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Volumn 131, Issue 20, 2009, Pages 6938-6939

Electrostatic redesign of the [Myoglobin, Cytochrome b 5] interface to create a well-defined docked complex with rapid Lnterprotein electron transfer

Author keywords

[No Author keywords available]

Indexed keywords

BINDING CONFIGURATION; CHARGE REVERSAL; CYTOCHROME B; ELECTRON TRANSFER; ENERGY LANDSCAPE; FERROHEME; STABLE STRUCTURES; SURFACE AREA; TRIPLE MUTANTS; TRIPLET STATE;

EID: 70349142283     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja902131d     Document Type: Article
Times cited : (27)

References (23)
  • 17
    • 70349086428 scopus 로고    scopus 로고
    • Configurations were compared using Suppose, available through the Structural Biology Facility at Vanderbilt University
    • Configurations were compared using Suppose, available through the Structural Biology Facility at Vanderbilt University.
  • 19
    • 70349132559 scopus 로고    scopus 로고
    • note
    • 20 was used as a template for Mb(+6), which was overexpressed in E. coli, purified, and reconstituted with Zn-deuteroporphyrin IX as in refs 10 and 11; complete characterization will be presented elsewhere. Flash photolysis employed LKS.60 (Applied Photophysics) equipped with a Xe-arc and a frequency-doubled Spectra-Physics INDI 40-10-HG Nd:YAG pulsed laser.
  • 23
    • 70349113398 scopus 로고    scopus 로고
    • note
    • Preliminary kinetic measurements in viscous solutions suggest that even this ET rate constant involves conformational gating, and not just the ET process itself.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.