc1-type complex of the acidophilic ferrous ion-oxidizing bacterium Thiobacillus ferrooxidans
    • A. Elbehti, W. Nitschke, P. Tron, C. Michel, and D. Lemesle-Meunier Redox components of cytochrome bc-type enzymes in acidophilic prokaryotes. I. Characterization of the cytochrome bc1-type complex of the acidophilic ferrous ion-oxidizing bacterium Thiobacillus ferrooxidans J. Biol. Chem. 274 1999 16760 16765
    • (1999) J. Biol. Chem. , vol.274 , pp. 16760-16765
    • Elbehti, A.1    Nitschke, W.2    Tron, P.3    Michel, C.4    Lemesle-Meunier, D.5
  • 47
    • 0033546142 scopus 로고    scopus 로고
    • Redox components of cytochrome bc-type enzymes in acidophilic prokaryotes. II. The Rieske protein of phylogenetically distant acidophilic organisms
    • M. Brugna, W. Nitschke, M. Asso, B. Guigliarelli, D. Lemesle-Meunier, and C. Schmidt Redox components of cytochrome bc-type enzymes in acidophilic prokaryotes. II. The Rieske protein of phylogenetically distant acidophilic organisms J. Biol. Chem. 274 1999 16766 16772
    • (1999) J. Biol. Chem. , vol.274 , pp. 16766-16772
    • Brugna, M.1    Nitschke, W.2    Asso, M.3    Guigliarelli, B.4    Lemesle-Meunier, D.5    Schmidt, C.6
  • 49
    • 0001102644 scopus 로고    scopus 로고
    • The archaeal SoxABCD complex is a proton pump in Sulfolobus acidocaldarius
    • DOI 10.1074/jbc.272.13.8417
    • M. Gleissner, U. Kaiser, E. Antonopoulos, and G. Schäfer The archaeal SoxABCD complex is a proton pump in Sulfolobus acidocaldarius J. Biol. Chem. 272 1997 8417 8426 (Pubitemid 27147802)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.13 , pp. 8417-8426
    • Gleissner, M.1    Kaiser, U.2    Antonopoulos, E.3    Schafer, G.4
  • 50
    • 0030273881 scopus 로고    scopus 로고
    • 562 in the archaeal aerobic respiratory chain of Sulfolobus sp. Strain 7
    • DOI 10.1016/0378-1097(96)00372-2
    • T. Iwasaki, and T. Oshima Role of cytochrome b562 in the archaeal aerobic respiratory chain of Sulfolobus sp. strain 7 FEMS Microbiol. Lett. 144 1996 259 266 (Pubitemid 26354337)
    • (1996) FEMS Microbiology Letters , vol.144 , Issue.2-3 , pp. 259-266
    • Iwasaki, T.1    Oshima, T.2
  • 51
    • 0029603607 scopus 로고
    • Resolution of the aerobic respiratory system of the thermoacidophilic archaeon, Sulfolobus sp. Strain 7. II. Characterization of the archaeal terminal oxidase subcomplexes and implication for the intramolecular electron transfer
    • T. Iwasaki, T. Wakagi, Y. Isogai, T. Iizuka, and T. Oshima Resolution of the aerobic respiratory system of the thermoacidophilic archaeon, Sulfolobus sp. strain 7. II. Characterization of the archaeal terminal oxidase subcomplexes and implication for the intramolecular electron transfer J. Biol. Chem. 270 1995 30893 30901
    • (1995) J. Biol. Chem. , vol.270 , pp. 30893-30901
    • Iwasaki, T.1    Wakagi, T.2    Isogai, Y.3    Iizuka, T.4    Oshima, T.5
  • 52
    • 0035808241 scopus 로고    scopus 로고
    • Sulfocyanin and subunit II, two copper proteins with novel features, provide new insight into the archaeal SoxM oxidase supercomplex
    • DOI 10.1016/S0014-5793(00)02343-7, PII S0014579300023437
    • L. Komorowski, and G. Schäfer Sulfocyanin and subunit II, two copper proteins with novel features, provide new insight into the archaeal SoxM oxidase supercomplex FEBS Lett. 487 2001 351 355 (Pubitemid 32121755)
    • (2001) FEBS Letters , vol.487 , Issue.3 , pp. 351-355
    • Komorowski, L.1    Schafer, G.2
  • 54
    • 0026563750 scopus 로고
    • An archaebacterial terminal oxidase combines core structures of two mitochondrial respiratory complexes
    • M. Lübben, B. Kolmerer, and M. Saraste An archaebacterial terminal oxidase combines core structures of two mitochondrial respiratory complexes EMBO J. 11 1992 805 812
    • (1992) EMBO J. , vol.11 , pp. 805-812
    • Lübben, M.1    Kolmerer, B.2    Saraste, M.3
  • 55
    • 0028339618 scopus 로고
    • The purified SoxABCD quinol oxidase complex of Sulfolobus acidocaldarius contains a novel haem
    • DOI 10.1111/j.1365-2958.1994.tb00426.x
    • M. Lübben, A. Warne, S.P. Albracht, and M. Saraste The purified SoxABCD quinol oxidase complex of Sulfolobus acidocaldarius contains a novel haem Mol. Microbiol. 13 1994 327 335 (Pubitemid 24225503)
    • (1994) Molecular Microbiology , vol.13 , Issue.2 , pp. 327-335
