Hyperfine Correlation Spectroscopy and Electron Spin Echo Envelope Modulation Spectroscopy Study of the Two Coexisting Forms of the Hemeprotein Cytochrome c6 from Anabaena Pcc7119
Resumen: Oxidized cytochrome from Anabaena PCC 7119 was studied by electron spin echo envelope modulation spectroscopy. Hyperfine couplings of the unpaired electron with several nuclei were detected, in particular those of the nitrogens bound to the iron atom. Combining the experimental information here presented and previous continuous wave-electron paramagnetic resonance and electron nuclear double resonance results, some details on the electronic structure of the heme center in the protein are obtained. These results are discussed on the basis of a molecular model that considers one unpaired electron localized mainly in the iron d orbitals and propagation of the spin density within the heme center via spin polarization of the nitrogen σ-orbitals. The coexistence of two heme forms at physiological pH values in this c-type cytochrome is also discussed taking into account the experimental evidence.
Idioma: Inglés
DOI: 10.1529/biophysj.108.133272
Año: 2009
Publicado en: BIOPHYSICAL JOURNAL 96, 1 (2009), 141-152
ISSN: 0006-3495

Factor impacto JCR: 4.39 (2009)
Categ. JCR: BIOPHYSICS rank: 10 / 74 = 0.135 (2009) - Q1 - T1
Tipo y forma: Article (Published version)
Área (Departamento): Área Bioquímica y Biolog.Mole. (Dpto. Bioq.Biolog.Mol. Celular)
Área (Departamento): Área Física Materia Condensada (Dpto. Física Materia Condensa.)

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Este artículo se encuentra en las siguientes colecciones:
articulos > articulos-por-area > bioquimica_y_biologia_molecular
articulos > articulos-por-area > fisica_de_la_materia_condensada



 Notice créée le 2024-02-19, modifiée le 2024-02-19


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