Literature DB >> 16798796

CW-EPR and ENDOR study of cytochrome c6 from Anabaena PCC 7119.

Inés García-Rubio1, Milagros Medina, Richard Cammack, Pablo J Alonso, Jesús I Martínez.   

Abstract

The detailed analysis of the continuous-wave electron paramagnetic resonance and electron nuclear double resonance measurements on cytochrome c(6) from Anabaena PCC7119 reveals several electronic and structural properties of this hemeprotein. The oxidized protein shows two forms that differ in the arrangement of the residues that act as heme axial ligands. Information about the orientation of these residues is obtained for one of the forms, which turns out to differ from that found in the reduced protein from x-ray experiments. The biological significance of these results is discussed.

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Year:  2006        PMID: 16798796      PMCID: PMC1557542          DOI: 10.1529/biophysj.105.080358

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  23 in total

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Journal:  J Am Chem Soc       Date:  2001-03-07       Impact factor: 15.419

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Authors:  A P Campos; A P Aguiar; M Hervás; M Regalla; J A Navarro; J M Ortega; A V Xavier; M A De La Rosa; M Teixeira
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  3 in total

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3.  Hyperfine correlation spectroscopy and electron spin echo envelope modulation spectroscopy study of the two coexisting forms of the hemeprotein cytochrome c6 from Anabaena Pcc7119.

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  3 in total

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