    • Lubben, M.1    Warne, A.2    Albracht, S.P.J.3    Saraste, M.4
  • 56
    • 13444307911 scopus 로고    scopus 로고
    • Rieske Iron-Sulfur Proteins from Extremophilic Organisms
    • DOI 10.1023/B:JOBB.0000019602.96578.78
    • C.L. Schmidt Rieske iron-sulfur proteins from extremophilic organisms J. Bioenerg. Biomembr. 36 2004 107 113 (Pubitemid 38500764)
    • (2004) Journal of Bioenergetics and Biomembranes , vol.36 , Issue.1 , pp. 107-113
    • Schmidt, C.L.1
  • 57
    • 0028821539 scopus 로고
    • Purification and characterization of the Rieske iron-sulfur protein from the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius
    • C.L. Schmidt, S. Anemüller, M. Teixeira, and G. Schäfer Purification and characterization of the Rieske iron-sulfur protein from the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius FEBS Lett. 359 1995 239 243
    • (1995) FEBS Lett. , vol.359 , pp. 239-243
    • Schmidt, C.L.1    Anemüller, S.2    Teixeira, M.3    Schäfer, G.4
  • 58
    • 0242494128 scopus 로고    scopus 로고
    • 6f Complex of Oxygenic Photosynthesis: Tuning the Cavity
    • DOI 10.1126/science.1090165
    • G. Kurisu, H. Zhang, J.L. Smith, and W.A. Cramer Structure of the cytochrome b6f complex of oxygenic photosynthesis: tuning the cavity Science 302 2003 1009 1014 (Pubitemid 37386186)
    • (2003) Science , vol.302 , Issue.5647 , pp. 1009-1014
    • Kurisu, G.1    Zhang, H.2    Smith, J.L.3    Cramer, W.A.4
  • 59
    • 0344497439 scopus 로고    scopus 로고
    • 6f complex
    • DOI 10.1038/nature02155
    • D. Stroebel, Y. Choquet, J.-L. Popot, and D. Picot An atypical haem in the cytochrome b6f complex Nature 426 2003 413 418 (Pubitemid 37490123)
    • (2003) Nature , vol.426 , Issue.6965 , pp. 413-418
    • Stroebel, D.1    Choquet, Y.2    Popot, J.-L.3    Picot, D.4
  • 60
    • 0032502756 scopus 로고    scopus 로고
    • Studies of the cytochrome subunits of menaquinone: Cytochrome c reductase (bc complex) of Bacillus subtilis
    • J. Yu, and N.E. Le Brun Studies of the cytochrome subunits of menaquinone:cytochrome c reductase (bc complex) of Bacillus subtilis J. Biol. Chem. 273 1998 8860 8866
    • (1998) J. Biol. Chem. , vol.273 , pp. 8860-8866
    • Yu, J.1    Le Brun, N.E.2
  • 62
    • 0027216025 scopus 로고
    • Chemotaxonomic investigation of various prosthecate and/or budding bacteria
    • M. Sittig, and H. Schlesner Chemotaxonomic investigation of various prosthecate and/or budding bacteria Syst. Appl. Microbiol. 16 1993 92 103 (Pubitemid 23152366)
    • (1993) Systematic and Applied Microbiology , vol.16 , Issue.1 , pp. 92-103
    • Sittig, M.1    Schlesner, H.2
  • 63
    • 0042812120 scopus 로고    scopus 로고
    • Gemmatimonas aurantiaca gen. Nov., sp. Nov., a Gram-negative, aerobic, polyphosphate-accumulating micro-organism, the first cultured representative of the new bacterial phylum Gemmatimonadetes phyl. Nov
    • DOI 10.1099/ijs.0.02520-0
    • H. Zhang, Y. Sekiguchi, S. Hanada, P. Hugenholtz, H. Kim, Y. Kamagata, and K. Nakamura Gemmatimonas aurantiaca gen. nov., sp. nov., a Gram-negative, aerobic, polyphosphate-accumulating micro-organism, the first cultured representative of the new bacterial phylum Gemmatimonadetes phyl. nov Int. J. Syst. Evol. Microbiol. 53 2003 1155 1163 (Pubitemid 36896531)
    • (2003) International Journal of Systematic and Evolutionary Microbiology , vol.53 , Issue.4 , pp. 1155-1163
    • Zhang, H.1    Sekiguchi, Y.2    Hanada, S.3    Hugenholtz, P.4    Kim, H.5    Kamagata, Y.6    Nakamura, K.7
  • 64
    • 84864703501 scopus 로고    scopus 로고
    • The alternative complex III: Properties and possible mechanisms for electron transfer and energy conservation
    • P.N. Refojo, M. Teixeira, and M.M. Pereira The alternative complex III: Properties and possible mechanisms for electron transfer and energy conservation Biochim. Biophys. Acta Bioenerg. 1817 2012 1852 1859
    • (2012) Biochim. Biophys. Acta Bioenerg. , vol.1817 , pp. 1852-1859
    • Refojo, P.N.1    Teixeira, M.2    Pereira, M.M.3
  • 65
    • 18144382963 scopus 로고    scopus 로고
    • Anaerobic ammonium oxidation (anammox) in the marine environment
    • DOI 10.1016/j.resmic.2005.01.011
    • T. Dalsgaard, B. Thamdrup, and D.E. Canfield Anaerobic ammonium oxidation (anammox) in the marine environment Res. Microbiol. 156 2005 457 464 (Pubitemid 40615411)
