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Volumn 100, Issue 4, 2005, Pages 365-379

Cytochrome c and bioenergetic hypothetical model for alkaliphilic Bacillus spp.

Author keywords

Alkaline adaptation; Alkaliphilic; Bacillus; Cytochrome c; H + condenser; Ion capacity; Membrane electrical potential; Redox potential

Indexed keywords

BACTERIA; PH EFFECTS; REDOX REACTIONS;

EID: 31844441329     PISSN: 13891723     EISSN: None     Source Type: Journal    
DOI: 10.1263/jbb.100.365     Document Type: Article
Times cited : (29)

References (133)
  • 1
    • 0001892616 scopus 로고
    • General view of alkaliphilic termophiles
    • Horikoshi K. Grant W.D. Springer-Verlag Berlin
    • Horikoshi K. General view of alkaliphilic termophiles Horikoshi K. Grant W.D. Superbugs, microorganisms in extreme environment 1991 Springer-Verlag Berlin 3 14
    • (1991) Superbugs, Microorganisms in Extreme Environment , pp. 3-14
    • Horikoshi, K.1
  • 4
    • 2142645470 scopus 로고
    • Studies on the reduction of indigo in industrial fermentation vat (VII)
    • Takahara Y., Tanabe O. Studies on the reduction of indigo in industrial fermentation vat (VII) J. Ferment. Technol. 38 1960 329 331
    • (1960) J. Ferment. Technol. , vol.38 , pp. 329-331
    • Takahara, Y.1    Tanabe, O.2
  • 6
    • 0030745477 scopus 로고    scopus 로고
    • Microbial flora in the deepest sea mud of the Mariana Trench
    • Takami H., Inoue A., Fujii F., Horikoshi K. Microbial flora in the deepest sea mud of the Mariana Trench FEMS Microbiol. Lett. 152 1997 279 285
    • (1997) FEMS Microbiol. Lett. , vol.152 , pp. 279-285
    • Takami, H.1    Inoue, A.2    Fujii, F.3    Horikoshi, K.4
  • 8
    • 0016670229 scopus 로고
    • The basis of the alkalophilic property of a species of Bacillus
    • Ohta K., Kiyomiya A., Koyama N., Nosoh Y. The basis of the alkalophilic property of a species of Bacillus J. Gen. Microbiol. 86 1975 259 266
    • (1975) J. Gen. Microbiol. , vol.86 , pp. 259-266
    • Ohta, K.1    Kiyomiya, A.2    Koyama, N.3    Nosoh, Y.4
  • 11
    • 0031263447 scopus 로고    scopus 로고
    • Mechanisms of cytoplasmic pH regulation in alkaliphilic strains of Bacillus
    • Krulwich T.A., Ito M., Gilmour R., Guffanti A.A. Mechanisms of cytoplasmic pH regulation in alkaliphilic strains of Bacillus Extremophiles 1 1997 163 169
    • (1997) Extremophiles , vol.1 , pp. 163-169
    • Krulwich, T.A.1    Ito, M.2    Gilmour, R.3    Guffanti, A.A.4
  • 13
    • 0036351377 scopus 로고    scopus 로고
    • Bioenergetics of alkaliphilic Bacillus spp.
    • Yumoto I. Bioenergetics of alkaliphilic Bacillus spp. J. Biosci. Bioeng. 93 2002 342 353
    • (2002) J. Biosci. Bioeng. , vol.93 , pp. 342-353
    • Yumoto, I.1
  • 14
    • 9744237489 scopus 로고    scopus 로고
    • Electron transport system in alkaliphilic Bacillus spp.
    • Yumoto I. Electron transport system in alkaliphilic Bacillus spp. Recent Res. Dev. Bacteriol. 1 2003 131 149
    • (2003) Recent Res. Dev. Bacteriol. , vol.1 , pp. 131-149
    • Yumoto, I.1
  • 15
    • 36949083936 scopus 로고
    • Coupling of phosphorylation to electron and hydrogen transfer by a chemiosmotic type of mechanism
    • Mitchell P. Coupling of phosphorylation to electron and hydrogen transfer by a chemiosmotic type of mechanism Nature 191 1961 144 148
    • (1961) Nature , vol.191 , pp. 144-148
    • Mitchell, P.1
  • 16
    • 0028144988 scopus 로고
    • i-loaded membrane vesicles from alkaliphilic Bacillus firmus OF4
    • i-loaded membrane vesicles from alkaliphilic Bacillus firmus OF4 J. Biol. Chem. 269 1994 21576 21582
    • (1994) J. Biol. Chem. , vol.269 , pp. 21576-21582
    • Guffanti, A.A.1    Krulwich, T.A.2
  • 17
    • 0028175857 scopus 로고
    • Comparative 16S rDNA sequence analysis of some alkaliphilic bacilli and the establishment of sixth rRNA group within the genus Bacillus
    • Nielsen P., Rainey F.A., Outtrup H., Priest F.G., Fritze D. Comparative 16S rDNA sequence analysis of some alkaliphilic bacilli and the establishment of sixth rRNA group within the genus Bacillus FEMS Microbiol. Lett. 177 1994 61 66
    • (1994) FEMS Microbiol. Lett. , vol.177 , pp. 61-66
    • Nielsen, P.1    Rainey, F.A.2    Outtrup, H.3    Priest, F.G.4    Fritze, D.5
  • 18
    • 0029095996 scopus 로고
    • Phenetic diversity of alkaliphilic Bacillus strains: Proposal for nine new species
    • Nielsen P., Fritze D., Priest F.G. Phenetic diversity of alkaliphilic Bacillus strains: proposal for nine new species Microbiology 141 1995 1745 1761
    • (1995) Microbiology , vol.141 , pp. 1745-1761
    • Nielsen, P.1    Fritze, D.2    Priest, F.G.3
  • 19
    • 51649217935 scopus 로고
    • Bacillus alcalophilus n. sp.; Benevens enkele ervaringen met sterk alcalischevoedingbodems
    • Vedder A. Bacillus alcalophilus n. sp.; benevens enkele ervaringen met sterk alcalischevoedingbodems Antonie van Leeuwenhoek J. Microbiol. Serol. 1 1934 143 147
    • (1934) Antonie Van Leeuwenhoek J. Microbiol. Serol. , vol.1 , pp. 143-147
    • Vedder, A.1
  • 20
    • 0027400351 scopus 로고
    • Bacillus cohnii sp. nov., new, obligately alkaliphilic, oval-spore-forming Bacillus species with ornithine and aspartic acid instead of diaminopimeric acid in the cell wall
    • Spanka R., Fritze D. Bacillus cohnii sp. nov., new, obligately alkaliphilic, oval-spore-forming Bacillus species with ornithine and aspartic acid instead of diaminopimeric acid in the cell wall Int. J. Syst. Bacteriol. 43 1993 150 156
    • (1993) Int. J. Syst. Bacteriol. , vol.43 , pp. 150-156
    • Spanka, R.1    Fritze, D.2
  • 21
    • 0029116656 scopus 로고
    • Isolation and characterization of novel alkaliphiles from bauxite-processing waste and description of Bacillus vedderi sp. nov., a new obligate alkaliphile
    • Agnew M.D., Koval S.F., Jarrell K.F. Isolation and characterization of novel alkaliphiles from bauxite-processing waste and description of Bacillus vedderi sp. nov., a new obligate alkaliphile Syst. Appl. Microbiol. 18 1995 221 230
    • (1995) Syst. Appl. Microbiol. , vol.18 , pp. 221-230
    • Agnew, M.D.1    Koval, S.F.2    Jarrell, K.F.3
  • 22
    • 0030050176 scopus 로고    scopus 로고
    • Bacillus haloalkaliphilus sp. nov.
