메뉴 건너뛰기




Volumn 28, Issue 4, 1997, Pages 580-585

Crystals of cytochrome c-553 from Bacillus pasteurii show diffraction to 0.97 Å Resolution

Author keywords

B. pasteurii; Crystallization; Cytochrome C553; Electron transfer; Gram positive; Purification; X ray diffraction

Indexed keywords

CYTOCHROME C;

EID: 0030746129     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199708)28:4<580::AID-PROT11>3.0.CO;2-C     Document Type: Article
Times cited : (9)

References (34)
  • 1
    • 1842313590 scopus 로고
    • An investigation of the Bacillus pasteurii group. III. Systematic relationship of the group
    • Gibson, T. An investigation of the Bacillus pasteurii group. III. Systematic relationship of the group. J. Bacteriol. 29:491-502, 1935.
    • (1935) J. Bacteriol. , vol.29 , pp. 491-502
    • Gibson, T.1
  • 2
    • 0000289253 scopus 로고
    • Requirement of an alkaline pH and ammonia for substrate oxidation by Bacillus pasteurii
    • Wiley, W.R., Stokes, J.L. Requirement of an alkaline pH and ammonia for substrate oxidation by Bacillus pasteurii. J. Bacteriol. 84:730-734, 1962.
    • (1962) J. Bacteriol. , vol.84 , pp. 730-734
    • Wiley, W.R.1    Stokes, J.L.2
  • 3
    • 0000277082 scopus 로고
    • Effect of pH and ammonium ions on the permeability of Bacillus pasteurii
    • Wiley, W.R., Stokes, J.L. Effect of pH and ammonium ions on the permeability of Bacillus pasteurii. J. Bacteriol. 86:1152-1156, 1963.
    • (1963) J. Bacteriol. , vol.86 , pp. 1152-1156
    • Wiley, W.R.1    Stokes, J.L.2
  • 4
    • 0002374114 scopus 로고
    • Purification and properties of bacterial urease
    • Larson, A.D., Kallio, R.E. Purification and properties of bacterial urease. J. Bacteriol. 68:67-73, 1954.
    • (1954) J. Bacteriol. , vol.68 , pp. 67-73
    • Larson, A.D.1    Kallio, R.E.2
  • 5
    • 0000764318 scopus 로고
    • Urea-hydrolyzing bacilli. I. A physiological approach to identification
    • Bornside, G.H., Kallio, R.E. Urea-hydrolyzing bacilli. I. A physiological approach to identification. J. Bacteriol. 71: 627-634, 1956.
    • (1956) J. Bacteriol. , vol.71 , pp. 627-634
    • Bornside, G.H.1    Kallio, R.E.2
  • 6
    • 0017147023 scopus 로고
    • Electron transport in the alkalophile Bacillus pasteurii (N.C.I.B. 8841)
    • Haddock, B.A., Cobley, J.G. Electron transport in the alkalophile Bacillus pasteurii (N.C.I.B. 8841). Biochem. Soc. Trans. 4:709-711, 1976.
    • (1976) Biochem. Soc. Trans. , vol.4 , pp. 709-711
    • Haddock, B.A.1    Cobley, J.G.2
  • 7
    • 0018064571 scopus 로고
    • The respiratory chain and proton electrochemical gradient in the alkalophile Bacillus pasteurii
    • Hoddinott, M.H., Reid, G.A., Ingledew, W.J. The respiratory chain and proton electrochemical gradient in the alkalophile Bacillus pasteurii. Biochem. Soc. Trans. 6:1295-1298, 1978.
    • (1978) Biochem. Soc. Trans. , vol.6 , pp. 1295-1298
    • Hoddinott, M.H.1    Reid, G.A.2    Ingledew, W.J.3
  • 8
    • 0030069642 scopus 로고    scopus 로고
    • Ammonium/urea-dependent generation of a proton electrochemical potential and synthesis of ATP in Bacillus pasteurii
    • Jahns, T. Ammonium/urea-dependent generation of a proton electrochemical potential and synthesis of ATP in Bacillus pasteurii. J. Bacteriol. 178:403-409, 1996.
    • (1996) J. Bacteriol. , vol.178 , pp. 403-409
    • Jahns, T.1
  • 9
    • 0030160824 scopus 로고    scopus 로고
    • Bacillus pasteurii urease: An heteropolymeric enzyme with a binuclear nickel active site
    • Benini, S., Gessa, C., Ciurli, S. Bacillus pasteurii urease: An heteropolymeric enzyme with a binuclear nickel active site. Soil Biol. Biochem. 28:819-821, 1996.
    • (1996) Soil Biol. Biochem. , vol.28 , pp. 819-821
    • Benini, S.1    Gessa, C.2    Ciurli, S.3
  • 10
    • 0029984803 scopus 로고    scopus 로고
    • X-ray absorption spectroscopy study of native and phenylphosphorodiamidate-inhibited Bacillus pasteurii urease
