The Open Macromolecules Journal




    (Discontinued)

    ISSN: 1874-3439 ― Volume 7, 2014

    Conformational Transition of Cytochrome c


    The Open Macromolecules Journal , 2010, 4: 53-55

    M. Antalík, D. Fedunová, J. Bágelová

    Institute of Chemistry, Department of Biochemistry, Faculty of Sciences, P. J. Šafárik University, Moyzesova 11, 040 01 Košice, Slovak Republic;

    Electronic publication date 21/12/2010
    [DOI: 10.2174/1874343901004010053]




    Abstract:

    Conformational transitions of oxidized and reduced cytochrome c at various solvent conditions are summarized. Sorbitol stabilizes and NaCl destabilizes native cytochrome c structure against the acid denaturation. In the process of heating, NaCl more strongly stabilizes molten globular cytochtome c state than sorbitol in secondary structure region, but in heme region, sorbitol is stronger stabilizer of cytochrome c molten globular state than NaCl. In the presence of strong inorganic acids H2SO4 and HClO4 and their salts two low spin and one high-spin heme conformers occur. The unstable pentacoordinated conformer is formed in 8M H2SO4. Cytochrome c creates complexes with polyanions poly(vynilsulfate) and poly(4-styrene-sulfonate), which are able to mimic the effect of cytochrome c natural redox partner on its structure, as well as to prevent its the aggregation in aggregation prone conditions. Cytochrome c forms complexes with gold nanoparticles covered by glutation, which enhance stability in heme region at room temperature.


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