Effect of chemical substitution on the surface charge of the photosynthetic Reaction Center from Rhodobacter sphaeroides
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MRS Advances © 2020 Materials Research Society DOI: 10.1557/adv.2020.281
Effect of chemical substitution on the surface charge of the photosynthetic Reaction Center from Rhodobacter sphaeroides: an in-silico investigation. Gabriella Buscemi,1,2 Francesco Milano2, Danilo Vona1, Gianluca M. Farinola1,*, Massimo Trotta2,* 1
Dipartimento di Chimica, Università degli Studi di Bari Aldo Moro, Via Orabona 4 70126, Bari Italy
2
IPCF-CNR Istituto per i processi Chimico-Fisici, Consiglio Nazionale delle Ricerche, Via Orabona 4, 70126, Bari, Italy
The Reaction Centers (RCs) proteins are membrane proteins representing the key component so flight energy transduction in photosynthetic organisms. Upon photon absorption, these photoenzymes produce a long lasting intra protein hole electron couples whose charges are separated by 3 nanometers. The dipoles formed within the RCs can be effectively employed as transducing cores of several biological-organic hybrid devices whose design can accomplish photocurrents generation or act as phototransistor. To widen the application of the RCs to as many substrate as possible one valuable strategy is the bioconjugation of the protein with specific molecules ad-hoc selected to improve enzymatic performance and/or integration in proper scaffolding. In the present manuscript, we investigate the changes of the isoelectric point of the RC from the carotenoidless strain of the photosynthetic bacterium Rhodobacter sphaeroides R26 by inducing “in silico” mutations to predict on the role of the aminoacids involved in the bioconjugation.
INTRODUCTION The integration of the stunning efficiency of photosynthesis with the rapidly developing field of organic electronics is opening a completely new scenario in the quest 1
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for biocompatible, environmentally sustainable and efficient energy conversion systems. Photosynthetic microorganisms, active subcellular components, photosynthetic enzymes and pigments can be used as energy transducing units in properly designed bioelectrical hybrid devices[1]. For the purpose of the present manuscript, attention will be focused on the photochemical core, the so-called reaction center (RC), extracted from the green strain of the purple non-sulphur bacterium Rhodobacter sphaeroides R26. The RC is a specialized pigment-protein complex able to absorb light and transducing its energy in a intraprotein dipole formed by a positive and a negative charges separated by roughly three nanometers. With the opportune precautions and chemical modifications[2-3], these photoenzymes can be integrate in biohybrid devices for several applicative purposes[46].The three-dimensional structure of the RC from Rhodobacter sphaeroides R26 and the role of the protein subunits and of the cofactors in the cascade of electron transfer reactions that eventually
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