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Volumn 120, Issue 30, 1998, Pages 7551-7556

Electron transfer in ruthenium-modified plastocyanin

Author keywords

[No Author keywords available]

Indexed keywords

PLASTOCYANIN;

EID: 0032486780     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja972625b     Document Type: Article
Times cited : (70)

References (56)
  • 1
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    • Haehnel, W. In Encyclopedia of Plant Physiology; Springer: Berlin, 1986; Vol. 4, pp 547-559. Sykes, A. G. Structure Bonding 1990, 75, 175-224. Redinbo, M. R.; Yeates, T. O.; Merchant S. J. Bioenerg. Biomembr. 1994, 26, 49-66.
    • (1986) Encyclopedia of Plant Physiology , vol.4 , pp. 547-559
    • Haehnel, W.1
  • 2
    • 0000211392 scopus 로고
    • Haehnel, W. In Encyclopedia of Plant Physiology; Springer: Berlin, 1986; Vol. 4, pp 547-559. Sykes, A. G. Structure Bonding 1990, 75, 175-224. Redinbo, M. R.; Yeates, T. O.; Merchant S. J. Bioenerg. Biomembr. 1994, 26, 49-66.
    • (1990) Structure Bonding , vol.75 , pp. 175-224
    • Sykes, A.G.1
  • 3
    • 0028207017 scopus 로고
    • Haehnel, W. In Encyclopedia of Plant Physiology; Springer: Berlin, 1986; Vol. 4, pp 547-559. Sykes, A. G. Structure Bonding 1990, 75, 175-224. Redinbo, M. R.; Yeates, T. O.; Merchant S. J. Bioenerg. Biomembr. 1994, 26, 49-66.
    • (1994) J. Bioenerg. Biomembr. , vol.26 , pp. 49-66
    • Redinbo, M.R.1    Yeates, T.O.2    Merchant, S.3
  • 4
    • 3543026994 scopus 로고    scopus 로고
    • note
    • 4-2,2′-bipyridine; im, imidazole; MLCT. metal-to-ligand charge transfer; LMCT, ligand-to-metal charge transfer; NHE, normal hydrogen electrode; FPLC, fast protein liquid chromatography; HPLC, high-pressure liquid chromatography; MALDI-TOF, matrix-assisted-laser-desorption/ionization time-of-flight mass spectrometry.
  • 27
    • 0004155427 scopus 로고
    • W. H. Freeman: New York
    • Stryer, L. Biochemistry, 4th ed.; W. H. Freeman: New York, 1995; pp 665-666.
    • (1995) Biochemistry, 4th Ed. , pp. 665-666
    • Stryer, L.1
  • 34
    • 0001457165 scopus 로고    scopus 로고
    • 2+ [Sigfridsson, K.; Sundhal, M.; Bjerrum, M. J.; Hansson, Ö. JBIC, J. Biol. Inorg. Chem. 1996, 1, 405-414. Sigfridsson, K.; Ejdebäck, M.; Sundahl, M.; Hansson, Ö. Arch. Biochem. Biophys. 1998, 351, 197-206]. Also note that Ru(trpy)(bpy)-modified cyt c has been reported [Isied, S. S. In Metal in Biological Systems; Sigel, H., Sigel, A., Eds.; Dekker: New York, 1991; Vol. 27, pp 1-56].
    • (1996) JBIC, J. Biol. Inorg. Chem. , vol.1 , pp. 405-414
    • Sigfridsson, K.1    Sundhal, M.2    Bjerrum, M.J.3    Hansson, Ö.4
  • 35
    • 0032520654 scopus 로고    scopus 로고
    • 2+ [Sigfridsson, K.; Sundhal, M.; Bjerrum, M. J.; Hansson, Ö. JBIC, J. Biol. Inorg. Chem. 1996, 1, 405-414. Sigfridsson, K.; Ejdebäck, M.; Sundahl, M.; Hansson, Ö. Arch. Biochem. Biophys. 1998, 351, 197-206]. Also note that Ru(trpy)(bpy)-modified cyt c has been reported [Isied, S. S. In Metal in Biological Systems; Sigel, H., Sigel, A., Eds.; Dekker: New York, 1991; Vol. 27, pp 1-56].
    • (1998) Arch. Biochem. Biophys. , vol.351 , pp. 197-206
    • Sigfridsson, K.1    Ejdebäck, M.2    Sundahl, M.3    Hansson, Ö.4
  • 36
    • 0142133806 scopus 로고
    • Sigel, H., Sigel, A., Eds.; Dekker: New York
    • 2+ [Sigfridsson, K.; Sundhal, M.; Bjerrum, M. J.; Hansson, Ö. JBIC, J. Biol. Inorg. Chem. 1996, 1, 405-414. Sigfridsson, K.; Ejdebäck, M.; Sundahl, M.; Hansson, Ö. Arch. Biochem. Biophys. 1998, 351, 197-206]. Also note that Ru(trpy)(bpy)-modified cyt c has been reported [Isied, S. S. In Metal in Biological Systems; Sigel, H., Sigel, A., Eds.; Dekker: New York, 1991; Vol. 27, pp 1-56].
    • (1991) Metal in Biological Systems , vol.27 , pp. 1-56
    • Isied, S.S.1
  • 38
    • 3542993986 scopus 로고    scopus 로고
    • note
    • 2O)(His59)Pc is readily made, and partially im-ligated fractions also can be prepared.
  • 39
    • 3543040170 scopus 로고    scopus 로고
    • note
    • 2+ (L = bpy, tmbpy) display broad band emission spectra in aqueous solution, with λ ∼ 650 nm; the luminescence decay lifetimes are 20 and 54 ns, respectively.
  • 43
    • 3543047492 scopus 로고    scopus 로고
    • note
    • +.
  • 44
    • 3542998834 scopus 로고    scopus 로고
    • note
    • 3+/2+ reduction potential. The rates we have measured for the slow phase are insensitive to the complexes used, although we did not examine a large driving-force range. Thus the results do not allow us conclusively to rule out an oxidation/rearrangement mechanism.
  • 46
    • 3543023448 scopus 로고    scopus 로고
    • 27
    • 27
  • 53
    • 0000844197 scopus 로고
    • 2+) with different affinities depending on the number and particular microenvironment of the histidine residue(s) [Hemdan, E. S.; Zhao, Y.-J.; Sulkowski, E.; Porath, J. Proc. Natl. Acad. Sci. U.S.A. 1989, 86, 1811-1815]; this ability is lost when, for instance, the histidine is derivatized with a metal complex. In general, metal complexes will not react specifically with histidine residues; however, the technique provides a fast and inexpensive way to ascertain whether a protein has actually been modified at a histidine. In addition to providing a convenient purification method, IMAC can be employed to probe the accessibility of surface histidines.
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 1811-1815
    • Hemdan, E.S.1    Zhao, Y.-J.2    Sulkowski, E.3    Porath, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.