메뉴 건너뛰기




Volumn 405, Issue 6788, 2000, Pages 814-817

Atomically defined mechanism for proton transfer to a buried redox centre in a protein

Author keywords

[No Author keywords available]

Indexed keywords

FERREDOXIN; IRON SULFUR PROTEIN; M PROTEIN;

EID: 0034659779     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/35015610     Document Type: Article
Times cited : (149)

References (30)
  • 2
    • 0032143387 scopus 로고    scopus 로고
    • Proton translocation by bacteriorhodopsin and heme-copper oxidases
    • Wikström, M. Proton translocation by bacteriorhodopsin and heme-copper oxidases. Curr. Opin. Struct. Biol. 8, 480-488 (1998).
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 480-488
    • Wikström, M.1
  • 3
    • 0032573052 scopus 로고    scopus 로고
    • How does cytochrome oxidase pump protons?
    • Gennis, R. B. How does cytochrome oxidase pump protons? Proc. Natl Acad. Sci. USA 95, 12747-12749 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 12747-12749
    • Gennis, R.B.1
  • 4
    • 0031827676 scopus 로고    scopus 로고
    • Cytochrome oxidase: Pathways for electron tunneling and proton transfer
    • Malmström, B. G. Cytochrome oxidase: pathways for electron tunneling and proton transfer. J. Biol. Inorg. Chem. 3, 339-343 (1998).
    • (1998) J. Biol. Inorg. Chem. , vol.3 , pp. 339-343
    • Malmström, B.G.1
  • 5
    • 0032573072 scopus 로고    scopus 로고
    • The mechanism of proton pumping by cytochrome c oxidase
    • Michel, H. The mechanism of proton pumping by cytochrome c oxidase. Proc. Natl Acad. Sci. USA 95, 12819-12824 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 12819-12824
    • Michel, H.1
  • 6
    • 0032492706 scopus 로고    scopus 로고
    • Bacteriorhodopsins intramolecular proton-release pathway consists of a hydrogen-bonded network
    • Rammelsberg, R., Huhn, G., Lübben, M. & Gerwert, K. Bacteriorhodopsins intramolecular proton-release pathway consists of a hydrogen-bonded network. Biochemistry 37, 5001-5009 (1998).
    • (1998) Biochemistry , vol.37 , pp. 5001-5009
    • Rammelsberg, R.1    Huhn, G.2    Lübben, M.3    Gerwert, K.4
  • 7
    • 0033536594 scopus 로고    scopus 로고
    • Structural changes in bacteriorhodopsin during ion transport at 2 Å resolution
    • Luecke, H., Schobert, B., Richter, H.-T., Cartailler, J. P. & Lanyi, J. Structural changes in bacteriorhodopsin during ion transport at 2 Å resolution. Science 286, 255-260 (1999).
    • (1999) Science , vol.286 , pp. 255-260
    • Luecke, H.1    Schobert, B.2    Richter, H.-T.3    Cartailler, J.P.4    Lanyi, J.5
  • 8
    • 0032514770 scopus 로고    scopus 로고
    • 8) in bacterial reaction centres from Rhodobacter sphaeroides: FTIR studies on the effects of replacing Glu H173
    • 8) in bacterial reaction centres from Rhodobacter sphaeroides: FTIR studies on the effects of replacing Glu H173. Biochemistry 37, 14457-14462 (1998).
    • (1998) Biochemistry , vol.37 , pp. 14457-14462
    • Nabedryk, E.1    Breton, J.2    Okamura, M.Y.3    Paddock, M.L.4
  • 9
    • 18144447465 scopus 로고    scopus 로고
    • Redox-coupled crystal structural changes in bovine heart cytochrome c oxidase
    • Yoshikawa, S. et al. Redox-coupled crystal structural changes in bovine heart cytochrome c oxidase. Science 280, 1723-1729 (1998).
    • (1998) Science , vol.280 , pp. 1723-1729
    • Yoshikawa, S.1
  • 10
    • 0030745897 scopus 로고    scopus 로고
    • The roles of two proton input channels in cytochrome c oxidase from Rhodobacter sphaeroides probed by the effects of site-directed mutations on time-resolved electrogenic intraprotein proton transfer
