FEBS Letters
Volume 582, Issue 6 , Pages 1003-1007, 19 March 2008

Fast folding kinetics and stabilization of apo-cytochrome c

Edited by Peter Brzezinski

  • Alessandro Borgia

      Affiliations

    • Dipartimento di Scienze Biochimiche, “A. Rossi Fanelli”, Sapienza, Università di Roma, Piazzale A. Moro 5, 00185 Rome, Italy
    • ,
  • Stefano Gianni

      Affiliations

    • Istituto di Biologia e Patologia Molecolari del CNR, Sapienza, Università di Roma, Piazzale A. Moro 5, 00185 Rome, Italy
    • ,
  • Maurizio Brunori

      Affiliations

    • Dipartimento di Scienze Biochimiche, “A. Rossi Fanelli”, Sapienza, Università di Roma, Piazzale A. Moro 5, 00185 Rome, Italy
    • ,
  • Carlo Travaglini-Allocatelli

      Affiliations

    • Dipartimento di Scienze Biochimiche, “A. Rossi Fanelli”, Sapienza, Università di Roma, Piazzale A. Moro 5, 00185 Rome, Italy
    • Corresponding Author InformationCorresponding author. Fax: +39 064440062.

Received 8 January 2008; received in revised form 19 February 2008; accepted 20 February 2008. published online 26 February 2008.

Abstract 

It is generally accepted that in the c-type cytochromes the covalently bound heme plays a primary role in the acquisition of the folded state. Here, we show that a stabilized site-directed variant of apo-cyt c551 from Pseudomonas aeruginosa (Pa-apocyt F7A/W77F) retains native-like features in the presence of sodium sulfate even in the absence of heme. By time-resolved intrinsic fluorescence, we have evidence that Pa-apocyt F7A/W77F may acquire a compact, native-like conformation within microseconds. These results challenge current thinking about the role of the heme group in the folding of c-type cytochromes.

Keywords: Apo-cytochrome c, Stability, Fast folding kinetics, Continuous-flow

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PII: S0014-5793(08)00157-9

doi:10.1016/j.febslet.2008.02.046

FEBS Letters
Volume 582, Issue 6 , Pages 1003-1007, 19 March 2008

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