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Volumn 74, Issue 21, 2009, Pages 8212-8218

Synthesis of a cyclic pentapeptide mimic of the active site His-Tyr cofactor of cytochrome c oxidase

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ARYLBORONIC ACIDS; CHEMICAL EQUATIONS; COFACTORS; CYTOCHROME C OXIDASE; DYNAMIC CHARACTER; N-ARYLATIONS; REGIO-SELECTIVE; SIDE CHAINS;

EID: 70350719281     PISSN: 00223263     EISSN: None     Source Type: Journal    
DOI: 10.1021/jo901744y     Document Type: Article
Times cited : (15)

References (47)
  • 20
    • 70350705130 scopus 로고    scopus 로고
    • Masters Thesis, University of California Santa Cruz
    • Moore, E. M., Masters Thesis, University of California Santa Cruz, 2000.
    • (2000)
    • Moore, E.M.1
  • 32
    • 70350707041 scopus 로고    scopus 로고
    • Ph.D. Thesis, University of California Santa Cruz
    • Gerstenberger, B. S., Ph.D. Thesis, University of California Santa Cruz , 2007
    • (2007)
    • Gerstenberger, B.S.1
  • 36
    • 70350711582 scopus 로고    scopus 로고
    • Increasing the arylboronic acid to histidine ratio to 1.4:1 does not improve the yield
    • Increasing the arylboronic acid to histidine ratio to 1.4:1 does not improve the yield.
  • 42
    • 5644298630 scopus 로고    scopus 로고
    • While this 10% impurity of free phenol was removed to obtain a pure sample of 23, its presence posed no problems for the production of 24
    • Nicolaou, K. C.; Chen, D. Y.-K.; Huang, X.; Ling, T.; Bella, M.; Snyder, S. A. J. Am. Chem. Soc. 2004, 126, 12888-12896. While this 10% impurity of free phenol was removed to obtain a pure sample of 23, its presence posed no problems for the production of 24.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 12888-12896
    • Nicolaou, K.C.1    Chen, D.Y.-K.2    Huang, X.3    Ling, T.4    Bella, M.5    Snyder, S.A.6
  • 44
    • 70350718615 scopus 로고    scopus 로고
    • Solvent and water molecules omitted for clarity
    • Solvent and water molecules omitted for clarity.
  • 45
    • 29844456385 scopus 로고    scopus 로고
    • DFTcalculations on simplemodel systems put the BDA at 42.5°, very close to the native enzyme BDA. Most X-ray structures, including our own previous work, suffer from intermolecular hydrogen bonds that likely perturb the fundamental BDA; in our laboratory we have documented BDAs ranging from -25.7° to -36.3°. By contrast, the structure of 24 appears devoid of serious intermolecular interactions. Hence, this molecule affords the best experimental evidence for the intrinsic BDA of the biaryl cofactor
    • DFTcalculations on simplemodel systems ( Pratt, D.A.; Pesavento, R. P.; van der Donk, W. A. Org. Lett. 2005, 7, 2735-2738.) put the BDA at 42.5°, very close to the native enzyme BDA. Most X-ray structures, including our own previous work, suffer from intermolecular hydrogen bonds that likely perturb the fundamental BDA; in our laboratory we have documented BDAs ranging from -25.7° to -36.3°. By contrast, the structure of 24 appears devoid of serious intermolecular interactions. Hence, this molecule affords the best experimental evidence for the intrinsic BDA of the biaryl cofactor.
    • (2005) Org. Lett. , vol.7 , pp. 2735-2738
    • Pratt, D.A.1    Pesavento, R.P.2    Van Der Donk, W.A.3
  • 46
    • 70350715727 scopus 로고    scopus 로고
    • Macromodel v9.0.014 was used for the calculations. The Amber* force field was employed, dielectric = 80, with a PRCG minimization method
    • Macromodel v9.0.014 was used for the calculations. The Amber* force field was employed, dielectric = 80, with a PRCG minimization method.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.