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Volumn 125, Issue 47, 2003, Pages 14220-14221

Spectroscopy and Reactivity of a Photogenerated Tryptophan Radical in a Structurally Defined Protein Environment

Author keywords

[No Author keywords available]

Indexed keywords

AZURIN; BACTERIAL ENZYME; COPPER; POLYPEPTIDE; RADICAL; TRYPTOPHAN; ZINC;

EID: 0344875237     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja037203i     Document Type: Article
Times cited : (70)

References (35)
  • 7
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    • Miller, J. E. Ph.D. Dissertation, California Institute of Technology, Pasadena, California, 2003.
    • (2003)
    • Miller, J.E.1
  • 8
    • 0031059866 scopus 로고    scopus 로고
    • 3- incorporation, and water placement with XFIT (McRee, D. E. J. Mol. Graphics 1992, 10, 44-46), followed by further anisotropic refinement of all heavy atoms' temperature factors (S, Cu, and Re) with SHELX-97 (Sheldrick, G.; Schneider, T. Methods Enzymol. 1997, 277, 319-343) produced the final model (1. 9 Å resolution, R-factor = 22.4%; R-free = 26.0%; against 5.0% of the free reflections removed from refinement). All residues have favored backbone dihedral angles. Stereochemical restraints were removed from the copper ligand bonds in the later stages of refinement.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 9
    • 0033081529 scopus 로고    scopus 로고
    • 3- incorporation, and water placement with XFIT (McRee, D. E. J. Mol. Graphics 1992, 10, 44-46), followed by further anisotropic refinement of all heavy atoms' temperature factors (S, Cu, and Re) with SHELX-97 (Sheldrick, G.; Schneider, T. Methods Enzymol. 1997, 277, 319-343) produced the final model (1. 9 Å resolution, R-factor = 22.4%; R-free = 26.0%; against 5.0% of the free reflections removed from refinement). All residues have favored backbone dihedral angles. Stereochemical restraints were removed from the copper ligand bonds in the later stages of refinement.
    • (1999) Acta Crystallogr. , vol.D55 , pp. 484-491
    • Kissinger, C.R.1    Gehlhaar, D.K.2    Fogel, D.B.3
  • 11
    • 0002705842 scopus 로고
    • 3- incorporation, and water placement with XFIT (McRee, D. E. J. Mol. Graphics 1992, 10, 44-46), followed by further anisotropic refinement of all heavy atoms' temperature factors (S, Cu, and Re) with SHELX-97 (Sheldrick, G.; Schneider, T. Methods Enzymol. 1997, 277, 319-343) produced the final model (1. 9 Å resolution, R-factor = 22.4%; R-free = 26.0%; against 5.0% of the free reflections removed from refinement). All residues have favored backbone dihedral angles. Stereochemical restraints were removed from the copper ligand bonds in the later stages of refinement.
    • (1992) J. Mol. Graphics , vol.10 , pp. 44-46
    • McRee, D.E.1
  • 12
    • 0030880598 scopus 로고    scopus 로고
    • 3- incorporation, and water placement with XFIT (McRee, D. E. J. Mol. Graphics 1992, 10, 44-46), followed by further anisotropic refinement of all heavy atoms' temperature factors (S, Cu, and Re) with SHELX-97 (Sheldrick, G.; Schneider, T. Methods Enzymol. 1997, 277, 319-343) produced the final model (1. 9 Å resolution, R-factor = 22.4%; R-free = 26.0%; against 5.0% of the free reflections removed from refinement). All residues have favored backbone dihedral angles. Stereochemical restraints were removed from the copper ligand bonds in the later stages of refinement.
    • (1997) Methods Enzymol. , vol.277 , pp. 319-343
    • Sheldrick, G.1    Schneider, T.2
  • 21
    • 4243553426 scopus 로고
    • x (protonated 2.00345; hydrogen-bonded 2.00359; deprotonated 2.00380).
    • (1988) Phys. Rev. A , vol.38 , pp. 3098-3100
    • Becke, A.D.1
  • 31
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    • Jovanovich S. V.; Harriman, A.; Simic, M. G. J. Phys. Chem. 1986, 90, 1935-1939. Harriman, A. J. Phys. Chem. 1987, 91, 6102-6104.
    • (1987) J. Phys. Chem. , vol.91 , pp. 6102-6104
    • Harriman, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.