    • Fritze D. Bacillus haloalkaliphilus sp. nov. Int. J. Syst. Bacteriol. 46 1996 98 101
    • (1996) Int. J. Syst. Bacteriol. , vol.46 , pp. 98-101
    • Fritze, D.1
  • 23
    • 0006301126 scopus 로고    scopus 로고
    • Bacillus arsenicoselenatis, sp. nov., and Bacillus selenitireducence, sp. nov.: Two haloalkaliphiles from Mono Lake, California that respire oxyanions of selenium and arsenic
    • Switzer Blum J., Burns Bindi A., Buzzelli J., Stolz J.F., Oremland R.S. Bacillus arsenicoselenatis, sp. nov., and Bacillus selenitireducence, sp. nov.: two haloalkaliphiles from Mono Lake, California that respire oxyanions of selenium and arsenic Arch. Microbiol. 171 1998 19 30
    • (1998) Arch. Microbiol. , vol.171 , pp. 19-30
    • Switzer Blum, J.1    Burns Bindi, A.2    Buzzelli, J.3    Stolz, J.F.4    Oremland, R.S.5
  • 26
    • 13244270096 scopus 로고    scopus 로고
    • Bacillus patagoniensis sp. nov., a novel alkalitolerant bacterium from Atriplex lampa rhizosphere, Patagonia, Argentina
    • Olivera N., Siñeriz F., Breccia J.D. Bacillus patagoniensis sp. nov., a novel alkalitolerant bacterium from Atriplex lampa rhizosphere, Patagonia, Argentina Int. J. Syst. Evol. Microbiol. 55 2005 443 447
    • (2005) Int. J. Syst. Evol. Microbiol. , vol.55 , pp. 443-447
    • Olivera, N.1    Siñeriz, F.2    Breccia, J.D.3
  • 27
    • 16844371501 scopus 로고    scopus 로고
    • Bacillus bogoriensis sp. nov., a new alkaliphilic halotolerant member of the genus Bacillus isolated from a Kenyan soda lake
    • Vargas V.A., Delgado O.D., Hatti-Kaul R., Mattiasson B. Bacillus bogoriensis sp. nov., a new alkaliphilic halotolerant member of the genus Bacillus isolated from a Kenyan soda lake Int. J. Syst. Evol. Microbiol. 55 2005 899 902
    • (2005) Int. J. Syst. Evol. Microbiol. , vol.55 , pp. 899-902
    • Vargas, V.A.1    Delgado, O.D.2    Hatti-Kaul, R.3    Mattiasson, B.4
  • 30
    • 22544479477 scopus 로고    scopus 로고
    • Alkalibacterium iburiense sp. nov., an obligate alkaliphile that reduces an indigo dye
    • Nakajima K., Hirota K., Nodasaka Y., Yumoto I. Alkalibacterium iburiense sp. nov., an obligate alkaliphile that reduces an indigo dye Int. J. Syst. Evol. Microbiol. 55 2005 1525 1530
    • (2005) Int. J. Syst. Evol. Microbiol. , vol.55 , pp. 1525-1530
    • Nakajima, K.1    Hirota, K.2    Nodasaka, Y.3    Yumoto, I.4
  • 31
    • 22644439547 scopus 로고    scopus 로고
    • Oceanobacillus oncorhynchi sp. nov., a halotolerant obligate alkaliphile isolated from the skin of a rainbow trout (Oncorhynchus mykiss), and emended description of the genus Oceanobacillus
    • Yumoto I., Hirota K., Nodasaka Y., Nakajima K. Oceanobacillus oncorhynchi sp. nov., a halotolerant obligate alkaliphile isolated from the skin of a rainbow trout (Oncorhynchus mykiss), and emended description of the genus Oceanobacillus Int. J. Syst. Evol. Microbiol. 55 2005 1521 1524
    • (2005) Int. J. Syst. Evol. Microbiol. , vol.55 , pp. 1521-1524
    • Yumoto, I.1    Hirota, K.2    Nodasaka, Y.3    Nakajima, K.4
  • 34
    • 4344703019 scopus 로고    scopus 로고
    • MotPS is the stator-force generator for motility of alkalipilic Bacillus, and its homologue is a second functional Mot in Bacillus subtilis
    • Ito M., Hicks D.B., Henkin T.M., Guffanti A.A., Powers B.D., Zvi L., Uematsu K., Krulwich T.A. MotPS is the stator-force generator for motility of alkalipilic Bacillus, and its homologue is a second functional Mot in Bacillus subtilis Mol. Microbiol. 53 2004 1035 1049
    • (2004) Mol. Microbiol. , vol.53 , pp. 1035-1049
    • Ito, M.1    Hicks, D.B.2    Henkin, T.M.3    Guffanti, A.A.4    Powers, B.D.5    Zvi, L.6    Uematsu, K.7    Krulwich, T.A.8
  • 35
    • 0025952204 scopus 로고
    • Molar growth yield and bioenergetic parameters of extremely alkaliphilic Bacillus species in batch cultures, and growth in a chemostat at pH 10.5
    • Guffanti A.A., Hicks D.B. Molar growth yield and bioenergetic parameters of extremely alkaliphilic Bacillus species in batch cultures, and growth in a chemostat at pH 10.5 Microbiology 137 1991 2375 2379
    • (1991) Microbiology , vol.137 , pp. 2375-2379
    • Guffanti, A.A.1    Hicks, D.B.2
  • 36
    • 0020504917 scopus 로고
    • Respiration-dependent proton translocation in alkalophilic Bacillus firmus RAB and its non-alkalophilic mutant derivative
    • Lewis R.J., Krulwich T.A., Reynafarje B., Lehninger A.L. Respiration-dependent proton translocation in alkalophilic Bacillus firmus RAB and its non-alkalophilic mutant derivative J. Biol. Chem. 258 1983 2109 2111
    • (1983) J. Biol. Chem. , vol.258 , pp. 2109-2111
    • Lewis, R.J.1    Krulwich, T.A.2    Reynafarje, B.3    Lehninger, A.L.4
  • 37
    • 0028912367 scopus 로고
    • Alkalipiles: 'Basic' molecular problems of pH tolerance and bioenergetics
    • Krulwich T.A. Alkalipiles: 'basic' molecular problems of pH tolerance and bioenergetics Mol. Microbiol. 15 1995 403 410
    • (1995) Mol. Microbiol. , vol.15 , pp. 403-410
    • Krulwich, T.A.1
  • 38
    • 0026766756 scopus 로고
    • Spin-label electron paramagnetic resonance and differential scanning calorimetry studies of the interaction between mitochondrial cytochrome c oxidase and adenosine triphospate synthase complex
    • Qiu Z.-H., Yu L., Yu C.-A. Spin-label electron paramagnetic resonance and differential scanning calorimetry studies of the interaction between mitochondrial cytochrome c oxidase and adenosine triphospate synthase complex Biochemistry 31 1992 3297 3302
    • (1992) Biochemistry , vol.31 , pp. 3297-3302
    • Qiu, Z.-H.1    Yu, L.2    Yu, C.-A.3
  • 39