    • Benini, S., Ciurli, S., Nolting, H.F., Mangani, S. X-ray absorption spectroscopy study of native and phenylphosphorodiamidate-inhibited Bacillus pasteurii urease. Eur. J. Biochem. 239:61-66, 1996.
    • (1996) Eur. J. Biochem. , vol.239 , pp. 61-66
    • Benini, S.1    Ciurli, S.2    Nolting, H.F.3    Mangani, S.4
  • 11
    • 0017854856 scopus 로고
    • The protonmotive force and α-aminoisobutyric acid transport in an obligately alkalophilic bacterium
    • Guffanti, A.A., Susman, P., Blanco, R., Krulwich, T.A. The protonmotive force and α-aminoisobutyric acid transport in an obligately alkalophilic bacterium. J. Biol. Chem. 253: 708-715, 1978.
    • (1978) J. Biol. Chem. , vol.253 , pp. 708-715
    • Guffanti, A.A.1    Susman, P.2    Blanco, R.3    Krulwich, T.A.4
  • 12
    • 0018975140 scopus 로고
    • Alkalophiles have much higher cytochrome contents than conventional bacteria and than their own non-alkalophilic mutant derivatives
    • Lewis, R.J., Belkina, S., Krulwich, T.A. Alkalophiles have much higher cytochrome contents than conventional bacteria and than their own non-alkalophilic mutant derivatives. Biochem. Biophys. Res. Commun. 95:857-863, 1980.
    • (1980) Biochem. Biophys. Res. Commun. , vol.95 , pp. 857-863
    • Lewis, R.J.1    Belkina, S.2    Krulwich, T.A.3
  • 13
    • 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. 110:267-273, 1991.
    • (1991) J. Biochem. , vol.110 , pp. 267-273
    • Yumoto, I.1    Fukumori, Y.2    Yamanaka, T.3
  • 14
    • 0028999635 scopus 로고
    • The respiratory chain of alkaliphilic bacteria
    • Hicks, D.B., Krulwich, T.A. The respiratory chain of alkaliphilic bacteria. Biochim. Biophys. Acta 1229:303-314, 1995.
    • (1995) Biochim. Biophys. Acta , vol.1229 , pp. 303-314
    • Hicks, D.B.1    Krulwich, T.A.2
  • 15
    • 0019820594 scopus 로고
    • The respiratory chain of Bacillus alcalophilus and its nonalkalophilic mutant derivative
    • Lewis, R.J., Prince, R.C., Dutton, P.L., Knaff, D.B., Krulwich, T.A. The respiratory chain of Bacillus alcalophilus and its nonalkalophilic mutant derivative. J. Biol. Chem. 256:10543-10549, 1981.
    • (1981) J. Biol. Chem. , vol.256 , pp. 10543-10549
    • Lewis, R.J.1    Prince, R.C.2    Dutton, P.L.3    Knaff, D.B.4    Krulwich, T.A.5
  • 16
    • 0020558032 scopus 로고
    • Respiratory chain of the alkalophilic bacterium Bacillus firmus RAB and its nonalkalophilic mutant derivatives
    • Kitada, M., Lewis, R.J., Krulwich, T.A. Respiratory chain of the alkalophilic bacterium Bacillus firmus RAB and its nonalkalophilic mutant derivatives. J. Bacteriol. 154:330-335, 1983.
    • (1983) J. Bacteriol. , vol.154 , pp. 330-335
    • Kitada, M.1    Lewis, R.J.2    Krulwich, T.A.3
  • 17
    • 0018474704 scopus 로고
    • Purification, physicochemical properties, and localization of cytochrome c in energy-transducing membranes from Mycobacterium phlei
    • Jacobs, A.J., Kalra, V.K., Cavari, B., Brodie, A.F. Purification, physicochemical properties, and localization of cytochrome c in energy-transducing membranes from Mycobacterium phlei. Arch. Biochem. Biophys. 194:531-541, 1979.
    • (1979) Arch. Biochem. Biophys. , vol.194 , pp. 531-541
    • Jacobs, A.J.1    Kalra, V.K.2    Cavari, B.3    Brodie, A.F.4
  • 18
    • 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. 254:376-379, 1987.
    • (1987) Arch. Biochem. Biophys. , vol.254 , pp. 376-379
    • Woolley, K.J.1
  • 19
    • 0024284303 scopus 로고
    • Purification and characterization of two soluble cytochromes from the alkalophile Bacillus firmus RAB
    • Davidson, M.W., Gray, K.A., Knaff, D.E., Krulwich, T.A. Purification and characterization of two soluble cytochromes from the alkalophile Bacillus firmus RAB. Biochim. Biophys. Acta 933:470-477, 1988.
    • (1988) Biochim. Biophys. Acta , vol.933 , pp. 470-477
    • Davidson, M.W.1    Gray, K.A.2    Knaff, D.E.3    Krulwich, T.A.4
  • 20
    • 0024331619 scopus 로고
    • Cytochrome c-551 from the thermophilic bacterium PS3 grown under air-limited conditions
