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Volumn 342, Issue 6160, 2013, Pages 825-829

Iron(IV)hydroxide pKa and the role of thiolate ligation in C-H bond activation by cytochrome P450

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME P450; FERRIC HYDROXIDE; HISTIDINE; HYDROCARBON; PHENYLALANINE; THIOL DERIVATIVE; TRYPTOPHAN; TYROSINE;

EID: 84887761225     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1244373     Document Type: Article
Times cited : (275)

References (60)
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    • note
    • ○' ∼ 0.9 V. The difference in these potentials is equivalent to ∼13 kcal/mol.
  • 9
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    • note
    • In the absence of substrate, P450-I decays predominantly through the oxidation of tyrosine residues (10, 11). The oxidation of tryptophan is energetically feasible, but tyrosine with its (generally) lower potential is the preferred target. Tryptophan radicals have been observed after P450-I decay, but these species constituted only a minor component of the decay product (10). The treatment of tyrosine oxidation presented here is an archetype for nonproductive one-electron processes. It may be applied equally well to tryptophan oxidation.
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    • Y. Kang et al., Chemistry 15, 10039-10046 (2009).
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    • note
    • Dawson and co-workers (39) have shown that exogenous thiol ligands bound trans to the proximal thiolate of P450 have enhanced basicity relative to analogous myoglobin adducts.
  • 49
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    • Revision C.01 Gaussian Inc., Wallingford, CT
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.