    • 0032511164 scopus 로고    scopus 로고
    • +-migration along the membrane surface as revealed by double patch-clamp experiments
    • +-migration along the membrane surface as revealed by double patch-clamp experiments FEBS Lett. 429 1998 197 200
    • (1998) FEBS Lett. , vol.429 , pp. 197-200
    • Antonenko, Y.N.1    Pohl, P.2
  • 40
    • 0027997585 scopus 로고
    • Covalently bound pH-indicator dyes at selected extracellular or cytoplasmic sites in bacteriorhodopsin. 1. Proton migration along the surface of bacteriorhodopsin micelles and delayed transfer from surface to bulk
    • Scherrer P., Alexiev U., Marti T., Khorana H.G., Heyn M.P. Covalently bound pH-indicator dyes at selected extracellular or cytoplasmic sites in bacteriorhodopsin. 1. Proton migration along the surface of bacteriorhodopsin micelles and delayed transfer from surface to bulk Biochemistry 33 1994 13684 13692
    • (1994) Biochemistry , vol.33 , pp. 13684-13692
    • Scherrer, P.1    Alexiev, U.2    Marti, T.3    Khorana, H.G.4    Heyn, M.P.5
  • 41
    • 0027940310 scopus 로고
    • Covalently bound pH-indicator dyes at selected extracellular or cytoplasmic sites in bacteriorhodopsin. 2. Rotational orientation of helices D and e and kinetic correlation between M formation and proton release in bacteriorhodopsin micelles
    • Alexiev U., Marti T., Heyn M.P., Khorana H.G., Scherrer P. Covalently bound pH-indicator dyes at selected extracellular or cytoplasmic sites in bacteriorhodopsin. 2. Rotational orientation of helices D and E and kinetic correlation between M formation and proton release in bacteriorhodopsin micelles Biochemistry 33 1994 13693 13699
    • (1994) Biochemistry , vol.33 , pp. 13693-13699
    • Alexiev, U.1    Marti, T.2    Heyn, M.P.3    Khorana, H.G.4    Scherrer, P.5
  • 42
    • 0029098354 scopus 로고
    • The dynamic of proton exchange between bulk and surface group
    • Gutoman M., Nachiel E. The dynamic of proton exchange between bulk and surface group Biochim. Biophys. Acta 1231 1995 123 138
    • (1995) Biochim. Biophys. Acta , vol.1231 , pp. 123-138
    • Gutoman, M.1    Nachiel, E.2
  • 43
    • 0035909798 scopus 로고    scopus 로고
    • Proton-collecting properties of bovine heart cytochrome c oxidase: Kinetic and electrostatic analysis
    • Marantz Y., Einarsdottir O., Nachliel E., Gutman M. Proton-collecting properties of bovine heart cytochrome c oxidase: kinetic and electrostatic analysis Biochemistry 40 2001 15086 15097
    • (2001) Biochemistry , vol.40 , pp. 15086-15097
    • Marantz, Y.1    Einarsdottir, O.2    Nachliel, E.3    Gutman, M.4
  • 46
    • 0037174138 scopus 로고    scopus 로고
    • Cardiolipin: A proton trap for oxidative phosphorylation
    • Haines T.H., Dencher N.A. Cardiolipin: a proton trap for oxidative phosphorylation FEBS Lett. 528 2002 35 39
    • (2002) FEBS Lett. , vol.528 , pp. 35-39
    • Haines, T.H.1    Dencher, N.A.2
  • 47
    • 0041843662 scopus 로고    scopus 로고
    • Low dielectric of water at the membrane interface: Effect on the energy coupling mechanisms in biological membranes
    • Cherepanov D., Feniouk B.A., Junge W., Mulkidjanian A.Y. Low dielectric of water at the membrane interface: effect on the energy coupling mechanisms in biological membranes Biophys. J. 85 2003 1307 1316
    • (2003) Biophys. J. , vol.85 , pp. 1307-1316
    • Cherepanov, D.1    Feniouk, B.A.2    Junge, W.3    Mulkidjanian, A.Y.4
  • 48
    • 0032555160 scopus 로고    scopus 로고
    • The proton collecting function of the inner surface of cytochrome c oxidase from Rhodobacter sphaeroides
    • Marantz Y., Nachliel E., Aagaard A., Brezezinski P., Gutman M. The proton collecting function of the inner surface of cytochrome c oxidase from Rhodobacter sphaeroides Proc. Natl. Acad. Sci. USA 95 1998 8590 8595
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 8590-8595
    • Marantz, Y.1    Nachliel, E.2    Aagaard, A.3    Brezezinski, P.4    Gutman, M.5
  • 49
    • 0019215039 scopus 로고
    • Quantitative measurements of proton motive force and motility in Bacillus subtilis
    • Shioi J.-I., Matsuura S., Imae Y. Quantitative measurements of proton motive force and motility in Bacillus subtilis J. Bacteriol. 144 1980 891 897
    • (1980) J. Bacteriol. , vol.144 , pp. 891-897
    • Shioi, J.-I.1    Matsuura, S.2    Imae, Y.3
  • 50
    • 11944255561 scopus 로고    scopus 로고
    • Global transcription profiles and intracellular pH regulation measured in Bacillus licheniformis upon external pH upshifts
    • Hornbæk T., Jakobsen M., Dynesen J., Nielsen A.K. Global transcription profiles and intracellular pH regulation measured in Bacillus licheniformis upon external pH upshifts Arch. Microbiol. 182 2004 467 474
    • (2004) Arch. Microbiol. , vol.182 , pp. 467-474
    • Hornbæk, T.1    Jakobsen, M.2    Dynesen, J.3    Nielsen, A.K.4
  • 51
    • 0025950687 scopus 로고
    • Continuous measurement of the cytoplasmic pH in Lactococcus lactic with a fluorescent pH indicator
    • Molenaar D., Abee T., Konings W.N. Continuous measurement of the cytoplasmic pH in Lactococcus lactic with a fluorescent pH indicator Biochim. Biophys. Acta 1115 1991 75 83
    • (1991) Biochim. Biophys. Acta , vol.1115 , pp. 75-83
    • Molenaar, D.1    Abee, T.2    Konings, W.N.3
  • 53
    • 0028233309 scopus 로고
    • Growth and bioenergetic of alkaliphilic Bacillus firmus OF4 in continuous culture at high pH
    • Sturr M.G., Guffanti A.A., Krulwich T.A. Growth and bioenergetic of alkaliphilic Bacillus firmus OF4 in continuous culture at high pH J. Bacteriol. 176 1994 3111 3116
    • (1994) J. Bacteriol. , vol.176 , pp. 3111-3116