    • (2005) Research in Microbiology , vol.156 , Issue.4 , pp. 457-464
    • Dalsgaard, T.1    Thamdrup, B.2    Canfield, D.E.3
  • 66
    • 23844470172 scopus 로고    scopus 로고
    • Structural identification of ladderane and other membrane lipids of planctomycetes capable of anaerobic ammonium oxidation (anammox)
    • DOI 10.1111/j.1742-4658.2005.04842.x
    • J.S. Sinninghe Damsté, W.I.C. Rijpstra, J.A.J. Geenevasen, M. Strous, and M.S.M. Jetten Structural identification of ladderane and other membrane lipids of planctomycetes capable of anaerobic ammonium oxidation (anammox) FEBS J. 272 2005 4270 4283 (Pubitemid 41160932)
    • (2005) FEBS Journal , vol.272 , Issue.16 , pp. 4270-4283
    • Sinninghe Damste, J.S.1    Rijpstra, W.I.C.2    Geenevasen, J.A.J.3    Strous, M.4    Jetten, M.S.M.5
  • 67
    • 38749146551 scopus 로고    scopus 로고
    • Linking ultrastructure and function in four genera of anaerobic ammonium-oxidizing bacteria: Cell plan, glycogen storage, and localization of cytochrome c proteins
    • DOI 10.1128/JB.01449-07
    • L. van Niftrik, W.J. Geerts, E.G. van Donselaar, B.M. Humbel, R.I. Webb, J.A. Fuerst, A.J. Verkleij, M.S. Jetten, and M. Strous Linking ultrastructure and function in four genera of anaerobic ammonium-oxidizing bacteria: cell plan, glycogen storage, and localization of cytochrome C proteins J. Bacteriol. 190 2008 708 717 (Pubitemid 351360087)
    • (2008) Journal of Bacteriology , vol.190 , Issue.2 , pp. 708-717
    • Van Niftrik, L.1    Geerts, W.J.C.2    Van Donselaar, E.G.3    Humbel, B.M.4    Webb, R.I.5    Fuerst, J.A.6    Verkleij, A.J.7    Jetten, M.S.M.8    Strous, M.9
  • 69
    • 0029820117 scopus 로고    scopus 로고
    • Autotrophic growth of anaerobic ammonium-oxidizing micro-organisms in a fluidized bed reactor
    • A.A. van de Graaf, P. de Bruijn, L.A. Robertson, M.S.M. Jetten, and J.G. Kuenen Autotrophic growth of anaerobic ammonium-oxidizing micro-organisms in a fluidized bed reactor Microbiology 142 1996 2187 2196 (Pubitemid 26288094)
    • (1996) Microbiology , vol.142 , Issue.8 , pp. 2187-2196
    • Van De Graaf, A.A.1    De Bruijn, P.2    Robertson, L.A.3    Jetten, M.S.M.4    Kuenen, J.G.5
  • 70
    • 79551491148 scopus 로고    scopus 로고
    • Proteins and protein complexes involved in the biochemical reactions of anaerobic ammonium-oxidizing bacteria
    • N.M. de Almeida, W.J. Maalcke, J.T. Keltjens, M.S. Jetten, and B. Kartal Proteins and protein complexes involved in the biochemical reactions of anaerobic ammonium-oxidizing bacteria Biochem. Soc. Trans. 39 2011 303 308
    • (2011) Biochem. Soc. Trans. , vol.39 , pp. 303-308
    • De Almeida, N.M.1    Maalcke, W.J.2    Keltjens, J.T.3    Jetten, M.S.4    Kartal, B.5
  • 72
    • 81855198129 scopus 로고    scopus 로고
    • The ultrastructure of the compartmentalized anaerobic ammonium-oxidizing bacteria is linked to their energy metabolism
    • S. Neumann, M.S. Jetten, and L. van Niftrik The ultrastructure of the compartmentalized anaerobic ammonium-oxidizing bacteria is linked to their energy metabolism Biochem. Soc. Trans. 39 2011 1805 1810
    • (2011) Biochem. Soc. Trans. , vol.39 , pp. 1805-1810
    • Neumann, S.1    Jetten, M.S.2    Van Niftrik, L.3
  • 73
    • 84871720360 scopus 로고    scopus 로고
    • Diversity and evolution of bioenergetic systems involved in microbial nitrogen compound transformations
    • J. Simon, and M.G. Klotz Diversity and evolution of bioenergetic systems involved in microbial nitrogen compound transformations Biochim. Biophys. Acta 1827 2013 114 137
    • (2013) Biochim. Biophys. Acta , vol.1827 , pp. 114-137
    • Simon, J.1    Klotz, M.G.2
  • 78
    • 79551492715 scopus 로고    scopus 로고
    • Physiological role of the respiratory quinol oxidase in the anaerobic nitrite-reducing methanotroph 'Candidatus Methylomirabilis oxyfera'
    • M.L. Wu, S. de Vries, T.A. van Alen, M.K. Butler, H.J. Op den Camp, J.T. Keltjens, M.S. Jetten, and M. Strous Physiological role of the respiratory quinol oxidase in the anaerobic nitrite-reducing methanotroph 'Candidatus Methylomirabilis oxyfera' Microbiology 157 2011 890 898
    • (2011) Microbiology , vol.157 , pp. 890-898
    • Wu, M.L.1    De Vries, S.2    Van Alen, T.A.3    Butler, M.K.4    Op Den Camp, H.J.5    Keltjens, J.T.6    Jetten, M.S.7    Strous, M.8