    • Sone, N., Kutoh, E., Yanagita, Y. Cytochrome c-551 from the thermophilic bacterium PS3 grown under air-limited conditions. Biochim. Biophys. Acta 977:329-334, 1989.
    • (1989) Biochim. Biophys. Acta , vol.977 , pp. 329-334
    • Sone, N.1    Kutoh, E.2    Yanagita, Y.3
  • 21
    • 0024997335 scopus 로고
    • Bacillus subtilis 13-kilodalton cytochrome c-550 encoded by ccc a consist of a membrane-anchor and heme domain
    • von Wachenfeldt, C., Hederstedt, L. Bacillus subtilis 13-kilodalton cytochrome c-550 encoded by ccc A consist of a membrane-anchor and heme domain. J. Biol. Chem. 265: 13939-13948, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 13939-13948
    • Von Wachenfeldt, C.1    Hederstedt, L.2
  • 22
    • 0025907364 scopus 로고
    • Two structurally different cytochromes c from Bacillus azotoformans: On the evolution of gram-positive bacteria
    • Hreggvidsson, G.O. Two structurally different cytochromes c from Bacillus azotoformans: On the evolution of gram-positive bacteria. Biochim. Biophys. Acta 1058:52-55, 1991.
    • (1991) Biochim. Biophys. Acta , vol.1058 , pp. 52-55
    • Hreggvidsson, G.O.1
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685, 1970.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0017170673 scopus 로고
    • An improved staining procedure for the detection of the peroxidase activity of cytochrome P-450 on sodium dodecyl sulfate polyacrylamide gels
    • Thomas, P.E., Ryan, D., Levin, W. An improved staining procedure for the detection of the peroxidase activity of cytochrome P-450 on sodium dodecyl sulfate polyacrylamide gels. Anal. Biochem. 75:168-176, 1976.
    • (1976) Anal. Biochem. , vol.75 , pp. 168-176
    • Thomas, P.E.1    Ryan, D.2    Levin, W.3
  • 26
    • 0013769988 scopus 로고
    • Estimation of molecular weights of proteins by sephadex gel-filtration
    • Andrews, P. Estimation of molecular weights of proteins by sephadex gel-filtration. Biochem. J. 91:222-233, 1964.
    • (1964) Biochem. J. , vol.91 , pp. 222-233
    • Andrews, P.1
  • 27
    • 0017258707 scopus 로고
    • Primary structure of a high potential iron-sulfur protein from the purple non-sulfur photosynthetic bacterium Rhodopseudomonas gelatinosa
    • Tedro, S.M., Meyer, T.E., Kamen, M.D. Primary structure of a high potential iron-sulfur protein from the purple non-sulfur photosynthetic bacterium Rhodopseudomonas gelatinosa. J. Biol. Chem. 251:129-136, 1976.
    • (1976) J. Biol. Chem. , vol.251 , pp. 129-136
    • Tedro, S.M.1    Meyer, T.E.2    Kamen, M.D.3
  • 29
    • 0003615263 scopus 로고
    • Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT
    • Gewirth, D., Otwinowski, Z., Minor, W. "The HKL Manual." Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, 1995.
    • (1995) The HKL Manual
    • Gewirth, D.1    Otwinowski, Z.2    Minor, W.3
  • 30
    • 24544444855 scopus 로고
    • Intensity statistics
    • Rees, D.C. Intensity statistics. Acta Cryst. Sect. A. 50:157-163, 1980.
    • (1980) Acta Cryst. Sect. A. , vol.50 , pp. 157-163
    • Rees, D.C.1
  • 31
    • 0025366965 scopus 로고
    • Cryocrystallography of biological macromolecules at ultra-low temperature
    • Hope, H. Cryocrystallography of biological macromolecules at ultra-low temperature. Annu. Rev. Biophys. Biophys. Chem. 19:107-126, 1990.
    • (1990) Annu. Rev. Biophys. Biophys. Chem. , vol.19 , pp. 107-126
    • Hope, H.1
  • 32
    • 0000722358 scopus 로고
    • Macromolecular crystallography at cryogenic temperatures
    • Watenpaugh, K.D. Macromolecular crystallography at cryogenic temperatures. Curr. Opin. Struct. Biol. 1:1012-1015, 1991.
    • (1991) Curr. Opin. Struct. Biol. , vol.1 , pp. 1012-1015
    • Watenpaugh, K.D.1
  • 33
    • 0028774714 scopus 로고
    • Cryocrystallography
    • Rogers, D.W. Cryocrystallography. Structure 2:1135-1139, 1994.
    • (1994) Structure , vol.2 , pp. 1135-1139
    • Rogers, D.W.1
  • 34
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews, B.W. Solvent content of protein crystals. J. Mol. Biol. 33:491-497, 1968.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.