    • Sturr, M.G.1    Guffanti, A.A.2    Krulwich, T.A.3
  • 55
    • 0025950163 scopus 로고
    • The electrochemical proton potential of Bacillus alcalophilus
    • Hoffmann A., Dimroth P. The electrochemical proton potential of Bacillus alcalophilus Eur. J. Biochem. 201 1991 467 473
    • (1991) Eur. J. Biochem. , vol.201 , pp. 467-473
    • Hoffmann, A.1    Dimroth, P.2
  • 57
    • 0034303092 scopus 로고    scopus 로고
    • Identification of facultatively alkaliphilic Bacillus sp. strain YN-2000 and its fatty acid composition and cell-surface aspects depending on culture pH
    • Yumoto I., Yamazaki K., Hishinuma M., Nodasaka Y., Inoue N., Kawasaki K. Identification of facultatively alkaliphilic Bacillus sp. strain YN-2000 and its fatty acid composition and cell-surface aspects depending on culture pH Extremophiles 4 2000 285 290
    • (2000) Extremophiles , vol.4 , pp. 285-290
    • Yumoto, I.1    Yamazaki, K.2    Hishinuma, M.3    Nodasaka, Y.4    Inoue, N.5    Kawasaki, K.6
  • 58
    • 0025267914 scopus 로고
    • A novel aco-type cytochrome-c oxidase from a facultative alkalophilic Bacillus: Purification, and some molecular and enzymatic features
    • Qureshi M.H., Yumoto I., Fujiwara T., Fukumori Y., Yamanaka T. A novel aco-type cytochrome-c oxidase from a facultative alkalophilic Bacillus: purification, and some molecular and enzymatic features J. Biochem. 107 1990 480 485
    • (1990) J. Biochem. , vol.107 , pp. 480-485
    • Qureshi, M.H.1    Yumoto, I.2    Fujiwara, T.3    Fukumori, Y.4    Yamanaka, T.5
  • 59
    • 0026326745 scopus 로고
    • Stopped-flow and Rapid-scan studies of the redox behavior of cytochrome aco from facultative alkalophilic Bacillus
    • Orii Y., Yumoto I., Fukumori Y., Yamanaka T. Stopped-flow and Rapid-scan studies of the redox behavior of cytochrome aco from facultative alkalophilic Bacillus J. Biol. Chem. 266 1991 14310 14316
    • (1991) J. Biol. Chem. , vol.266 , pp. 14310-14316
    • Orii, Y.1    Yumoto, I.2    Fukumori, Y.3    Yamanaka, T.4
  • 61
    • 0028118779 scopus 로고
    • Proton pumping activity and visible absorption and resonance Raman spectra of a cao-type cytochrome c oxidase isolated from the thermophilic bacterium Bacillus PS3
    • Sone N., Ogura T., Noguchi S., Kitagawa T. Proton pumping activity and visible absorption and resonance Raman spectra of a cao-type cytochrome c oxidase isolated from the thermophilic bacterium Bacillus PS3 Biochemistry 33 1994 849 855
    • (1994) Biochemistry , vol.33 , pp. 849-855
    • Sone, N.1    Ogura, T.2    Noguchi, S.3    Kitagawa, T.4
  • 62
    • 0020352655 scopus 로고
    • 3-type terminal oxidase of a thermophilic bacterium. Purification, properties and proton pumping
    • 3-type terminal oxidase of a thermophilic bacterium. Purification, properties and proton pumping Biochim. Biophys. Acta 682 1982 216 226
    • (1982) Biochim. Biophys. Acta , vol.682 , pp. 216-226
    • Sone, N.1    Yanagita, Y.2
  • 64
    • 0025963395 scopus 로고
    • The ATPase of Bacillus alcalophilus. Reconstitution of energy-transducing function
    • Hoffmann A., Dimroth P. The ATPase of Bacillus alcalophilus. Reconstitution of energy-transducing function Eur. J. Biochem. 196 1991 493 497
    • (1991) Eur. J. Biochem. , vol.196 , pp. 493-497
    • Hoffmann, A.1    Dimroth, P.2
  • 65
    • 2942718765 scopus 로고    scopus 로고
    • Replacement of amino acid sequence features of a- and c-subunits of ATP synthases of alkaliphilic Bacillus with Bacillus consensus sequence results in defective oxidative phosphorylation and non-fermetative growth at pH 10.5
    • Wang Z., Hicks D.B., Guffanti A.A., Baldwin K., Krulwich T.A. Replacement of amino acid sequence features of a- and c-subunits of ATP synthases of alkaliphilic Bacillus with Bacillus consensus sequence results in defective oxidative phosphorylation and non-fermetative growth at pH 10.5 J. Biol. Chem. 297 2004 26546 26554
    • (2004) J. Biol. Chem. , vol.297 , pp. 26546-26554
    • Wang, Z.1    Hicks, D.B.2    Guffanti, A.A.3    Baldwin, K.4    Krulwich, T.A.5
  • 66
    • 0032077030 scopus 로고    scopus 로고
    • Studies on the respiratory system in alkaliphilic Bacillus; A proposed new respiratory mechanism
    • Higashibata A., Fujiwara T., Fukumori Y. Studies on the respiratory system in alkaliphilic Bacillus; a proposed new respiratory mechanism Extremophiles 2 1998 83 92
    • (1998) Extremophiles , vol.2 , pp. 83-92
    • Higashibata, A.1    Fujiwara, T.2    Fukumori, Y.3
  • 67
    • 0025049510 scopus 로고
    • Purification and characterization of catalase from a facultative alkalophilic Bacillus
    • Yumoto I., Fukumori Y., Yamanaka T. Purification and characterization of catalase from a facultative alkalophilic Bacillus J. Biochem. 108 1990 583 587
    • (1990) J. Biochem. , vol.108 , pp. 583-587
    • Yumoto, I.1    Fukumori, Y.2    Yamanaka, T.3
  • 71
    • 0000837519 scopus 로고    scopus 로고
    • Structural studies of eukaryotic cytochromes c
    • Scott R.A. Mauk A.G. University Science Books Sausalio, CA
    • Brayer G.D., Murphy M.P. Structural studies of eukaryotic cytochromes c Scott R.A. Mauk A.G. Cytochrome c A multidisciplinary approach 1996 University Science Books Sausalio, CA 103 166
    • (1996) Cytochrome C a Multidisciplinary Approach , pp. 103-166
    • Brayer, G.D.1    Murphy, M.P.2
  • 72
    • 0024997335 scopus 로고
    • Bacillus subtilis 13-kilodalton cytochrome c-550 encoded by cccA consists of a membrane-anchor and a heme domain
    • Von Wachenfeldt C., Hederstedt L. Bacillus subtilis 13-kilodalton cytochrome c-550 encoded by cccA consists of a membrane-anchor and a heme domain J. Biol. Chem. 265 1990 13939 13948
