Disentangling electron tunneling and protein dynamics of cytochrome c through a rationally designed surface mutation
Nonexponential distance dependence of the apparent electron-transfer (ET) rate has been reported for a variety of redox proteins immobilized on biocompatible electrodes, thus posing a physicochemical challenge of possible physiological relevance. We have recently proposed that this behavior may aris...
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American Chemical Society
2013
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| 003 | AR-BaUEN | ||
| 005 | 20230518205606.0 | ||
| 008 | 190411s2013 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-84878084932 | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 030 | |a JPCBF | ||
| 100 | 1 | |a Alvarez-Paggi, D. | |
| 245 | 1 | 0 | |a Disentangling electron tunneling and protein dynamics of cytochrome c through a rationally designed surface mutation |
| 260 | |b American Chemical Society |c 2013 | ||
| 270 | 1 | 0 | |m Hildebrandt, P.; Institut für Chemie, Technische Universität Berlin, Strasse des 17. Juni 135, Sekr. PC14, D-10623-Berlin, Germany; email: hildebrandt@chem.tu-berlin.de |
| 506 | |2 openaire |e Política editorial | ||
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| 520 | 3 | |a Nonexponential distance dependence of the apparent electron-transfer (ET) rate has been reported for a variety of redox proteins immobilized on biocompatible electrodes, thus posing a physicochemical challenge of possible physiological relevance. We have recently proposed that this behavior may arise not only from the structural and dynamical complexity of the redox proteins but also from their interplay with strong electric fields present in the experimental setups and in vivo (J. Am Chem. Soc. 2010, 132, 5769-5778). Therefore, protein dynamics are finely controlled by the energetics of both specific contacts and the interaction between the protein's dipole moment and the interfacial electric fields. In turn, protein dynamics may govern electron-transfer kinetics through reorientation from low to high donor-acceptor electronic coupling orientations. Here we present a combined computational and experimental study of WT cytochrome c and the surface mutant K87C adsorbed on electrodes coated with self-assembled monolayers (SAMs) of varying thickness (i.e., variable strength of the interfacial electric field). Replacement of the positively charged K87 by a neutral amino acid allowed us to disentangle protein dynamics and electron tunneling from the reaction kinetics and to rationalize the anomalous distance dependence in terms of (at least) two populations of distinct average electronic couplings. Thus, it was possible to recover the exponential distance dependence expected from ET theory. These results pave the way for gaining further insight into the parameters that control protein electron transfer. © 2013 American Chemical Society. |l eng | |
| 593 | |a INQUIMAE-CONICET, Departamento de Química Inorgánica, Analítica y Química Física, Universidad de Buenos Aires, piso 3, C1428EHA-Buenos Aires, Argentina | ||
| 593 | |a Institut für Chemie, Technische Universität Berlin, Strasse des 17. Juni 135, Sekr. PC14, D-10623-Berlin, Germany | ||
| 593 | |a Biological Research Center, Institute of Biophysics, Temesvári krt. 62, H-6726 Szeged, Hungary | ||
| 593 | |a Department of Biotechnology, University of Szeged, Közép fasor 52, H-6726, Hungary | ||
| 690 | 1 | 0 | |a AMINO ACIDS |
| 690 | 1 | 0 | |a DYNAMICS |
| 690 | 1 | 0 | |a ELECTRIC FIELDS |
| 690 | 1 | 0 | |a ELECTRODES |
| 690 | 1 | 0 | |a ELECTRON TUNNELING |
| 690 | 1 | 0 | |a REACTION KINETICS |
| 690 | 1 | 0 | |a SELF ASSEMBLED MONOLAYERS |
| 690 | 1 | 0 | |a DYNAMICAL COMPLEXITY |
| 690 | 1 | 0 | |a ELECTRON TRANSFER |
| 690 | 1 | 0 | |a ELECTRON TRANSFER KINETICS |
| 690 | 1 | 0 | |a ELECTRONIC COUPLING |
| 690 | 1 | 0 | |a EXPERIMENTAL STUDIES |
| 690 | 1 | 0 | |a POSITIVELY CHARGED |
| 690 | 1 | 0 | |a STRONG ELECTRIC FIELDS |
| 690 | 1 | 0 | |a VARYING THICKNESS |
| 690 | 1 | 0 | |a PROTEINS |
| 700 | 1 | |a Meister, W. | |
| 700 | 1 | |a Kuhlmann, U. | |
| 700 | 1 | |a Weidinger, I. | |
| 700 | 1 | |a Tenger, K. | |
| 700 | 1 | |a Zimányi, L. | |
| 700 | 1 | |a Rákhely, G. | |
| 700 | 1 | |a Hildebrandt, P. | |
| 700 | 1 | |a Murgida, D.H. | |
| 773 | 0 | |d American Chemical Society, 2013 |g v. 117 |h pp. 6061-6068 |k n. 20 |p J Phys Chem B |x 15206106 |w (AR-BaUEN)CENRE-5879 |t Journal of Physical Chemistry B | |
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