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Volumn 121, Issue 23, 1999, Pages 5500-5506

Direct observation of the ferric-porphyrin cation radical as an intermediate in the phototriggered oxidation of ferric- to ferryl-heme tethered to Ru(bpy)3 in reconstituted myoglobin

Author keywords

[No Author keywords available]

Indexed keywords

FERRIC ION; MYOGLOBIN; PORPHYRIN; RADICAL;

EID: 0033575098     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja984199f     Document Type: Article
Times cited : (58)

References (62)
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    • (d) The Enzymes; Sigman, D. S., Ed.; Academic Press: San Diego, 1992; Vol. 20.
    • (1992) The Enzymes , vol.20
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    • For reviews, see: (a) Wasielewski, M. R. Chem. Rev. 1992, 92, 435. (b) Balzani, V.; Credi, A.; Venturi, M. Curr. Opin. Chem. Biol. 1997, 1, 506.
    • (1992) Chem. Rev. , vol.92 , pp. 435
    • Wasielewski, M.R.1
  • 46
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    • note
    • In contrast, for the intermolecular reaction, negative peaks at 208 and 222 nm and a positive peak at 195 nm due to a typical α-helix in the CD spectrum are gradually lessened and lost during photolysis. The results obtained from HPLC showed that, during the photolysis, the peak intensity due to protoheme and the protein skeleton is reduced for the intermolecular system. In SDS - PAGE, the original band due to apo-Mb is smeared, and several bands are observed. These suggest that the Mb structure was considerably damaged in the intermolecular photooxidation process.
  • 47
    • 0344014615 scopus 로고    scopus 로고
    • note
    • A sharp Soret-band is never regenerated by addition of 2-methoxyphenol.
  • 48
    • 0344014614 scopus 로고    scopus 로고
    • note
    • 8c
  • 50
    • 0344014613 scopus 로고    scopus 로고
    • note
    • 1 at pH 9.0 independently.
  • 51
    • 0344445906 scopus 로고    scopus 로고
    • note
    • 1.
  • 52
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    • note
    • 3.
  • 53
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    • note
    • 10 (25) In eqs 3 and 7, it is not clear so far that electron and proton transfers are concerted or stepwise. It is only insisted that this process includes one kinetic rate needed for fitting the present pH dependence.
  • 54
    • 0344877681 scopus 로고    scopus 로고
    • note
    • 2O, we cannot conduct the curve-fitting analysis.
  • 55
    • 0004155427 scopus 로고
    • Freeman: New York
    • a of ε-N of Lys in general is about 10 ± 1. See: Biochemistry, 3rd ed.; Stryer, L., Ed.; Freeman: New York, 1988.
    • (1988) Biochemistry, 3rd Ed.
    • Stryer, L.1
  • 58
    • 0344877680 scopus 로고    scopus 로고
    • note
    • 3-Mb, more physicochemical experiments using various mutant Mbs are required.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.