    • (1990) J. Biol. Chem. , vol.265 , pp. 13939-13948
    • Von Wachenfeldt, C.1    Hederstedt, L.2
  • 73
    • 0033543692 scopus 로고    scopus 로고
    • Bacillus subtilis contains two small c-type cytocheome with homologous heme domains but different type of membrane anchors
    • Bengtsson J., Rivolta C., Hederstedt L., Karamata D. Bacillus subtilis contains two small c-type cytocheome with homologous heme domains but different type of membrane anchors J. Biol. Chem. 274 1999 26179 26184
    • (1999) J. Biol. Chem. , vol.274 , pp. 26179-26184
    • Bengtsson, J.1    Rivolta, C.2    Hederstedt, L.3    Karamata, D.4
  • 74
    • 0027403011 scopus 로고
    • Physico-chemical characterisation of membrane-bound and water-soluble forms of Bacillus subtilis cytochrome c-550
    • Von Wachenfeldt C., Hederstedt L. Physico-chemical characterisation of membrane-bound and water-soluble forms of Bacillus subtilis cytochrome c-550 Eur. J. Biochem. 212 1993 499 509
    • (1993) Eur. J. Biochem. , vol.212 , pp. 499-509
    • Von Wachenfeldt, C.1    Hederstedt, L.2
  • 75
    • 0024331619 scopus 로고
    • Cytochrome c-551 from the thermophilic bacterium PS3 grown under air-limited condition
    • Sone N., Kutoh E., Yanagita Y. Cytochrome c-551 from the thermophilic bacterium PS3 grown under air-limited condition Biochim. Biophys. Acta 977 1989 329 334
    • (1989) Biochim. Biophys. Acta , vol.977 , pp. 329-334
    • Sone, N.1    Kutoh, E.2    Yanagita, Y.3
  • 77
    • 0033595670 scopus 로고    scopus 로고
    • Cytochrome c-553 from the alkalophilic bacterium Bacillus pasteurii has the primary structure characteristics of a lipoprotein
    • Vandenberghe I.H.M., Guisez Y., Ciurli S., Benini S., van Beeumen J.J. Cytochrome c-553 from the alkalophilic bacterium Bacillus pasteurii has the primary structure characteristics of a lipoprotein Biochem. Biophys. Res. Commun. 264 1999 329 334
    • (1999) Biochem. Biophys. Res. Commun. , vol.264 , pp. 329-334
    • Vandenberghe, I.H.M.1    Guisez, Y.2    Ciurli, S.3    Benini, S.4    Van Beeumen, J.J.5
  • 78
    • 0034544593 scopus 로고    scopus 로고
    • 3 oxidase in clinically relevant proteobacteria?
    • 3 oxidase in clinically relevant proteobacteria? Trends Microbiol. 8 2000 542 543
    • (2000) Trends Microbiol. , vol.8 , pp. 542-543
    • Myllykallio, H.1    Liebl, U.2
  • 81
    • 0018975140 scopus 로고
    • Alkalophiles have much higher cytochrome contents than conventional bacteria and their own non-alkalophilic mutant derivatives
    • Lewis R.J., Belkina S., Krulwich T.A. Alkalophiles have much higher cytochrome contents than conventional bacteria and their own non-alkalophilic mutant derivatives Biochem. Biophys. Res. Commun. 95 1980 857 867
    • (1980) Biochem. Biophys. Res. Commun. , vol.95 , pp. 857-867
    • Lewis, R.J.1    Belkina, S.2    Krulwich, T.A.3
  • 83
    • 0030990855 scopus 로고    scopus 로고
    • Comparative study on cytochrome content of alkaliphilic Bacillus strains
    • Yumoto I., Nakajima K., Ikeda K. Comparative study on cytochrome content of alkaliphilic Bacillus strains J. Ferment. Bioeng. 83 1997 466 469
    • (1997) J. Ferment. Bioeng. , vol.83 , pp. 466-469
    • Yumoto, I.1    Nakajima, K.2    Ikeda, K.3
  • 84
    • 0024284303 scopus 로고
    • Purification and characterization of two soluble cytochromes from the alkalophilic Bacillus firmus RAB
    • Davidson M.W., Gray K.A., Knaff D.B., Krulwich T.A. Purification and characterization of two soluble cytochromes from the alkalophilic Bacillus firmus RAB Biochim. Biophys. Acta 933 1988 470 477
    • (1988) Biochim. Biophys. Acta , vol.933 , pp. 470-477
    • Davidson, M.W.1    Gray, K.A.2    Knaff, D.B.3    Krulwich, T.A.4
  • 87
    • 0030746129 scopus 로고    scopus 로고
    • Crystals of cytochrome c-553 from Bacillus pasteurii show diffraction to 0.97 Å resolution
    • Benini S., Ciurli S., Rypnjewski W., Wilson K.S. Crystals of cytochrome c-553 from Bacillus pasteurii show diffraction to 0.97 Å resolution Proteins 28 1997 580 585
    • (1997) Proteins , vol.28 , pp. 580-585
    • Benini, S.1    Ciurli, S.2    Rypnjewski, W.3    Wilson, K.S.4
  • 89
    • 0037469128 scopus 로고    scopus 로고
    • Structure and dynamics of reduced Bacillus pasteurii cytochrome c: Oxidation state dependent properties and implication for electron transfer processes
    • Bartalesi I., Bertini I., Rosato A. Structure and dynamics of reduced Bacillus pasteurii cytochrome c: oxidation state dependent properties and implication for electron transfer processes Biochemistry 42 2003 739 745
    • (2003) Biochemistry , vol.42 , pp. 739-745
    • Bartalesi, I.1    Bertini, I.2    Rosato, A.3
  • 90
    • 0023198172 scopus 로고
    • The c-type cytochromes of the gram-positive bacterium Bacillus licheniformis
    • Woolley K.J. The c-type cytochromes of the gram-positive bacterium Bacillus licheniformis Arch. Biochem. Biophys. 245 1987 376 379
    • (1987) Arch. Biochem. Biophys. , vol.245 , pp. 376-379
    • Woolley, K.J.1
  • 91
    • 0027198519 scopus 로고
    • Cytochrome c-551 of the thermophilic bacterium PS3. DNA sequence and analysis of mature cytochrome
    • Fujiwara Y., Oka M., Hamamoto T., Sone N. Cytochrome c-551 of the thermophilic bacterium PS3. DNA sequence and analysis of mature cytochrome Biochim. Biophys. Acta 1141 1993 213 219
    • (1993) Biochim. Biophys. Acta , vol.1141 , pp. 213-219
    • Fujiwara, Y.1    Oka, M.2    Hamamoto, T.3    Sone, N.4
  • 92
    • 0000679937 scopus 로고
    • Preparation of crystalline Pseudomonas cytochrome c-551 and its general properties