    • Konstantinov, A. A., Siletsky, S., Mitchell, D., Kaulen, A. & Gennis, R. B. The roles of two proton input channels in cytochrome c oxidase from Rhodobacter sphaeroides probed by the effects of site-directed mutations on time-resolved electrogenic intraprotein proton transfer. Proc. Natl Acad. Sci. USA 94, 9085-9090 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 9085-9090
    • Konstantinov, A.A.1    Siletsky, S.2    Mitchell, D.3    Kaulen, A.4    Gennis, R.B.5
  • 12
    • 17344382320 scopus 로고    scopus 로고
    • Effects of mutation of the conserved glutamic acid-286 in subunit I of cytochrome c oxidase from Rhodobacter sphaeroides
    • Junemann, S., Meunier, B., Fisher, N. & Rich, P. R. Effects of mutation of the conserved glutamic acid-286 in subunit I of cytochrome c oxidase from Rhodobacter sphaeroides. Biochemistry 38, 5248-5255 (1999).
    • (1999) Biochemistry , vol.38 , pp. 5248-5255
    • Junemann, S.1    Meunier, B.2    Fisher, N.3    Rich, P.R.4
  • 13
    • 0032558152 scopus 로고    scopus 로고
    • Kinetics and mechanism of redox-coupled, long-range proton transfer in an iron-sulfur protein. Investigation by fast-scan protein-film voltammetry
    • Hirst, J. et al. Kinetics and mechanism of redox-coupled, long-range proton transfer in an iron-sulfur protein. Investigation by fast-scan protein-film voltammetry. J. Am. Chem. Soc. 120, 7085-7094 (1998).
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 7085-7094
    • Hirst, J.1
  • 14
    • 0027082924 scopus 로고
    • Internal water molecules and H-bonding in biological macromolecules: A review of structural features with functional implications
    • Meyer, E. Internal water molecules and H-bonding in biological macromolecules: a review of structural features with functional implications. Protein Sci. 1, 1543-1562 (1992).
    • (1992) Protein Sci. , vol.1 , pp. 1543-1562
    • Meyer, E.1
  • 16
    • 0033523919 scopus 로고    scopus 로고
    • Natural engineering principles of electron tunnelling in biological oxidation-reduction
    • Page, C. G., Moser, C. C., Chen, X. & Dutton, P. L. Natural engineering principles of electron tunnelling in biological oxidation-reduction. Nature 402, 47-52 (1999).
    • (1999) Nature , vol.402 , pp. 47-52
    • Page, C.G.1    Moser, C.C.2    Chen, X.3    Dutton, P.L.4
  • 17
    • 0024723235 scopus 로고
    • Quantum mechanical effects in enzyme-catalyzed hydrogen transfer reactions
    • Klinman, J. P. Quantum mechanical effects in enzyme-catalyzed hydrogen transfer reactions. Trends Biochem. Sci. 14, 368-373 (1989).
    • (1989) Trends Biochem. Sci. , vol.14 , pp. 368-373
    • Klinman, J.P.1
  • 18
    • 0029098354 scopus 로고
    • The dynamics of proton exchange between bulk and surface groups
    • Gutman, M. & Nachliel, E. The dynamics of proton exchange between bulk and surface groups. Biochim. Biophys. Acta 1231, 123-138 (1995).
    • (1995) Biochim. Biophys. Acta , vol.1231 , pp. 123-138
    • Gutman, M.1    Nachliel, E.2
  • 19
    • 0027518193 scopus 로고
    • Azotobacter vinelandii ferredoxin I. Aspartate 15 facilitates proton transfer to the reduced [3Fe-4S] cluster
    • Shen, B. et al. Azotobacter vinelandii ferredoxin I. Aspartate 15 facilitates proton transfer to the reduced [3Fe-4S] cluster. J. Biol. Chem. 268, 25928-25939 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 25928-25939
    • Shen, B.1
  • 20
    • 0027374490 scopus 로고
    • Crystal structures of oxidized and reduced Azotobacter vinelandii ferredoxin at pH8 and 6
    • Stout, C. D. Crystal structures of oxidized and reduced Azotobacter vinelandii ferredoxin at pH8 and 6. J. Biol. Chem. 268, 25920-25927 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 25920-25927
    • Stout, C.D.1
  • 21