  • 79
    • 79551503528 scopus 로고    scopus 로고
    • A new intra-aerobic metabolism in the nitrite-dependent anaerobic methane-oxidizing bacterium Candidatus 'Methylomirabilis oxyfera'
    • M.L. Wu, K.F. Ettwig, M.S. Jetten, M. Strous, J.T. Keltjens, and L. van Niftrik A new intra-aerobic metabolism in the nitrite-dependent anaerobic methane-oxidizing bacterium Candidatus 'Methylomirabilis oxyfera' Biochem. Soc. Trans. 39 2011 243 248
    • (2011) Biochem. Soc. Trans. , vol.39 , pp. 243-248
    • Wu, M.L.1    Ettwig, K.F.2    Jetten, M.S.3    Strous, M.4    Keltjens, J.T.5    Van Niftrik, L.6
  • 80
    • 0025277145 scopus 로고
    • Evidence for electron transfer via ubiquinone between quinoproteins D-glucose dehydrogenase and alcohol dehydrogenase of Gluconobacter suboxydans
    • E. Shinagawa, K. Matsushita, O. Adachi, and M. Ameyama Evidence for electron transfer via ubiquinone between quinoproteins d-glucose dehydrogenase and alcohol dehydrogenase of Gluconobacter suboxydans J. Biochem. 107 1990 863 867 (Pubitemid 20186299)
    • (1990) Journal of Biochemistry , vol.107 , Issue.6 , pp. 863-867
    • Shinagawa, E.1    Matsushita, K.2    Adachi, O.3    Ameyama, M.4
  • 81
    • 84857885821 scopus 로고    scopus 로고
    • Identification of the bacteriochlorophylls, carotenoids, quinones, lipids, and hopanoids of "candidatus Chloracidobacterium thermophilum"
    • A.M. Garcia Costas, Y. Tsukatani, W.I. Rijpstra, S. Schouten, P.V. Welander, R.E. Summons, and D.A. Bryant Identification of the bacteriochlorophylls, carotenoids, quinones, lipids, and hopanoids of "Candidatus Chloracidobacterium thermophilum" J. Bacteriol. 194 2012 1158 1168
    • (2012) J. Bacteriol. , vol.194 , pp. 1158-1168
    • Garcia Costas, A.M.1    Tsukatani, Y.2    Rijpstra, W.I.3    Schouten, S.4    Welander, P.V.5    Summons, R.E.6    Bryant, D.A.7
  • 83
    • 78650071259 scopus 로고    scopus 로고
    • Granulicella paludicola gen. Nov., sp. Nov., Granulicella pectinivorans sp. Nov., Granulicella aggregans sp. Nov. and Granulicella rosea sp. Nov., acidophilic, polymer-degrading acidobacteria from Sphagnum peat bogs
    • T.A. Pankratov, and S.N. Dedysh Granulicella paludicola gen. nov., sp. nov., Granulicella pectinivorans sp. nov., Granulicella aggregans sp. nov. and Granulicella rosea sp. nov., acidophilic, polymer-degrading acidobacteria from Sphagnum peat bogs Int. J. Syst. Evol. Microbiol. 60 2010 2951 2959
    • (2010) Int. J. Syst. Evol. Microbiol. , vol.60 , pp. 2951-2959
    • Pankratov, T.A.1    Dedysh, S.N.2
  • 85
    • 80052851351 scopus 로고    scopus 로고
    • Biological consequences of ancient gene acquisition and duplication in the large genome of Candidatus Solibacter usitatus Ellin6076
    • J.F. Challacombe, S.A. Eichorst, L. Hauser, M. Land, G. Xie, and C.R. Kuske Biological consequences of ancient gene acquisition and duplication in the large genome of Candidatus Solibacter usitatus Ellin6076 PLoS One 6 2011 e24882
    • (2011) PLoS One , vol.6 , pp. 24882
    • Challacombe, J.F.1    Eichorst, S.A.2    Hauser, L.3    Land, M.4    Xie, G.5    Kuske, C.R.6
  • 86
    • 0344573100 scopus 로고    scopus 로고
    • Evidence for a chemiosmotic model of dehalorespiration in Desulfomonile tiedjei DCB-1
    • T.M. Louie, and W.W. Mohn Evidence for a chemiosmotic model of dehalorespiration in Desulfomonile tiedjei DCB-1 J. Bacteriol. 181 1999 40 46 (Pubitemid 29013651)
    • (1999) Journal of Bacteriology , vol.181 , Issue.1 , pp. 40-46
    • Louie, T.M.1    Mohn, W.W.2
  • 87
    • 59449094426 scopus 로고    scopus 로고
    • Polar lipid fatty acids, LPS-hydroxy fatty acids, and respiratory quinones of three Geobacter strains, and variation with electron acceptor
    • D. Hedrick, A. Peacock, D. Lovley, T. Woodard, K. Nevin, P. Long, and D. White Polar lipid fatty acids, LPS-hydroxy fatty acids, and respiratory quinones of three Geobacter strains, and variation with electron acceptor J. Ind. Microbiol. Biotechnol. 36 2009 205 209
    • (2009) J. Ind. Microbiol. Biotechnol. , vol.36 , pp. 205-209
    • Hedrick, D.1    Peacock, A.2    Lovley, D.3    Woodard, T.4    Nevin, K.5    Long, P.6    White, D.7
  • 88
    • 3843070019 scopus 로고    scopus 로고
    • Geobacter sulfurreducens Can Grow with Oxygen as a Terminal Electron Acceptor
    • DOI 10.1128/AEM.70.4.2525-2528.2004