    • Horio T., Higashi T., Sasagawa M., Kusai K., Nakai M., Okunuki K. Preparation of crystalline Pseudomonas cytochrome c-551 and its general properties Biochem. J. 77 1960 194 201
    • (1960) Biochem. J. , vol.77 , pp. 194-201
    • Horio, T.1    Higashi, T.2    Sasagawa, M.3    Kusai, K.4    Nakai, M.5    Okunuki, K.6
  • 93
    • 0020004138 scopus 로고
    • Structure of cytochrome c551 from Pseudomonas aeruginosa refined at 1.6 Å resolution and comparison of the two redox forms
    • Matsuura Y., Takano T., Dickerson R.E. Structure of cytochrome c551 from Pseudomonas aeruginosa refined at 1.6 Å resolution and comparison of the two redox forms J. Mol. Biol. 156 1982 389 409
    • (1982) J. Mol. Biol. , vol.156 , pp. 389-409
    • Matsuura, Y.1    Takano, T.2    Dickerson, R.E.3
  • 94
    • 0029132455 scopus 로고
    • 6 from the green alga Monoraphidium braunii crystallization and preminary diffraction studies
    • 6 from the green alga Monoraphidium braunii crystallization and preminary diffraction studies Acta Crystallogr. D Biol. Crystallogr. 51 1995 232 234
    • (1995) Acta Crystallogr. D Biol. Crystallogr. , vol.51 , pp. 232-234
    • Frazao, C.1
  • 96
    • 0029918864 scopus 로고    scopus 로고
    • 553 from Desulfovibrio vulgaris with the class I cytochrome c family
    • 553 from Desulfovibrio vulgaris with the class I cytochrome c family Proteins 24 1996 178 194
    • (1996) Proteins , vol.24 , pp. 178-194
    • Blackledge, M.J.1    Guerlesquin, F.2    Marion, D.3
  • 98
    • 0029855438 scopus 로고    scopus 로고
    • Three-dimensional solution of Saccharomyces cerevisiae reduced iso-1-cytochrome c
    • Baistrocchi P., Banci L., Bertini I., Turano P., Bren K.L., Gray H.B. Three-dimensional solution of Saccharomyces cerevisiae reduced iso-1-cytochrome c Biochemistry 35 1996 13788 13796
    • (1996) Biochemistry , vol.35 , pp. 13788-13796
    • Baistrocchi, P.1    Banci, L.2    Bertini, I.3    Turano, P.4    Bren, K.L.5    Gray, H.B.6
  • 99
    • 0025884434 scopus 로고
    • Purification and characterization of two membrane-bound c-type cytochromes from a facultative alkalophilic Bacillus
    • Yumoto I., Fukumori Y., Yamanaka T. Purification and characterization of two membrane-bound c-type cytochromes from a facultative alkalophilic Bacillus J. Biochem. 110 1991 267 273
    • (1991) J. Biochem. , vol.110 , pp. 267-273
    • Yumoto, I.1    Fukumori, Y.2    Yamanaka, T.3
  • 101
    • 0015928945 scopus 로고
    • A theoretical model for the effects of local nonpolar heme environments on the redox potential in cytochromes
    • Kassner R.J. A theoretical model for the effects of local nonpolar heme environments on the redox potential in cytochromes J. Am. Chem. Soc. 95 1973 2674 2677
    • (1973) J. Am. Chem. Soc. , vol.95 , pp. 2674-2677
    • Kassner, R.J.1
  • 102
    • 0018853333 scopus 로고
    • PH dependence of the redox potential of Pseudomonas aeruginosa cytochrome c-551
    • Moore G.R., Pettigrew G.W., Pitt R.C., Williams R.J. pH dependence of the redox potential of Pseudomonas aeruginosa cytochrome c-551 Biochim. Biophys. Acta 590 1980 261 271
    • (1980) Biochim. Biophys. Acta , vol.590 , pp. 261-271
    • Moore, G.R.1    Pettigrew, G.W.2    Pitt, R.C.3    Williams, R.J.4
  • 103
    • 0021759421 scopus 로고
    • Structural basis for the variation of pH-dependent redox potential of Pseudomonas cytochrome c-551
    • Leitch F.A., Moore G.R., Pettigrew G.W. Structural basis for the variation of pH-dependent redox potential of Pseudomonas cytochrome c-551 Biochemistry 23 1984 1831 1838
    • (1984) Biochemistry , vol.23 , pp. 1831-1838
    • Leitch, F.A.1    Moore, G.R.2    Pettigrew, G.W.3
  • 104
    • 0028674194 scopus 로고
    • Inorganic microbial sulfur metabolism
    • Coutinho I.B., Xavier A.V. Inorganic microbial sulfur metabolism Methods Enzymol. 234 1994 119 140
    • (1994) Methods Enzymol. , vol.234 , pp. 119-140
    • Coutinho, I.B.1    Xavier, A.V.2
  • 107
    • 0023010550 scopus 로고
    • Energy transduction coupling mechanisms in multiredox center proteins
    • Xavier A.V. Energy transduction coupling mechanisms in multiredox center proteins J. Inorg. Biochem. 28 1986 239 243
    • (1986) J. Inorg. Biochem. , vol.28 , pp. 239-243
    • Xavier, A.V.1
  • 109
    • 0034795290 scopus 로고    scopus 로고
    • Proton-coupled electron transfer of cytochrome c
    • Murgida D.H., Hildebrandt P. Proton-coupled electron transfer of cytochrome c J. Am. Chem. Soc. 123 2001 4062 4068
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 4062-4068
    • Murgida, D.H.1    Hildebrandt, P.2
  • 110
    • 0019774523 scopus 로고
    • A respiration-dependent primary sodium extrusion system functioning at alkaline pH in the marine bacterium Vibrio alginolyticus
    • Tokuda H., Unemoto T. A respiration-dependent primary sodium extrusion system functioning at alkaline pH in the marine bacterium Vibrio alginolyticus Biochem. Biophys. Res. Commun. 102 1981 265 271
    • (1981) Biochem. Biophys. Res. Commun. , vol.102 , pp. 265-271
    • Tokuda, H.1    Unemoto, T.2
  • 111
    • 0021275705 scopus 로고
    • + is translocated at NADH: Quinone oxidoreductase segment in the respiratory chain of Vibrio alginolyticus
    • + is translocated at NADH: quinone oxidoreductase segment in the respiratory chain of Vibrio alginolyticus J. Biol. Chem. 259 1984 7785 7790
    • (1984) J. Biol. Chem. , vol.259 , pp. 7785-7790
    • Tokuda, H.1    Unemoto, T.2
  • 112
    • 0027332206 scopus 로고
    • Occurrence of teichurono peptide in cell walls of group 2 alkaliphilic Bacillus sp.
