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Volumn 330, Issue 6006, 2010, Pages 933-937

Cytochrome P450 compound I: Capture, characterization, and C-H bond activation kinetics

Author keywords

[No Author keywords available]

Indexed keywords

3 CHLOROPERBENZOIC ACID; CARBON; CHLORIDE PEROXIDASE; CYTOCHROME P450; CYTOCHROME P450 119; CYTOCHROME P450 119 I; CYTOCHROME P450 I; HYDROGEN; LAURIC ACID; OXIDOREDUCTASE; UNCLASSIFIED DRUG;

EID: 78149373621     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1193478     Document Type: Article
Times cited : (1098)

References (47)
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    • K. D. Karlin, Nature 463, 168 (2010).
    • Nature , vol.463 , Issue.168 , pp. 2010
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    • (1992) FEBS Lett. , vol.305 , pp. 206
    • Egawa, T.1
  • 32
    • 78149378554 scopus 로고    scopus 로고
    • note
    • -1. This is at least 2000 times slower than CYP119-I. No spectroscopic characterizations of the LFP-generated species other than UV/visible have been reported. We have recently suggested that the LFP-generated intermediate is not compound I (41).
  • 40
    • 2142803437 scopus 로고    scopus 로고
    • Materials and methods are available as supporting material on
    • Materials and methods are available as supporting material on Science Online.
    • Science Online
  • 42
    • 78149386411 scopus 로고    scopus 로고
    • note
    • Although it is clear from our fitting - as well as the spectra displayed in Fig. 4 - that |J|/D in CYP119-I has increased substantially relative to its value in CPO-I, the magnitude of the increase is not definite. The actual value of J/D depends critically on the choice of ferryl g values, for which only estimates are available. In our analysis, we have obtained ferryl g values by fitting CPO-I under the assumption that |J|/D = 1.02, as originally reported by Rutter et al. (23). This procedure provided the ferryl g values listed for CPO-I in Table 1, which were then used as input for the fitting of CYP119-I. The ferryl g values obtained for both species are reasonably similar to the CPO-I values (g⊥= 2.28 and g|| = 1.94) used by Rutter et al., whomodeled but did not fit their CPO-I data. Our ferryl g values result in a 27% increase in |J|/D relative to CPO, whereas the values of Rutter et al. result in an increase of 24%. Recently, it was suggested that g? = 2.0 may be more appropriate for the ferrylmoiety (27). If this report is accurate, it would suggest that the ratio of |J|/D in CYP119-I is almost twice as large as the value observed for CPO-I.
  • 46
    • 79952746514 scopus 로고    scopus 로고
    • R. K. Allemann, N. S. Scrutton, Eds. The Royal Society of Chemistry, Cambridge
    • J. P. Klinman, in Quantum Tunnelling in Enzyme-Catalysed Reactions, R. K. Allemann, N. S. Scrutton, Eds. (The Royal Society of Chemistry, Cambridge, 2009), pp. 132-157.
    • (2009) Quantum Tunnelling in Enzyme-Catalysed Reactions , pp. 132-157
    • Klinman, J.P.1
  • 47
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    • note
    • This work was supported by NSF. We thank T. Grove and J. C. Calixto Moreno for assistance with GC-MS and C. Krest for help with preliminary EPR experiments. The CYP119 plasmid was graciously provided by P. R. Ortiz de Montellano.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.