    • W.C. Lin, M.V. Coppi, and D.R. Lovley Geobacter sulfurreducens can grow with oxygen as a terminal electron acceptor Appl. Environ. Microbiol. 70 2004 2525 2528 (Pubitemid 38500561)
    • (2004) Applied and Environmental Microbiology , vol.70 , Issue.4 , pp. 2525-2528
    • Lin, W.C.1    Coppi, M.V.2    Lovley, D.R.3
  • 89
    • 36549003122 scopus 로고    scopus 로고
    • Steady state protein levels in Geobacter metallireducens grown with iron (III) citrate or nitrate as terminal electron acceptor
    • DOI 10.1002/pmic.200600955
    • A.J. Ahrendt, S.L. Tollaksen, C. Lindberg, W. Zhu, J.R. Yates III, K.P. Nevin, G. Babnigg, D.R. Lovley, and C.S. Giometti Steady state protein levels in Geobacter metallireducens grown with iron (III) citrate or nitrate as terminal electron acceptor Proteomics 7 2007 4148 4157 (Pubitemid 350190286)
    • (2007) Proteomics , vol.7 , Issue.22 , pp. 4148-4157
    • Ahrendt, A.J.1    Tollaksen, S.L.2    Lindberg, C.3    Zhu, W.4    Yates III, J.R.5    Nevin, K.P.6    Babnigg, G.7    Lovley, D.R.8    Giometti, C.S.9
  • 90
    • 77956470482 scopus 로고    scopus 로고
    • The genome of Geobacter bemidjiensis, exemplar for the subsurface clade of Geobacter species that predominate in Fe(III)-reducing subsurface environments
    • M. Aklujkar, N.D. Young, D. Holmes, M. Chavan, C. Risso, H.E. Kiss, C.S. Han, M.L. Land, and D.R. Lovley The genome of Geobacter bemidjiensis, exemplar for the subsurface clade of Geobacter species that predominate in Fe(III)-reducing subsurface environments BMC Genomics 11 2010 490
    • (2010) BMC Genomics , vol.11 , pp. 490
    • Aklujkar, M.1    Young, N.D.2    Holmes, D.3    Chavan, M.4    Risso, C.5    Kiss, H.E.6    Han, C.S.7    Land, M.L.8    Lovley, D.R.9
  • 91
    • 32144462839 scopus 로고    scopus 로고
    • Differential protein expression in the metal-reducing bacterium Geobacter sulfurreducens strain PCA grown with fumarate or ferric citrate
    • DOI 10.1002/pmic.200500137
    • T. Khare, A. Esteve-Nunez, K.P. Nevin, W. Zhu, J.R. Yates III, D. Lovley, and C.S. Giometti Differential protein expression in the metal-reducing bacterium Geobacter sulfurreducens strain PCA grown with fumarate or ferric citrate Proteomics 6 2006 632 640 (Pubitemid 43208043)
    • (2006) Proteomics , vol.6 , Issue.2 , pp. 632-640
    • Khare, T.1    Esteve-Nunez, A.2    Nevin, K.P.3    Zhu, W.4    Yates III, J.R.5    Lovley, D.6    Giometti, C.S.7
  • 93
    • 84855754203 scopus 로고    scopus 로고
    • Electron donors supporting growth and electroactivity of Geobacter sulfurreducens anode biofilms
    • A.M. Speers, and G. Reguera Electron donors supporting growth and electroactivity of Geobacter sulfurreducens anode biofilms Appl. Environ. Microbiol. 78 2012 437 444
    • (2012) Appl. Environ. Microbiol. , vol.78 , pp. 437-444
    • Speers, A.M.1    Reguera, G.2
  • 94
    • 78549269463 scopus 로고    scopus 로고
    • Metabolic response of Geobacter sulfurreducens towards electron donor/acceptor variation
    • T.H. Yang, M.V. Coppi, D.R. Lovley, and J. Sun Metabolic response of Geobacter sulfurreducens towards electron donor/acceptor variation Microb. Cell Fact. 9 2010 90
    • (2010) Microb. Cell Fact. , vol.9 , pp. 90
    • Yang, T.H.1    Coppi, M.V.2    Lovley, D.R.3    Sun, J.4
  • 95
    • 38049139132 scopus 로고    scopus 로고
    • Fluorescent properties of c-type cytochromes reveal their potential role as an extracytoplasmic electron sink in Geobacter sulfurreducens
    • A. Esteve-Nunez, J. Sosnik, P. Visconti, and D.R. Lovley Fluorescent properties of c-type cytochromes reveal their potential role as an extracytoplasmic electron sink in Geobacter sulfurreducens Environ. Microbiol. 10 2008 497 505
    • (2008) Environ. Microbiol. , vol.10 , pp. 497-505
    • Esteve-Nunez, A.1    Sosnik, J.2    Visconti, P.3    Lovley, D.R.4
  • 98
    • 8144220027 scopus 로고    scopus 로고
    • Ferrihydrite-dependent growth of Sulfurospirillum deleyianum through electron transfer via sulfur cycling
    • DOI 10.1128/AEM.70.10.5744-5749.2004
    • K.L. Straub, and B. Schink Ferrihydrite-dependent growth of Sulfurospirillum deleyianum through electron transfer via sulfur cycling Appl. Environ. Microbiol. 70 2004 5744 5749 (Pubitemid 39471812)
    • (2004) Applied and Environmental Microbiology , vol.70 , Issue.10 , pp. 5744-5749