    • Aono R., Ito M., Horikoshi K. Occurrence of teichurono peptide in cell walls of group 2 alkaliphilic Bacillus sp. J. Gen. Microbiol. 139 1993 2738 2744
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 2738-2744
    • Aono, R.1    Ito, M.2    Horikoshi, K.3
  • 113
    • 0028863965 scopus 로고
    • A high cell wall negative charge is necessary for the growth of the alkaliphile Bacillus lentus C-125 at elevated pH
    • Aono R., Ito M., Joblin K.N., Horikoshi K. A high cell wall negative charge is necessary for the growth of the alkaliphile Bacillus lentus C-125 at elevated pH Microbiology 141 1995 2955 2964
    • (1995) Microbiology , vol.141 , pp. 2955-2964
    • Aono, R.1    Ito, M.2    Joblin, K.N.3    Horikoshi, K.4
  • 114
    • 0032729244 scopus 로고    scopus 로고
    • Contribution of the cell wall component teichuronopeptide to pH homeostasis and alkaliphily in the alkaliphile Bacillus lentus C-125
    • Aono R., Ito M., Machida T. Contribution of the cell wall component teichuronopeptide to pH homeostasis and alkaliphily in the alkaliphile Bacillus lentus C-125 J. Bacteriol. 181 1999 6600 6606
    • (1999) J. Bacteriol. , vol.181 , pp. 6600-6606
    • Aono, R.1    Ito, M.2    MacHida, T.3
  • 115
    • 0033764479 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis analyses of pH-dependent protein expression in facultatively alkaliphilic Bacillus pseudofirmus OF4 lead to characterization of an S-layer protein with a role in alkaliphily
    • Gilmore R., Messner P., Guffanti A.A., Kent R., Scheberl A., Kendrick N., Krulwich T.A. Two-dimensional gel electrophoresis analyses of pH-dependent protein expression in facultatively alkaliphilic Bacillus pseudofirmus OF4 lead to characterization of an S-layer protein with a role in alkaliphily J. Bacteriol. 182 2000 5969 5981
    • (2000) J. Bacteriol. , vol.182 , pp. 5969-5981
    • Gilmore, R.1    Messner, P.2    Guffanti, A.A.3    Kent, R.4    Scheberl, A.5    Kendrick, N.6    Krulwich, T.A.7
  • 116
    • 0023643136 scopus 로고
    • Spectral and potentiometric analysis of cytochromes from Bacillus subtilis
    • de Vrij W., van den Burg B., Konings W.N. Spectral and potentiometric analysis of cytochromes from Bacillus subtilis Eur. J. Biochem. 166 1987 589 595
    • (1987) Eur. J. Biochem. , vol.166 , pp. 589-595
    • De Vrij, W.1    Van Den Burg, B.2    Konings, W.N.3
  • 117
    • 11144249354 scopus 로고    scopus 로고
    • Characterization of steady-state activities of cytochrome c oxidase at alkaline pH: Mimicking the effect of K-channel mutations in the bovine enzyme
    • Riegler D., Shroyer L., Pokalsky C., Zaslavsky D., Gennis R., Prochaska L.J. Characterization of steady-state activities of cytochrome c oxidase at alkaline pH: mimicking the effect of K-channel mutations in the bovine enzyme Biochim. Biophys. Acta 1706 2005 126 133
    • (2005) Biochim. Biophys. Acta , vol.1706 , pp. 126-133
    • Riegler, D.1    Shroyer, L.2    Pokalsky, C.3    Zaslavsky, D.4    Gennis, R.5    Prochaska, L.J.6
  • 118
    • 0020631295 scopus 로고
    • Purification and properties of NADH dehydrogenase from an alkalophilic Bacillus
    • Hisae N., Aizawa K., Koyama N., Sekiguchi T., Nosoh Y. Purification and properties of NADH dehydrogenase from an alkalophilic Bacillus Biophys. Acta 743 1983 232 238
    • (1983) Biophys. Acta , vol.743 , pp. 232-238
    • Hisae, N.1    Aizawa, K.2    Koyama, N.3    Sekiguchi, T.4    Nosoh, Y.5
  • 119
    • 0025908097 scopus 로고
    • Nucleotide sequence of the gene encoding NADH dehydrogenase from an alkalophilic, Bacillus sp. YN-1
    • Xu X.M., Koyama N., Cui M., Yamagishi A., Nosoh Y., Oshima T. Nucleotide sequence of the gene encoding NADH dehydrogenase from an alkalophilic, Bacillus sp. YN-1 J. Biochem. 109 1991 678 683
    • (1991) J. Biochem. , vol.109 , pp. 678-683
    • Xu, X.M.1    Koyama, N.2    Cui, M.3    Yamagishi, A.4    Nosoh, Y.5    Oshima, T.6
  • 120
    • 0000619516 scopus 로고
    • Chemotaxonomic study of an alkalophilic bacterium, Exiguobacterium aurantiacum gen. nov., sp. nov.
    • Collins M.D., Lund B.M., Farrow J.A.E., Schleifer K.H. Chemotaxonomic study of an alkalophilic bacterium, Exiguobacterium aurantiacum gen. nov., sp. nov. J. Gen. Microbiol. 129 1983 2037 2042
    • (1983) J. Gen. Microbiol. , vol.129 , pp. 2037-2042
    • Collins, M.D.1    Lund, B.M.2    Farrow, J.A.E.3    Schleifer, K.H.4
  • 121
    • 0023909367 scopus 로고
    • Methanohalophilus zhilinae sp. nov., an alkaliphilic, halophilic, methylotrophic methanogen
    • Mathrai I.M., Boone D.R., Mah R.A., Fox G.E., Lau P.P. Methanohalophilus zhilinae sp. nov., an alkaliphilic, halophilic, methylotrophic methanogen Int. J. Syst. Bacteriol. 38 1988 139 142
    • (1988) Int. J. Syst. Bacteriol. , vol.38 , pp. 139-142
    • Mathrai, I.M.1    Boone, D.R.2    Mah, R.A.3    Fox, G.E.4    Lau, P.P.5
  • 122
    • 0027228137 scopus 로고
    • Isolation and characterization of moderately thermophilic anaerobic alkaliphile, Clostridium paradoxum sp. nov.
