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Volumn 122, Issue 3, 2000, Pages 536-537

Theoretical studies on N(g)-hydroxy-L-arginine and derived radicals: Implications for the mechanism of nitric oxide synthase

Author keywords

[No Author keywords available]

Indexed keywords

N(G) HYDROXYARGININE; NITRIC OXIDE SYNTHASE; RADICAL;

EID: 0034716344     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja991876c     Document Type: Article
Times cited : (36)

References (38)
  • 22
    • 0011083273 scopus 로고    scopus 로고
    • Reported energies include zero-point energy corrections scaled by 0.9806 as suggested in: Scott, A. P.; Radom, L. J. Phys. Chem. 1996, 100, 16502-16513.
    • (1996) J. Phys. Chem. , vol.100 , pp. 16502-16513
    • Scott, A.P.1    Radom, L.2
  • 23
    • 0342739195 scopus 로고    scopus 로고
    • personal communication. See also ref 23
    • The active site residues available to bind NOHA are conserved amongst the three isoforms of NOS. Raman, C. S.; Poulos, T., personal communication. See also ref 23.
    • Raman, C.S.1    Poulos, T.2
  • 29
    • 0342304117 scopus 로고    scopus 로고
    • note
    • Reference 23 notes that arginine and various inhibitors of NOS all bind to the conserved active site carboxylate in a bidentate fashion, while NOHA bound to eNOS appears to interact with this carboxylate in a monodentate fashion. Further experiments are necessary, however, to clarify the details of NOHA binding by the various isoforms of NOS.
  • 33
    • 0343609161 scopus 로고    scopus 로고
    • note
    • 2) values for all radical species described are between 0.75 and 0.78.
  • 34
    • 0342304114 scopus 로고    scopus 로고
    • note
    • Both 10 and 11 are π-radicals.
  • 35
    • 0343609160 scopus 로고    scopus 로고
    • note
    • 32b-d with ∈ = 78.5) has a negligible effect on this energy difference.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.