    • Straub, K.L.1    Schink, B.2
  • 99
    • 0028587578 scopus 로고
    • Characterization of Thiobacillus caldus sP. Nov., A moderately thermophilic acidophile
    • K.B. Hallberg, and E.B. Lindström Characterization of Thiobacillus caldus sp. nov., a moderately thermophilic acidophile Microbiology 140 1994 3451 3456
    • (1994) Microbiology , vol.140 , pp. 3451-3456
    • Hallberg, K.B.1    Lindström, E.B.2
  • 100
    • 2642582298 scopus 로고    scopus 로고
    • 1 complexes and terminal oxidases in the extremophilic chemolithoautotrophic Acidithiobacillus ferrooxidans
    • DOI 10.1016/j.bbabio.2004.02.008, PII S0005272804000441
    • G. Brasseur, G. Levican, V. Bonnefoy, D. Holmes, E. Jedlicki, and D. Lemesle-Meunier Apparent redundancy of electron transfer pathways via bc(1) complexes and terminal oxidases in the extremophilic chemolithoautotrophic Acidithiobacillus ferrooxidans Biochim. Biophys. Acta 1656 2004 114 126 (Pubitemid 38721273)
    • (2004) Biochimica et Biophysica Acta - Bioenergetics , vol.1656 , Issue.2-3 , pp. 114-126
    • Brasseur, G.1    Levican, G.2    Bonnefoy, V.3    Holmes, D.4    Jedlicki, E.5    Lemesle-Meunier, D.6
  • 101
    • 3242780146 scopus 로고    scopus 로고
    • Effect of uncouplers on endogenous respiration and ferrous iron oxidation in a chemolithoautotrophic bacterium Acidithiobacillus (Thiobacillus) ferrooxidans
    • DOI 10.1016/j.femsle.2004.06.027, PII S037810970400446X
    • Y. Chen, and I. Suzuki Effect of uncouplers on endogenous respiration and ferrous iron oxidation in a chemolithoautotrophic bacterium Acidithiobacillus (Thiobacillus) ferrooxidans FEMS Microbiol. Lett. 237 2004 139 145 (Pubitemid 38980016)
    • (2004) FEMS Microbiology Letters , vol.237 , Issue.1 , pp. 139-145
    • Chen, Y.1    Suzuki, I.2
  • 102
    • 0028089328 scopus 로고
    • 1 complex reconstituted into potassium-loaded phospholipid vesicles
    • T. Miki, M. Miki, and Y. Orii Membrane potential-linked reversed electron transfer in the beef heart cytochrome bc1 complex reconstituted into potassium-loaded phospholipid vesicles J. Biol. Chem. 269 1994 1827 1833 (Pubitemid 24035380)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.3 , pp. 1827-1833
    • Miki, T.1    Miki, M.2    Orii, Y.3
  • 103
    • 0025602517 scopus 로고
    • Partial reversion of the electrogenic reaction in the ubiquinol: Cytochrome c2-oxidoreductase of Rhodobacter sphaeroides chromatophores under neutral and alkaline conditions
    • A.Y. Mulkidjanian, M.D. Mamedov, A.Y. Semenov, V.P. Shinkarev, M.I. Verkhovsky, and L.A. Drachev Partial reversion of the electrogenic reaction in the ubiquinol: cytochrome c2-oxidoreductase of Rhodobacter sphaeroides chromatophores under neutral and alkaline conditions FEBS Lett. 277 1990 127 130
    • (1990) FEBS Lett. , vol.277 , pp. 127-130
    • Mulkidjanian, A.Y.1    Mamedov, M.D.2    Semenov, A.Y.3    Shinkarev, V.P.4    Verkhovsky, M.I.5    Drachev, L.A.6
  • 104
    • 1342325555 scopus 로고    scopus 로고
    • Reversible redox energy coupling in electron transfer chains
    • DOI 10.1038/nature02242
    • A. Osyczka, C.C. Moser, F. Daldal, and P.L. Dutton Reversible redox energy coupling in electron transfer chains Nature 427 2004 607 612 (Pubitemid 38248474)
    • (2004) Nature , vol.427 , Issue.6975 , pp. 607-612
    • Osyczka, A.1    Moser, C.C.2    Daldal, F.3    Dutton, P.L.4
  • 105
    • 0021227370 scopus 로고
    • The acidophilic thiobacilli and other acidophilic bacteria that share their habitat
    • A.P. Harrison Jr. The acidophilic thiobacilli and other acidophilic bacteria that share their habitat Annu. Rev. Microbiol. 38 1984 265 292
    • (1984) Annu. Rev. Microbiol. , vol.38 , pp. 265-292
    • Harrison, Jr.A.P.1
  • 106
    • 84865283609 scopus 로고    scopus 로고
    • Nitrospira-dominated biofilm within a thermal artesian spring: A case for nitrification-driven primary production in a geothermal setting
    • C.R. Marks, B.S. Stevenson, S. Rudd, and P.A. Lawson Nitrospira-dominated biofilm within a thermal artesian spring: a case for nitrification-driven primary production in a geothermal setting Geobiology 10 2012 457 466
    • (2012) Geobiology , vol.10 , pp. 457-466
    • Marks, C.R.1    Stevenson, B.S.2    Rudd, S.3    Lawson, P.A.4
  • 107
    • 35448931242 scopus 로고    scopus 로고
