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Volumn 50, Issue 4, 2011, Pages 1242-1249

Alkylamine-ligated H93G myoglobin cavity mutant: A model system for endogenous lysine and terminal amine ligation in heme proteins such as nitrite reductase and cytochrome f

Author keywords

[No Author keywords available]

Indexed keywords

AMINE; CYTOCHROME F; GLYCINE; HISTIDINE; LIGAND; LYSINE; MYOGLOBIN; NITRITE REDUCTASE;

EID: 79951619428     PISSN: 00201669     EISSN: None     Source Type: Journal    
DOI: 10.1021/ic101644u     Document Type: Article
Times cited : (16)

References (45)
  • 1
    • 0024294403 scopus 로고
    • Dawson, J. H. Science 1988, 240, 433-439
    • (1988) Science , vol.240 , pp. 433-439
    • Dawson, J.H.1
  • 34
    • 79951588917 scopus 로고    scopus 로고
    • The assumption that the added amine ligand binds in the proximal pocket is based on the crystal structures of ferric H93G Mb with Im, (26) thiolate, (35) or acetate (35) bound adducts. In addition, the distal pocket is more polar than the proximal cavity and thus is the more likely location for water to bind, as seen in the Im and acetate complexes. (26, 35)
    • The assumption that the added amine ligand binds in the proximal pocket is based on the crystal structures of ferric H93G Mb with Im, (26) thiolate, (35) or acetate (35) bound adducts. In addition, the distal pocket is more polar than the proximal cavity and thus is the more likely location for water to bind, as seen in the Im and acetate complexes. (26, 35)


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.