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Volumn 121, Issue 46, 1999, Pages 10781-10787

Intramolecular electron transfer from Mn or ligand phenolate to photochemically generated Ru(III) in multinuclear Ru/Mn complexes. Laser flash photolysis and EPR studies on photosystem II models

Author keywords

[No Author keywords available]

Indexed keywords

LIGAND; MANGANESE; PHENOL DERIVATIVE; RUTHENIUM COMPLEX;

EID: 0033601064     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja991402d     Document Type: Article
Times cited : (74)

References (89)
  • 16
  • 22
    • 0032023777 scopus 로고    scopus 로고
    • For an excellent recent review on radicals in enzymatic systems, see: Stubbe, J. A.; van der Donk, W. A. Chem. Rev. 1998, 98, 705.
    • (1998) Chem. Rev. , vol.98 , pp. 705
    • Stubbe, J.A.1    Van Der Donk, W.A.2
  • 42
    • 13044258223 scopus 로고    scopus 로고
    • In all cases, the hexafluorophosphate salts were used
    • In all cases, the hexafluorophosphate salts were used.
  • 57
    • 13044275453 scopus 로고    scopus 로고
    • note
    • .- is ca. 0.4 V (see ref 32).
  • 61
    • 13044293180 scopus 로고    scopus 로고
    • Ph.D. Dissertation, Ruhr-Universität, Bochum, Germany
    • Sokolowski, A. Ph.D. Dissertation, Ruhr-Universität, Bochum, Germany, 1996.
    • (1996)
    • Sokolowski, A.1
  • 62
    • 13044285228 scopus 로고    scopus 로고
    • Ph.D. Dissertation, Ruhr-Universität, Bochum, Germany
    • III, see: Burdinski, D. Ph.D. Dissertation, Ruhr-Universität, Bochum, Germany, 1998.
    • (1998)
    • Burdinski, D.1
  • 64
    • 0032508393 scopus 로고    scopus 로고
    • In the WOC, upon oxidation of Yz, the phenolic proton is transferred to an adjacent histidine via a preexisting intramolecular H-bond (see: Hays, A.-M. A.; et al. Biochemistry 1998, 37, 11352. Diner, B. A.; et al. Biochemistry 1998, 37, 17931. Mamedov, F.; et al. Biochemistry 1998, 37, 14245. O'Malley, P. J. J. Am. Chem. Soc. 1998, 120, 11732).
    • (1998) , vol.37 , pp. 11352
    • Hays, A.-M.A.1    Biochemistry, E.A.2
  • 65
    • 0032559015 scopus 로고    scopus 로고
    • In the WOC, upon oxidation of Yz, the phenolic proton is transferred to an adjacent histidine via a preexisting intramolecular H-bond (see: Hays, A.-M. A.; et al. Biochemistry 1998, 37, 11352. Diner, B. A.; et al. Biochemistry 1998, 37, 17931. Mamedov, F.; et al. Biochemistry 1998, 37, 14245. O'Malley, P. J. J. Am. Chem. Soc. 1998, 120, 11732).
    • (1998) Biochemistry , vol.37 , pp. 17931
    • Diner, B.A.1
  • 66
    • 0032491189 scopus 로고    scopus 로고
    • In the WOC, upon oxidation of Yz, the phenolic proton is transferred to an adjacent histidine via a preexisting intramolecular H-bond (see: Hays, A.-M. A.; et al. Biochemistry 1998, 37, 11352. Diner, B. A.; et al. Biochemistry 1998, 37, 17931. Mamedov, F.; et al. Biochemistry 1998, 37, 14245. O'Malley, P. J. J. Am. Chem. Soc. 1998, 120, 11732).
    • (1998) Biochemistry , vol.37 , pp. 14245
    • Mamedov, F.1
  • 67
    • 0032545002 scopus 로고    scopus 로고
    • In the WOC, upon oxidation of Yz, the phenolic proton is transferred to an adjacent histidine via a preexisting intramolecular H-bond (see: Hays, A.-M. A.; et al. Biochemistry 1998, 37, 11352. Diner, B. A.; et al. Biochemistry 1998, 37, 17931. Mamedov, F.; et al. Biochemistry 1998, 37, 14245. O'Malley, P. J. J. Am. Chem. Soc. 1998, 120, 11732).
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 11732
    • O'Malley, P.J.1
  • 73
    • 13044283974 scopus 로고    scopus 로고
    • note
    • The smaller ring splittings seen for the "simple" phenoxyls are buried in the large line-width characteristic of the "complex" (= intermediate molecular weight) phenoxyls. As is evident from Table 1, the methoxy substituent decreases the spin density such that the splittings at the ortho and para positions are decreased.
  • 77
    • 13044282252 scopus 로고    scopus 로고
    • note
    • +/Fc couple in acetonitrile, unless specified otherwise.
  • 78
    • 13044268867 scopus 로고    scopus 로고
    • note
    • Note the long lifetime of the MLCT state in the model compound 1.
  • 79
    • 0032321583 scopus 로고    scopus 로고
    • Quenching by energy transfer (Hammarström, L.; et al. Biochim. Biophys. Acta 1998, 1365, 193) can be excluded on the basis of the observations described below.
    • (1998) Biochim. Biophys. Acta , vol.1365 , pp. 193
    • Hammarström, L.1
  • 84
    • 13044260739 scopus 로고    scopus 로고
    • note
    • 2+. However, we are planning to measure the rate of eq 8b or 11 directly using a time resolution better than the presently available 20 ns.
  • 85
    • 13044273412 scopus 로고    scopus 로고
    • note
    • As in the case of 8, there seem to be two kinetic components in these processes; see inset to Figure 8.
  • 86
    • 13044255594 scopus 로고    scopus 로고
    • Ph.D. Dissertation, Ruhr-Universität, Bochum, Germany
    • See: Burdinski, D. Ph.D. Dissertation, Ruhr-Universität, Bochum, Germany, 1998.
    • (1998)
    • Burdinski, D.1
  • 87
    • 13044278126 scopus 로고    scopus 로고
    • note
    • The influence of electron density can be seen from the much shorter half-life of the Mn(IV)-coordinated radical as compared to that of the "free" one.
  • 88
    • 13044278127 scopus 로고    scopus 로고
    • As concluded from crystal data on similar compounds; see ref 38
    • As concluded from crystal data on similar compounds; see ref 38.
  • 89
    • 13044263676 scopus 로고    scopus 로고
    • note
    • . in the WOC.


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