    • Look on the positive side! The orientation, identification and bioenergetics of 'Archaeal' membrane-bound nitrate reductases
    • DOI 10.1111/j.1574-6968.2007.00887.x
    • R.M. Martinez-Espinosa, E.J. Dridge, M.J. Bonete, J.N. Butt, C.S. Butler, F. Sargent, and D.J. Richardson Look on the positive side! The orientation, identification and bioenergetics of 'Archaeal' membrane-bound nitrate reductases FEMS Microbiol. Lett. 276 2007 129 139 (Pubitemid 47621780)
    • (2007) FEMS Microbiology Letters , vol.276 , Issue.2 , pp. 129-139
    • Martinez-Espinosa, R.M.1    Dridge, E.J.2    Bonete, M.J.3    Butt, J.N.4    Butler, C.S.5    Sargent, F.6    Richardson, D.J.7
  • 108
    • 33846174685 scopus 로고    scopus 로고
    • Haloarcula marismortui cytochrome b-561 is encoded by the narC gene in the dissimilatory nitrate reductase operon
    • DOI 10.1007/s00792-006-0016-3
    • K. Yoshimatsu, O. Araya, and T. Fujiwara Haloarcula marismortui cytochrome b-561 is encoded by the narC gene in the dissimilatory nitrate reductase operon Extremophiles 11 2007 41 47 (Pubitemid 46089628)
    • (2007) Extremophiles , vol.11 , Issue.1 , pp. 41-47
    • Yoshimatsu, K.1    Araya, O.2    Fujiwara, T.3
  • 110
    • 84866432793 scopus 로고    scopus 로고
    • The nitrogen cycle in the archaeaon: An intricate interplay of enzymatic and abiotic reactions
    • J.W. Moir, Castor Academic Press Norfolk (UK)
    • R. van Lis, A.L. Ducluzeau, W. Nitschke, and B. Schoepp-Cothenet The nitrogen cycle in the archaeaon: an intricate interplay of enzymatic and abiotic reactions J.W. Moir, Nitrogen Cycling in Bacteria: Molecular Analysis 2010 Castor Academic Press Norfolk (UK) 1 12
    • (2010) Nitrogen Cycling in Bacteria: Molecular Analysis , pp. 1-12
    • Van Lis, R.1    Ducluzeau, A.L.2    Nitschke, W.3    Schoepp-Cothenet, B.4
  • 111
    • 12544251532 scopus 로고    scopus 로고
    • Halobacterium noricense sp. Nov., an archaeal isolate from a bore core of an alpine Permian salt deposit, classification of Halobacterium sp. NRC-1 as a strain of H. Salinarum and emended description of H. Salinarum
    • C. Gruber, A. Legat, M. Pfaffenhuemer, C. Radax, G. Weidler, H.J. Busse, and H. Stan-Lotter Halobacterium noricense sp. nov., an archaeal isolate from a bore core of an alpine Permian salt deposit, classification of Halobacterium sp. NRC-1 as a strain of H. salinarum and emended description of H. salinarum Extremophiles 8 2004 431 439
    • (2004) Extremophiles , vol.8 , pp. 431-439
    • Gruber, C.1    Legat, A.2    Pfaffenhuemer, M.3    Radax, C.4    Weidler, G.5    Busse, H.J.6    Stan-Lotter, H.7
  • 112
    • 0016139829 scopus 로고
    • Salt-dependant properties of proteins from extremely halophilic bacteria
    • J.K. Lanyi Salt-dependant properties of proteins from extremely halophilic bacteria Bacteriol. Rev. 38 1974 9
    • (1974) Bacteriol. Rev. , vol.38 , pp. 9
    • Lanyi, J.K.1
  • 113
    • 0033031775 scopus 로고    scopus 로고
    • Caldivirga maquilingensis gen. Nov., sp. Nov., a new genus of rod-shaped crenarchaeote isolated from a hot spring in the Philippines
    • T. Itoh, K.-i. Suzuki, P.C. Sanchez, and T. Nakase Caldivirga maquilingensis gen. nov., sp. nov., a new genus of rod-shaped crenarchaeote isolated from a hot spring in the Philippines Int. J. Syst. Bacteriol. 49 1999 1157 1163
    • (1999) Int. J. Syst. Bacteriol. , vol.49 , pp. 1157-1163
    • Itoh, T.1    Suzuki, K.-I.2    Sanchez, P.C.3    Nakase, T.4
  • 114
    • 0025194727 scopus 로고
    • 3 from Sulfolobus acidocaldarius. A single-subunit, quinol-oxidizing archaebacterial terminal oxidase
    • DOI 10.1111/j.1432-1033.1990.tb19123.x
    • S. Anemüller, and G. Schäfer Cytochrome aa3 from Sulfolobus acidocaldarius. A single-subunit, quinol-oxidizing archaebacterial terminal oxidase Eur. J. Biochem. 191 1990 297 305 (Pubitemid 20233742)
    • (1990) European Journal of Biochemistry , vol.191 , Issue.2 , pp. 297-305
    • Anemuller, S.1    Schafer, G.2
  • 115
    • 0036868094 scopus 로고    scopus 로고
    • The archaeal respiratory supercomplex SoxM from S. Acidocaldarius combines features of quinole and cytochrome c oxidases
    • DOI 10.1515/BC.2002.200
    • L. Komorowski, W. Verheyen, and G. Schäfer The archaeal respiratory supercomplex SoxM from S. acidocaldarius combines features of quinole and cytochrome c oxidases Biol. Chem. 383 2002 1791 1799 (Pubitemid 36040331)