    • 0032496372 scopus 로고    scopus 로고
    • Structure of Azotobacter vinelandii 7Fe ferredoxin at 1.35 Å resolution and determination of the [Fe-S] bonds with 0.01 Å accuracy
    • Stout, C. D., Stura, E. A. & McRee, D. E. Structure of Azotobacter vinelandii 7Fe ferredoxin at 1.35 Å resolution and determination of the [Fe-S] bonds with 0.01 Å accuracy. J. Mol. Biol. 278, 629-639 (1998).
    • (1998) J. Mol. Biol. , vol.278 , pp. 629-639
    • Stout, C.D.1    Stura, E.A.2    McRee, D.E.3
  • 23
    • 33846281497 scopus 로고    scopus 로고
    • Reactions of complex metalloproteins studied by protein-film voltammetry
    • Armstrong, F. A., Heering, H. A. & Hirst, J. Reactions of complex metalloproteins studied by protein-film voltammetry. Chem. Soc. Rev. 26, 169-179 (1997).
    • (1997) Chem. Soc. Rev. , vol.26 , pp. 169-179
    • Armstrong, F.A.1    Heering, H.A.2    Hirst, J.3
  • 24
    • 0025729928 scopus 로고
    • Circular-dichroism and magnetic circular-dichroism of Azotobacter vinelandii ferredoxin I
    • Stephens, P. J. et al. Circular-dichroism and magnetic circular-dichroism of Azotobacter vinelandii ferredoxin I. Biochemistry 30, 3200-3209 (1991).
    • (1991) Biochemistry , vol.30 , pp. 3200-3209
    • Stephens, P.J.1
  • 25
    • 0028670507 scopus 로고
    • Mössbauer and EPR studies of Azotobacter vinelandii ferredoxin I
    • Hu, Z. G., Jollie, D., Burgess, B. K., Stephens, P. J. & Münck, E. Mössbauer and EPR studies of Azotobacter vinelandii ferredoxin I. Biochemistry 33, 14475-14485 (1994).
    • (1994) Biochemistry , vol.33 , pp. 14475-14485
    • Hu, Z.G.1    Jollie, D.2    Burgess, B.K.3    Stephens, P.J.4    Münck, E.5
  • 26
    • 0032493473 scopus 로고    scopus 로고
    • 1H NMR spectroscopy
    • 1H NMR spectroscopy. Biochemistry 37, 9812-9826 (1998).
    • (1998) Biochemistry , vol.37 , pp. 9812-9826
    • Aono, S.1
  • 27
    • 0032509404 scopus 로고    scopus 로고
    • 2+ conversion in vitro but not in vivo
    • 2+ conversion in vitro but not in vivo. J. Chem. Biol. 273, 33692-33701 (1998).
    • (1998) J. Chem. Biol. , vol.273 , pp. 33692-33701
    • Gao-Sheridan1
  • 28
    • 0030475979 scopus 로고    scopus 로고
    • Intrinsic barriers for protons transfer reactions involving electronegative atoms, and the water mediated proton switch: An analysis in terms of Marcus theory
    • Guthrie, J. P. Intrinsic barriers for protons transfer reactions involving electronegative atoms, and the water mediated proton switch: an analysis in terms of Marcus theory. J. Am. Chem. Soc. 118, 12886-12890 (1996).
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 12886-12890
    • Guthrie, J.P.1
  • 29
    • 5344278362 scopus 로고
    • Molecular-dynamics on HIPIP from Chromatium vinosum and comparison with NMR data
    • Banci, L., Bertini, I., Carloni, P., Luchinat, C. & Orioli, P. L. Molecular-dynamics on HIPIP from Chromatium vinosum and comparison with NMR data. J. Am. Chem. Soc. 114, 10683-10689 (1992).
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10683-10689
    • Banci, L.1    Bertini, I.2    Carloni, P.3    Luchinat, C.4    Orioli, P.L.5
  • 30
    • 33845378908 scopus 로고
    • Models for ferredoxins -electronic structures of iron sulfur clusters with one, two and four iron atoms
    • Noodleman, L., Norman, J. G. Jr, Osborne, J. H., Aizman, A. & Case, D. A. Models for ferredoxins -electronic structures of iron sulfur clusters with one, two and four iron atoms. J. Am. Chem. Soc. 107, 3418-3426 (1985).
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 3418-3426
    • Noodleman, L.1    Norman J.G., Jr.2    Osborne, J.H.3    Aizman, A.4    Case, D.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.