Literature DB >> 6301577

Electrochemical approach to the mechanism of urea denaturation of horse heart cytochrome c.

R Pilard, J Haladjian, P Bianco, P A Serre, V Brabec.   

Abstract

The effect of urea denaturation on the electroactivity of horse heart cytochrome c has been studied by differential pulse polarography and cyclic voltammetry at a gold electrode; the gold electrode was activated by 4,4'-bipyridine. Essentially, two redox couples with E'01 approximately equal to 0.25 V and E'02 approximately equal to -0.05 V (vs. normal hydrogen electrode) have been detected. The experimental results have been interpreted on the basis of the existence of equilibria between native and denatured electroactive forms; transitory species have been assumed to appear on reduction. The scheme that we have proposed agrees well with the conclusions obtained previously by other authors on conformational changes. Moreover, the advantage of electrochemical techniques in investigating the denaturation process has been underlined.

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Year:  1983        PMID: 6301577     DOI: 10.1016/0301-4622(83)80007-6

Source DB:  PubMed          Journal:  Biophys Chem        ISSN: 0301-4622            Impact factor:   2.352


  1 in total

1.  The impact of urea-induced unfolding on the redox process of immobilised cytochrome c.

Authors:  Stefano Monari; Diego Millo; Antonio Ranieri; Giulia Di Rocco; Gert van der Zwan; Cees Gooijer; Silvia Peressini; Claudio Tavagnacco; Peter Hildebrandt; Marco Borsari
Journal:  J Biol Inorg Chem       Date:  2010-06-13       Impact factor: 3.358

  1 in total

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