    • (2002) Biological Chemistry , vol.383 , Issue.11 , pp. 1791-1799
    • Komorowski, L.1    Verheyen, W.2    Schafer, G.3
  • 116
    • 0027446594 scopus 로고
    • Evidence for a Rieske-type FeS center in the thermoacidophilic archaebacterium Sulfolobus acidocaldarius
    • DOI 10.1016/0014-5793(93)81328-W
    • S. Anemüller, C.L. Schmidt, G. Schäfer, and M. Teixeira Evidence for a Rieske-type FeS center in the thermoacidophilic archaebacterium Sulfolobus acidocaldarius FEBS Lett. 318 1993 61 64 (Pubitemid 23057037)
    • (1993) FEBS Letters , vol.318 , Issue.1 , pp. 61-64
    • Anemuller, S.1    Schmidt, C.L.2    Schafer, G.3    Teixeira, M.4
  • 117
    • 0035808256 scopus 로고    scopus 로고
    • 558/566 from the Archaeon Sulfolobus acidocaldarius performs pivoting movements with respect to the membrane surface
    • DOI 10.1016/S0014-5793(00)02357-7, PII S0014579300023577
    • B. Schoepp-Cothenet, M. Schütz, F. Baymann, M. Brugna, W. Nitschke, H. Myllykallio, and C. Schmidt The membrane-extrinsic domain of cytochrome b558/566 from the archaeon Sulfolobus acidocaldarius performs pivoting movements with respect to the membrane surface FEBS Lett. 487 2001 372 376 (Pubitemid 32121759)
    • (2001) FEBS Letters , vol.487 , Issue.3 , pp. 372-376
    • Schoepp-Cothenet, B.1    Schutz, M.2    Baymann, F.3    Brugna, M.4    Nitschke, W.5    Myllykallio, H.6    Schmidt, C.7
  • 118
    • 0032523235 scopus 로고    scopus 로고
    • Cytochrome b(558/566) from the Archaeon Sulfolobus acidocaldarius. A novel highly glycosylated, membrane-bound B-type hemoprotein
    • DOI 10.1074/jbc.273.20.12032
    • T. Hettmann, C.L. Schmidt, S. Anemüller, U. Zähringer, H. Moll, A. Petersen, and G. Schäfer Cytochrome b558/566 from the archaeon Sulfolobus acidocaldarius. A novel highly glycosylated, membrane-bound b-type hemoprotein J. Biol. Chem. 273 1998 12032 12040 (Pubitemid 28240560)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.20 , pp. 12032-12040
    • Hettmann, T.1    Schmidt, C.L.2    Anemuller, S.3    Zahringer, U.4    Moll, H.5    Petersen, A.6    Schafer, G.7
  • 119
    • 0037667756 scopus 로고    scopus 로고
    • 1-analogous complex in the respiratory chain of the hyperthermoacidophilic crenarchaeon Sulfolobus acidocaldarius
    • DOI 10.1023/A:1023742002493
    • A. Hiller, T. Henninger, G. Schäfer, and C.L. Schmidt New genes encoding subunits of a cytochrome bc1-analogous complex in the respiratory chain of the hyperthermoacidophilic crenarchaeon Sulfolobus acidocaldarius J. Bioenerg. Biomembr. 35 2003 121 131 (Pubitemid 36733531)
    • (2003) Journal of Bioenergetics and Biomembranes , vol.35 , Issue.2 , pp. 121-131
    • Hiller, A.1    Henninger, T.2    Schafer, G.3    Schmidt, C.L.4
  • 121
    • 38949170756 scopus 로고    scopus 로고
    • The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism
    • DOI 10.1128/AEM.02019-07
    • K.S. Auernik, Y. Maezato, P.H. Blum, and R.M. Kelly The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism Appl. Environ. Microbiol. 74 2008 682 692 (Pubitemid 351225719)
    • (2008) Applied and Environmental Microbiology , vol.74 , Issue.3 , pp. 682-692
    • Auernik, K.S.1    Maezato, Y.2    Blum, P.H.3    Kelly, R.M.4
  • 124
    • 0035143611 scopus 로고    scopus 로고
    • Quinone profiles of thermoplasma acidophilum HO-62
    • DOI 10.1128/JB.183.4.1462-1465.2001
    • H. Shimada, Y. Shida, N. Nemoto, T. Oshima, and A. Yamagishi Quinone profiles of Thermoplasma acidophilum HO-62 J. Bacteriol. 183 2001 1462 1465 (Pubitemid 32107745)
    • (2001) Journal of Bacteriology , vol.183 , Issue.4 , pp. 1462-1465
    • Shimada, H.1    Shida, Y.2    Nemoto, N.3    Oshima, T.4    Yamagishi, A.5
  • 126
    • 0026717634 scopus 로고
    • The Rieske FeS center from the gram-positive bacterium PS3 and its interaction with the menaquinone pool studied by EPR
    • U. Liebl, S. Pezennec, A. Riedel, E. Kellner, and W. Nitschke The Rieske FeS center from the gram-positive bacterium PS3 and its interaction with the menaquinone pool studied by EPR J. Biol. Chem. 267 1992 14068 14072
    • (1992) J. Biol. Chem. , vol.267 , pp. 14068-14072
    • Liebl, U.1    Pezennec, S.2    Riedel, A.3    Kellner, E.4    Nitschke, W.5


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