    • Li Y., Mandelco L., Wiegel J. Isolation and characterization of moderately thermophilic anaerobic alkaliphile, Clostridium paradoxum sp. nov. Int. J. Syst. Bacteriol. 43 1993 450 460
    • (1993) Int. J. Syst. Bacteriol. , vol.43 , pp. 450-460
    • Li, Y.1    Mandelco, L.2    Wiegel, J.3
  • 123
    • 0031670308 scopus 로고    scopus 로고
    • Isolation and characterization of novel facultatively alkaliphilic Nitrobacter species, N. alkalicus sp. nov.
    • Sorkin D.Y., Muyzer G., Brinkhoff T., Kuenen J.G., Jetten M.S.M. Isolation and characterization of novel facultatively alkaliphilic Nitrobacter species, N. alkalicus sp. nov. Arch. Microbiol. 170 1998 345 352
    • (1998) Arch. Microbiol. , vol.170 , pp. 345-352
    • Sorkin, D.Y.1    Muyzer, G.2    Brinkhoff, T.3    Kuenen, J.G.4    Jetten, M.S.M.5
  • 124
    • 0032872485 scopus 로고    scopus 로고
    • Heliorestis daurensis, gen. nov. sp. nov., an alkaliphilic rod-to-coiled-shaped phototrophic heliobacterium from a Siberian soda lake
    • Bryantseva I.A., Gorlenko V.M., Kompantseva E.I., Achenbach L.A., Madigan M.T. Heliorestis daurensis, gen. nov. sp. nov., an alkaliphilic rod-to-coiled-shaped phototrophic heliobacterium from a Siberian soda lake Arch. Microbiol. 172 1999 167 174
    • (1999) Arch. Microbiol. , vol.172 , pp. 167-174
    • Bryantseva, I.A.1    Gorlenko, V.M.2    Kompantseva, E.I.3    Achenbach, L.A.4    Madigan, M.T.5
  • 125
    • 0035910123 scopus 로고    scopus 로고
    • Ocenobacillus iheyenisis gen. nov., sp. nov., a deep-sea extremely halotolerant and alkaliphilic species isolated from a depth of 1050 m on the Iheya Ridge
    • Lu J., Nogi Y., Takami H. Ocenobacillus iheyenisis gen. nov., sp. nov., a deep-sea extremely halotolerant and alkaliphilic species isolated from a depth of 1050 m on the Iheya Ridge FEMS Microbiol. Lett. 205 2001 291 297
    • (2001) FEMS Microbiol. Lett. , vol.205 , pp. 291-297
    • Lu, J.1    Nogi, Y.2    Takami, H.3
  • 127
    • 0034993329 scopus 로고    scopus 로고
    • Alkalibacterium olivoapovliticus gen. nov., sp. nov., a new obligately alkaliphilic bacterium isolated from edible-olive wash-waters
    • Ntougias S., Russell N.J. Alkalibacterium olivoapovliticus gen. nov., sp. nov., a new obligately alkaliphilic bacterium isolated from edible-olive wash-waters Int. J. Syst. Evol. Microbiol. 51 2001 1161 1170
    • (2001) Int. J. Syst. Evol. Microbiol. , vol.51 , pp. 1161-1170
    • Ntougias, S.1    Russell, N.J.2
  • 128
    • 0035196802 scopus 로고    scopus 로고
    • Alcalilimnicola halodurans gen. nov., sp. nov., analkaliphilic, moderately halophilic and extremely halotolerant bacterium, isolated from sediments of soda-depositing Lake Natron, East Africa Rift Valley
    • Yakimov M.M., Giuliano L., Chernikova T.N., Gentile G., Abraham W.-R., Lüsdorf H., Timmis K.N., Golyshin P.N. Alcalilimnicola halodurans gen. nov., sp. nov., analkaliphilic, moderately halophilic and extremely halotolerant bacterium, isolated from sediments of soda-depositing Lake Natron, East Africa Rift Valley Int. J. Syst. Evol. Microbiol. 51 2001 2133 2143
    • (2001) Int. J. Syst. Evol. Microbiol. , vol.51 , pp. 2133-2143
    • Yakimov, M.M.1    Giuliano, L.2    Chernikova, T.N.3    Gentile, G.4    Abraham, W.-R.5    Lüsdorf, H.6    Timmis, K.N.7    Golyshin, P.N.8
  • 131
    • 0141706881 scopus 로고    scopus 로고
    • Anoxybacillus gonensis sp. nov., a moderately thermophilic, xylose-utilizing, edospore-forming
    • Belduz A.O., Dulger S., Demirbag Z. Anoxybacillus gonensis sp. nov., a moderately thermophilic, xylose-utilizing, edospore-forming Int. J. Syst. Evol. Microbiol. 53 2003 1315 1320
    • (2003) Int. J. Syst. Evol. Microbiol. , vol.53 , pp. 1315-1320
    • Belduz, A.O.1    Dulger, S.2    Demirbag, Z.3
  • 132
    • 4644362851 scopus 로고    scopus 로고
    • Alkaline anerobic respiration: Isolation and characterization of a novel alkaliphilic and metal-reducing bacterium
    • Ye Q., Roh Y., Carrol S.L., Blair B., Zhou J., Zhang C.L., Fields M.W. Alkaline anerobic respiration: isolation and characterization of a novel alkaliphilic and metal-reducing bacterium Appl. Environ. Microbiol. 70 2004 5595 5602
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 5595-5602
    • Ye, Q.1    Roh, Y.2    Carrol, S.L.3    Blair, B.4    Zhou, J.5    Zhang, C.L.6    Fields, M.W.7
  • 133
    • 9744244884 scopus 로고    scopus 로고
    • Alkalibacterium psychrotolerans sp. nov., a psychrotolerant obligate alkaliphile that reduces an indigo dye
    • Yumoto I., Hirota K., Nodasaka Y., Yokota Y., Hoshino T., Nakajima K. Alkalibacterium psychrotolerans sp. nov., a psychrotolerant obligate alkaliphile that reduces an indigo dye Int. J. Syst. Evol. Microbiol. 54 2004 2379 2383
    • (2004) Int. J. Syst. Evol. Microbiol. , vol.54 , pp. 2379-2383
    • Yumoto, I.1    Hirota, K.2    Nodasaka, Y.3    Yokota, Y.4    Hoshino, T.5    Nakajima, K.6


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