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Volumn 132, Issue 41, 2010, Pages 14590-14595

Outer-sphere effects on reduction potentials of copper sites in proteins: The curious case of high potential type 2 C112D/M121E pseudomonas aeruginosa azurin

Author keywords

[No Author keywords available]

Indexed keywords

COORDINATION SPHERE; COPPER SITES; ELECTRONIC ABSORPTION; HIGH PH; HIGH POTENTIAL; HYDROGEN BONDINGS; METAL PROTEINS; MULTIFREQUENCY ELECTRON PARAMAGNETIC RESONANCE; NEUTRAL PH; PSEUDOMONAS AERUGINOSA; REDOX BEHAVIOR; REDUCTION POTENTIAL; STRUCTURAL CONSTRAINTS; X RAY CRYSTAL STRUCTURES;

EID: 77958072064     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja105731x     Document Type: Article
Times cited : (32)

References (43)
  • 26
    • 77958027873 scopus 로고    scopus 로고
    • EXAFSPAK; Stanford Synchrotron Radiation Lightsource, Stanford Linear Accelerator Center, Stanford University
    • George, G. N. EXAFSPAK; Stanford Synchrotron Radiation Lightsource, Stanford Linear Accelerator Center, Stanford University.
    • George, G.N.1
  • 41
    • 77958054379 scopus 로고    scopus 로고
    • As the pH 9.0 structure represents a point toward the center of the equilibrium, we collected diffraction data at pH 10.0 to confirm the P36/G37 peptide flip. Despite missing electron density and hence poor refinement statistics, we could unequivocally resolve the structural rearrangement in this region (Figure S4, Tables S1-2)
    • As the pH 9.0 structure represents a point toward the center of the equilibrium, we collected diffraction data at pH 10.0 to confirm the P36/G37 peptide flip. Despite missing electron density and hence poor refinement statistics, we could unequivocally resolve the structural rearrangement in this region (Figure S4, Tables S1-2).


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.