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Volumn 113, Issue 13, 2009, Pages 4492-4499

Low-frequency heme, iron-ligand, and ligand modes of imidazole and imidazolate complexes of iron protoporphyrin and microperoxidase in aqueous solution. an analysis by far-infrared difference spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

BIOPOLYMERS; DEFORMATION; DEUTERIUM; ELECTRIC BATTERIES; ELECTROLYTIC CELLS; ELECTRONIC PROPERTIES; FOURIER TRANSFORM INFRARED SPECTROSCOPY; HEMOGLOBIN; IRON COMPOUNDS; METAL ANALYSIS; POLYMERS; PORPHYRINS; SOLUTIONS; SPIN DYNAMICS;

EID: 65249103480     PISSN: 15206106     EISSN: None     Source Type: Journal    
DOI: 10.1021/jp810774g     Document Type: Article
Times cited : (15)

References (77)
  • 1
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    • Spiro, T. G. The Resonance Raman Spectroscopy of Metalloporphyrins and Heme Proteins. Iron Porphyrins. E. In Physical Bioinorganic Chemistry Series, part 2; Lever, A. B. P., Gray, H. B., Eds.; Wiley VCH: New York, 1982; p 89.
    • Spiro, T. G. The Resonance Raman Spectroscopy of Metalloporphyrins and Heme Proteins. Iron Porphyrins. E. In Physical Bioinorganic Chemistry Series, part 2; Lever, A. B. P., Gray, H. B., Eds.; Wiley VCH: New York, 1982; p 89.
  • 2
    • 0002153672 scopus 로고
    • Infrared and Raman spectra of metalloporphyrins
    • Buchler, I. J. W, Ed, Springer Berlin: Heidelberg
    • Kitagawa, T.; Osaki Y. Infrared and Raman spectra of metalloporphyrins. In Structure and bonding: Metal Complexes with Tetrapyrrole Ligands; Buchler, I. J. W., Ed.; Springer Berlin: Heidelberg, 1987; Vol. 64, p 71.
    • (1987) Structure and bonding: Metal Complexes with Tetrapyrrole Ligands , vol.64 , pp. 71
    • Kitagawa, T.1    Osaki, Y.2
  • 13
    • 0001769551 scopus 로고    scopus 로고
    • The hemepeptides from cytochrome c: Preparation, physical and chemical properties, and their use as model compounds for the hemoproteins
    • Scott, R. A, Mauk, A. G, Eds, University Science Books: Sausalito, CA, and references therein
    • Adams, P. A. Baldwin, D. A., et al. The hemepeptides from cytochrome c: preparation, physical and chemical properties, and their use as model compounds for the hemoproteins. In Cytochrome c: a Multidisciplinary Approach; Scott, R. A., Mauk, A. G., Eds.; University Science Books: Sausalito, CA, 1996; pp 636-692 and references therein.
    • (1996) Cytochrome c: A Multidisciplinary Approach , pp. 636-692
    • Adams, P.A.1    Baldwin, D.A.2
  • 55
    • 84906375148 scopus 로고    scopus 로고
    • The pK a values of the imidazole ligands bound to FePP was found to be 9.0 and 10.8 for the Fe3+ species and 13.0 and 14.1 for the Fe2+ form; the ionization properties of the heme bound 4MeImH ligand are most likely very similar to those of ImH.32,55.
    • The pK a values of the imidazole ligands bound to FePP was found to be 9.0 and 10.8 for the Fe3+ species and 13.0 and 14.1 for the Fe2+ form; the ionization properties of the heme bound 4MeImH ligand are most likely very similar to those of ImH.32,55.
  • 57
    • 84906406286 scopus 로고    scopus 로고
    • The reduction of the 5c MP8 species was direct when a gold electrode coated with PATS-3 was used
    • The reduction of the 5c MP8 species was direct when a gold electrode coated with PATS-3 was used. Re-oxidation was accelerated using TMPD as a redox mediator.
    • Re-oxidation was accelerated using TMPD as a redox mediator
  • 62
    • 84906389303 scopus 로고    scopus 로고
    • The sample transmission is very low in this region, which is the transmission limit of the detector, and water absorbs strongly. While it is possible to detect absorption bands in concentrated samples, the noise level is too high in the FTIR difference spectra
    • The sample transmission is very low in this region, which is the transmission limit of the detector, and water absorbs strongly. While it is possible to detect absorption bands in concentrated samples, the noise level is too high in the FTIR difference spectra.
  • 67
    • 84906360872 scopus 로고    scopus 로고
    • An assignment corresponding to a major ν (Fe-N4(Pyr, stretching in the normal mode can be excluded. The frequencies of the 412(+)/394- 398(, cm-1 bands do not match with the lengths of the Fe-N(pyrrole) bonds that are longer in planar ferrohemes than in ruffled ferrihemes. The frequency of a ν (Fe-N4Pyr, mode would be higher for the ferric species than for the ferrous species. We propose a folding or tilting mode of the pyrroles, but we cannot exclude a minor contribution of the Fe-N coordinates
    • An assignment corresponding to a major ν (Fe-N4(Pyr)) stretching in the normal mode can be excluded. The frequencies of the 412(+)/394- 398(-) cm-1 bands do not match with the lengths of the Fe-N(pyrrole) bonds that are longer in planar ferrohemes than in ruffled ferrihemes. The frequency of a ν (Fe-N4(Pyr)) mode would be higher for the ferric species than for the ferrous species. We propose a folding or tilting mode of the pyrroles, but we cannot exclude a minor contribution of the Fe-N coordinates.
  • 72
    • 84906391703 scopus 로고
    • Schnek, A. G, Paul, C, Eds, Editions de l 'Université de Bruxelles: Brussels, Belgium
    • Desbois, A.; Lutz, M. In Hemoglobin; Schnek, A. G., Paul, C., Eds.; Editions de l 'Université de Bruxelles: Brussels, Belgium, 1983; pp 285-298.
    • (1983) Hemoglobin , pp. 285-298
    • Desbois, A.1    Lutz, M.2
  • 74
    • 84906360873 scopus 로고    scopus 로고
    • as mode with a pyrrole tilt is considered.41.
    • as mode with a pyrrole tilt is considered.41.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.