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Volumn 293, Issue 2, 1999, Pages 343-350

Structural bioenergetics and energy transduction mechanisms

Author keywords

Biological energy transduction; G proteins; Nitrogenase; Nucleotide switch proteins

Indexed keywords

ADENOSINE TRIPHOSPHATE; GUANINE NUCLEOTIDE BINDING PROTEIN; NITROGENASE; NUCLEOTIDE; PROTEIN;

EID: 0032751576     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3005     Document Type: Article
Times cited : (48)

References (37)
  • 1
    • 0028246242 scopus 로고
    • Thermodynamics of nitrogenase reactions
    • Alberty R. A. Thermodynamics of nitrogenase reactions. J. Biol. Chem. 269:1994;7099-7102.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7099-7102
    • Alberty, R.A.1
  • 2
    • 0000913086 scopus 로고
    • A fast algorithm for rendering space-filling molecule pictures
    • Bacon D. J., Anderson W. F. A fast algorithm for rendering space-filling molecule pictures. J. Mol. Graph. 6:1988;219-220.
    • (1988) J. Mol. Graph. , vol.6 , pp. 219-220
    • Bacon, D.J.1    Anderson, W.F.2
  • 4
    • 0032544491 scopus 로고    scopus 로고
    • Energy, life and ATP
    • Boyer P. D. Energy, life and ATP. Angew Chem. Int. Edit. 37:1998;2996-2307.
    • (1998) Angew Chem. Int. Edit. , vol.37 , pp. 2996-2307
    • Boyer, P.D.1
  • 5
    • 0000703950 scopus 로고    scopus 로고
    • Mechanism of molybdenum nitrogenase
    • Burgess B. K., Lowe D. J. Mechanism of molybdenum nitrogenase. Chem. Rev. 96:1996;2983-3011.
    • (1996) Chem. Rev. , vol.96 , pp. 2983-3011
    • Burgess, B.K.1    Lowe, D.J.2
  • 9
    • 0026662162 scopus 로고
    • Crystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii
    • Georgiadis M. M., Komiya H., Chakrabarti P., Woo D., Kornuc J. J., Rees D. C. Crystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii. Science. 257:1992;1653-1659.
    • (1992) Science , vol.257 , pp. 1653-1659
    • Georgiadis, M.M.1    Komiya, H.2    Chakrabarti, P.3    Woo, D.4    Kornuc, J.J.5    Rees, D.C.6
  • 13
    • 7744224797 scopus 로고    scopus 로고
    • Structural basis of biological nitrogen fixation
    • Howard J. B., Rees D. C. Structural basis of biological nitrogen fixation. Chem. Rev. 96:1996;2965-2982.
    • (1996) Chem. Rev. , vol.96 , pp. 2965-2982
    • Howard, J.B.1    Rees, D.C.2
  • 14
    • 84893482610 scopus 로고
    • A solution for the best rotation to relate two sets of vectors
    • Kabsch W. A solution for the best rotation to relate two sets of vectors. Acta Crystallog. sect. A. 32:1976;922-923.
    • (1976) Acta Crystallog. Sect. a , vol.32 , pp. 922-923
    • Kabsch, W.1
  • 15
    • 0029958571 scopus 로고    scopus 로고
    • The GTP binding motif: Variations on a theme
    • Kjeldgaard M., Nyborg J., Clark B. F. C. The GTP binding motif: variations on a theme. FASEB J. 10:1996;1347-1368.
    • (1996) FASEB J. , vol.10 , pp. 1347-1368
    • Kjeldgaard, M.1    Nyborg, J.2    Clark, B.F.C.3
  • 16
    • 0026244229 scopus 로고
    • MOLSCRIPT - A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. J. MOLSCRIPT - a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 17
    • 0029781354 scopus 로고    scopus 로고
    • Ras-catalyzed hydrolysis of GTP: A new perspective from model studies
    • Maegley K. A., Admiraal S. J., Herschlag D. Ras-catalyzed hydrolysis of GTP: a new perspective from model studies. Proc. Natl Acad. Sci. USA. 93:1996;8160-8166.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 8160-8166
    • Maegley, K.A.1    Admiraal, S.J.2    Herschlag, D.3
  • 18
    • 0032522882 scopus 로고    scopus 로고
    • How do kinases transfer phosphoryl groups?
    • Matte A., Tari L. W., Delbaere L. T. J. How do kinases transfer phosphoryl groups? Structure. 6:1998;413-419.
    • (1998) Structure , vol.6 , pp. 413-419
    • Matte, A.1    Tari, L.W.2    Delbaere, L.T.J.3
  • 19
    • 0028057108 scopus 로고
    • Raster3D Version 2.0 - A program for photorealistic molecular graphics
    • Merritt E. A., Murphy M. E. P. Raster3D Version 2.0 - a program for photorealistic molecular graphics. Acta Crystallog. sect. D. 50:1994;869-873.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 20
    • 0025117674 scopus 로고
    • Molecular switch for signal transduction - structural differences between active and inactive forms of protooncogenic ras proteins
