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Biophysical Journal 89:2783-2791 (2005)
© 2005 The Biophysical Society

Single Molecule Recognition between Cytochrome C 551 and Gold-Immobilized Azurin by Force Spectroscopy

B. Bonanni *, A. S. M. Kamruzzahan {dagger}, A. R. Bizzarri *, C. Rankl {dagger}, H. J. Gruber {dagger}, P. Hinterdorfer {dagger} and S. Cannistraro *

* Biophysics and Nanoscience Centre, Istituto Nazionale Fisica della Materia-Consorzio Nazionale Interuniversitario per le Scienze Fisiche della Materia (INFM-CNISM), Dipartimento di Scienze Ambientali, Università della Tuscia, Viterbo, Italy; and {dagger} Institute for Biophysics, Johannes Kepler University of Linz, Linz, Austria

Correspondence: Address reprint requests to Beatrice Bonanni, Biophysics and Nanoscience Centre, INFM-CNISM, Dipartimento di Scienze Ambientali, Università della Tuscia, Largo dell'Università, I-01100 Viterbo, Italy. Tel.: 39-0761-357027; Fax: 39-0761-357179; E-mail: bonanni{at}unitus.it.

Recent developments in single molecule force spectroscopy have allowed investigating the interaction between two redox partners, Azurin and Cytochrome C 551. Azurin has been directly chemisorbed on a gold electrode whereas cytochrome c has been linked to the atomic force microscopy tip by means of a heterobifunctional flexible cross-linker. When recording force-distance cycles, molecular recognition events could be observed, displaying unbinding forces of ~95 pN for an applied loading rate of 10 nN/s. The specificity of molecular recognition was confirmed by the significant decrease of unbinding probability observed in control block experiments performed adding free azurin solution in the fluid cell. In addition, the complex dissociation kinetics has been here investigated by monitoring the unbinding forces as a function of the loading rate: the thermal off-rate was estimated to be ~14 s–1, much higher than values commonly estimated for complexes more stable than electron transfer complexes. Results here discussed represent the first studies on molecular recognition between two redox partners by atomic force microscopy.




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