메뉴 건너뛰기




Volumn 127, Issue 15, 2005, Pages 5449-5462

Spectroscopic and computational studies of Ni superoxide dismutase: Electronic structure contributions to enzymatic function

Author keywords

[No Author keywords available]

Indexed keywords

CHARGE TRANSFER; CHEMICAL BONDS; COMPUTATIONAL METHODS; ELECTRONIC STRUCTURE; LIGHT ABSORPTION; NICKEL; RAMAN SCATTERING; SPECTROSCOPIC ANALYSIS; ULTRAVIOLET RADIATION;

EID: 17644414093     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja042521i     Document Type: Article
Times cited : (113)

References (97)
  • 3
    • 0026587335 scopus 로고
    • (c) Wallace, D. C. Science 1992, 256, 628-632.
    • (1992) Science , vol.256 , pp. 628-632
    • Wallace, D.C.1
  • 5
    • 0001329545 scopus 로고
    • Valentine, J. S., Foote, C. S., Greenberg, A., Liebman, J. F., Eds.; Blackie Academic and Professional: New York
    • (e) Halliwell, B. In Active Oxygen in Biochemistry; Valentine, J. S., Foote, C. S., Greenberg, A., Liebman, J. F., Eds.; Blackie Academic and Professional: New York, 1995; pp 313-335.
    • (1995) Active Oxygen in Biochemistry , pp. 313-335
    • Halliwell, B.1
  • 31
    • 17644405533 scopus 로고    scopus 로고
    • Unpublished results
    • Ahlrichs, R. Unpublished results.
    • Ahlrichs, R.1
  • 34
    • 0000189651 scopus 로고
    • Becke, A. D. J. Chem. Phys. 1993, 98, 5648-5652. Becke, A. D. J. Chem. Phys. 1993, 98, 1372-1377.
    • (1993) J. Chem. Phys. , vol.98 , pp. 5648-5652
    • Becke, A.D.1
  • 35
    • 34250817103 scopus 로고
    • Becke, A. D. J. Chem. Phys. 1993, 98, 5648-5652. Becke, A. D. J. Chem. Phys. 1993, 98, 1372-1377.
    • (1993) J. Chem. Phys. , vol.98 , pp. 1372-1377
    • Becke, A.D.1
  • 39
  • 41
    • 0035936304 scopus 로고    scopus 로고
    • (c) Neese, F. J. Chem. Phys. 2001, 115, 11080-11096.
    • (2001) J. Chem. Phys. , vol.115 , pp. 11080-11096
    • Neese, F.1
  • 46
    • 17644362747 scopus 로고    scopus 로고
    • note
    • red is displayed in Figure 1.
  • 77
    • 17644370727 scopus 로고    scopus 로고
    • note
    • ax by nearly an order or magnitude.
  • 78
    • 17644411736 scopus 로고    scopus 로고
    • note
    • -1. The value reported herein for this model reflects the average of these two energies.
  • 82
    • 17644420420 scopus 로고    scopus 로고
    • note
    • 2 can access the thiolate ligands in nitrile hydratase, this may not be the case in NiSOD.
  • 84
    • 17644368618 scopus 로고    scopus 로고
    • note
    • 2)-based MO is the same in the oxidized and reduced enzyme. Although not strictly true, this assumption seems reasonable, since the equatorial metal-ligand bonding interactions experience little change upon oxidation/reduction.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.