    • Milburn M. V., Tong L., De Vos A. M., Brunger A., Yamaizumi Z., Nishimura S., Kim S. H. Molecular switch for signal transduction - structural differences between active and inactive forms of protooncogenic ras proteins. Science. 247:1990;939-945.
    • (1990) Science , vol.247 , pp. 939-945
    • Milburn, M.V.1    Tong, L.2    De Vos, A.M.3    Brunger, A.4    Yamaizumi, Z.5    Nishimura, S.6    Kim, S.H.7
  • 21
    • 0018784261 scopus 로고
    • Keilin's respiratory chain concept and its chemiosmotic consequences
    • Mitchell P. Keilin's respiratory chain concept and its chemiosmotic consequences. Science. 206:1979;1148-1159.
    • (1979) Science , vol.206 , pp. 1148-1159
    • Mitchell, P.1
  • 22
  • 24
    • 0024463212 scopus 로고
    • Structure of the guanine-nucleotide binding domain of the HA-ras oncogene product p21 in the triphosphate conformation
    • Pai E. F., Kabsch W., Krengel U., Holmes K. C., John J., Wittinghofer A. Structure of the guanine-nucleotide binding domain of the HA-ras oncogene product p21 in the triphosphate conformation. Nature. 341:1989;209-214.
    • (1989) Nature , vol.341 , pp. 209-214
    • Pai, E.F.1    Kabsch, W.2    Krengel, U.3    Holmes, K.C.4    John, J.5    Wittinghofer, A.6
  • 25
    • 0030061189 scopus 로고    scopus 로고
    • The structural basis of the myosin ATPase activity
    • Rayment I. The structural basis of the myosin ATPase activity. J. Biol. Chem. 271:1996;15850-15853.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15850-15853
    • Rayment, I.1
  • 29
    • 0030920782 scopus 로고    scopus 로고
    • G protein mechanisms: Insights from structural analysis
    • Sprang S. R. G protein mechanisms: insights from structural analysis. Annu. Rev. Biochem. 66:1997;639-678.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 639-678
    • Sprang, S.R.1
  • 30
    • 0019921514 scopus 로고
    • Aluminum: A requirement for activation of the regulatory component of adenylate cyclase by fluoride
    • Steinweis P. C., Gilman A. G. Aluminum: a requirement for activation of the regulatory component of adenylate cyclase by fluoride. Proc. Natl Acad. Sci. USA. 79:1982;4888-4891.
    • (1982) Proc. Natl Acad. Sci. USA , vol.79 , pp. 4888-4891
    • Steinweis, P.C.1    Gilman, A.G.2
  • 31
    • 0032214622 scopus 로고    scopus 로고
    • Protein Data Bank (PDB): Database of three-dimensional structural information of biological macromolecules
    • Sussman J., Lin D., Jiang J., Manning N., Prilusky J., Ritter O., Abola E. Protein Data Bank (PDB): database of three-dimensional structural information of biological macromolecules. Acta Crystallog. sect. D. 54:1998;1078-1084.
    • (1998) Acta Crystallog. Sect. D , vol.54 , pp. 1078-1084
    • Sussman, J.1    Lin, D.2    Jiang, J.3    Manning, N.4    Prilusky, J.5    Ritter, O.6    Abola, E.7
  • 32
    • 0020669965 scopus 로고
    • Mechanism of free energy coupling in active transport
    • Tanford C. Mechanism of free energy coupling in active transport. Annu. Rev. Biochem. 52:1983;379-409.
    • (1983) Annu. Rev. Biochem. , vol.52 , pp. 379-409
    • Tanford, C.1
  • 34
    • 0032544312 scopus 로고    scopus 로고
    • ATP synthesis by rotary catalysis
    • Walker J. E. ATP synthesis by rotary catalysis. Angew Chem. Int. Edit. 37:1998;2309-2319.
    • (1998) Angew Chem. Int. Edit. , vol.37 , pp. 2309-2319
    • Walker, J.E.1
  • 35
    • 0001607723 scopus 로고
    • Distantly related sequences in the α- And β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker J. E., Saraste M., Runswick M. J., Gay N. J. Distantly related sequences in the α- and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 8:1982;945-981.
    • (1982) EMBO J. , vol.8 , pp. 945-981
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 36
    • 0030744604 scopus 로고    scopus 로고
    • Electron tunneling in proteins: Role of the intervening medium
    • Winkler J. R., Gray H. B. Electron tunneling in proteins: role of the intervening medium. J. Biol. Inorg. Chem. 2:1997;399-404.
    • (1997) J. Biol. Inorg. Chem. , vol.2 , pp. 399-404
    • Winkler, J.R.1    Gray, H.B.2
  • 37
    • 0031282504 scopus 로고    scopus 로고
    • Signalling mechanistics: Aluminium fluoride for molecule of the year
    • Wittinghofer A. Signalling mechanistics: Aluminium fluoride for molecule of the year. Curr. Biol. 7:1997;R682-R685.
    • (1997) Curr. Biol. , vol.7
    • Wittinghofer, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.