Charge transport in bacteriorhodopsin monolayers: The contribution of conformational change to current-voltage characteristics

E. Alfinito; L. Reggiani

doi:10.1209/0295-5075/85/68002

All issues

Volume 85 / No 6 (March 2009)

EPL, 85 6 (2009) 68002

Abstract

Issue		EPL Volume 85, Number 6, March 2009


Article Number		68002
Number of page(s)		6
Section		Interdisciplinary Physics and Related Areas of Science and Technology
DOI		https://doi.org/10.1209/0295-5075/85/68002
Published online		01 April 2009

EPL, 85 (2009) 68002

Charge transport in bacteriorhodopsin monolayers: The contribution of conformational change to current-voltage characteristics

E. Alfinito¹^,2 and L. Reggiani¹^,2

¹ Dipartimento di Ingegneria dell'Innovazione, Università del Salento - via Arnesano, I-73100 Lecce, Italy, EU
² CNISM, Consorzio Nazionale Interuniversitario per le Scienze Fisiche della Materia via della Vasca Navale 84, I-00146 Roma, Italy, EU

Corresponding author: eleonora.alfinito@unile.it

Received: 13 November 2008
Accepted: 23 February 2009

Abstract

When moving from native to light-activated bacteriorhodospin, modification of charge transport consisting of an increase of conductance is correlated to the protein conformational change. A theoretical model based on a map of the protein tertiary structure into a resistor network is implemented to account for a sequential tunneling mechanism of charge transfer through neighbouring amino acids. The model is validated by comparison with current-voltage experiments. The predictability of the model is further tested on bovine rhodopsin, a G-protein coupled receptor (GPCR) also sensitive to light. In this case, results show an opposite behaviour with a decrease of conductance in the presence of light.

PACS: 87.85.jc – Electrical, thermal, and mechanical properties of biological matter / 87.15.hp – Conformational changes / 87.10.Rt – Monte Carlo simulations

© EPLA, 2009

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