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Volumn 20, Issue 6, 2014, Pages 1602-1614

New insights into the nature of observable reaction intermediates in cytochrome P450 NO reductase by using a combination of spectroscopy and quantum mechanics/molecular mechanics calculations

Author keywords

enzymes; metalloenzymes; qm mm calculations; spectroscopy; theoretical spectroscopy

Indexed keywords

CYTOCHROME P450; ENZYME; NITRIC OXIDE; NITRIC OXIDE REDUCTASE (P450); NITRIC-OXIDE REDUCTASE (P450);

EID: 84895060545     PISSN: 09476539     EISSN: 15213765     Source Type: Journal    
DOI: 10.1002/chem.201302443     Document Type: Article
Times cited : (25)

References (80)
  • 73
    • 77956632873 scopus 로고    scopus 로고
    • It was recently shown that B3LYP-D (B3LYP* with dispersion correction) gives much better Heme-NO binding energies than B3LYP-D. (,). In the companion paper to this work (ref. [13]), an even larger set of density functionals was used for the calculation of heme-NO binding energies and the same conclusion was reached
    • It was recently shown that B3LYP-D (B3LYP* with dispersion correction) gives much better Heme-NO binding energies than B3LYP-D. (, P. E. M. Siegbahn, M. R. A. Blomberg, S.-L. Chen, J. Chem. Theory Comput. 2010, 6, 2040.). In the companion paper to this work (ref. [13]), an even larger set of density functionals was used for the calculation of heme-NO binding energies and the same conclusion was reached.
    • (2010) J. Chem. Theory Comput. , vol.6 , pp. 2040
    • Siegbahn, P.E.M.1    Blomberg, M.R.A.2    Chen, S.-L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.