Unidirectional Photosynthetic Complex Functionalization for Tunnel Current Distance Decay Spectroscopy

Manuel Lopez-Ortiz^a^,^b, Ricardo Zamora Brito^a^,^b, Marina Inés Giannotti^a^,^b^,^c, Nuria Camarero Palao^a^,^b, Chen Hu^d, Roberta Croce^d, Pau Gorostiza^a^,^b^,^e

^aInstitute for Bioengineering of Catalonia (IBEC), Carrer de Baldiri Reixac, Barcelona, Spain

^bBarcelona Institute of Science and Technology (BIST), Campus UAB, Bellaterra, 08193 Barcelona, Spain

^cBiomedical Research Networking Center in Bioengineering, Biomaterials, and Nanomedicine, CIBER-BBN, Spain, Spain

^dVrije Universiteit Amsterdam, Department of Physics and Astronomy, Faculty of Science, Netherlands

^eInstitució Catalana de Recerca i Estudis Avançats (ICREA), Spain, Passeig Lluis Companys 23, Barcelona, Spain

Proceedings of International Online Conference on Bio-hybrid Approaches to Solar Energy Conversion (Biohybrid)

Online, Spain, 2020 October 27th - 29th

Organizers: Jenny Zhang, Vincent Friebe and Lars Jeuken

Contributed talk, Manuel Lopez-Ortiz, presentation 019
Publication date: 8th October 2020

Interprotein electron transport (ET) is a key process for living organisms, playing a fundamental role in respiration and photosynthesis. ET processes between photosynthetic complexes and electron carrier partner proteins have been widely studied with bulk spectroscopic techniques [1]. However the characterization of ET at the level of single molecules with controlled protein-protein distance is lacking. This is due in part to the lack of a well-defined experimental setup for protein orientation and current measurement. In this work, a peptide [2] that binds selectively to plant Photosynthetic Complex I (PSI) is used to functionalize atomically flat gold monocrystal electrodes.

PSI binding is evaluated in bulk with photo-current and chopped light voltammetry and by scanning probe techniques with atomic force microscopy (AFM) and electrochemical scanning tunneling microscopy (ECSTM). ECSTM-based spectroscopic measurements allow investigating the current decay distance [3] (β [nm^-1]) of PSI functionalized electrodes under electrochemical control. Mapping β over sample and probe potentials reveals enhanced charge exchange distance as probe potential is aligned with PSI’s electron acceptor cofactor redox potential.

References:

[1] Hope, A.B. Electron transfers amongst cytochrome f, plastocyanin and photosystem I : kinetics and mechanisms. Biochimica et Biophisica acta, 2000, 1456, 5-26

[2] Gordiichuk, P;Pesce, P.; Castañeda-Ocampo, O.E; Marcozzi, A. Wetzelaer, G.J.; Paul, A; Loznik, M.; Gloukhikh, E.; Richter, S; Chiechi, R. C.; Herrmann, A. Orientation and Incorporation of Photosystem I in Bioelectronics Devices Enabled by Phage Display. Advanced Science 2017, 1600393.

[3] Artés, J. M.; Díez-Pérez I.; Sanz F., Gorostiza Artés J. M., Díez Pérez, I.; Sanz, F.; Gorostiza, P. Direct measurement of electron transfer distance decay constants of single redox proteins by electrochemical tunneling spectroscopy. , ACS Nano 2011, 5, 2060-2066.

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