Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 137, Issue 35, Pages 11226-11229Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jacs.5b06501
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- J & R Center for Scientific Research
- Council for Higher Education (Israel)
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We observe temperature-independent electron transport, characteristic of tunneling across a similar to 6 nm thick Halorhodopsin (phR) monolayer. phR contains both retinal and a carotenoid, bacterioruberin, as cofactors, in a trimeric protein-chromophore complex. This finding is unusual because for conjugated oligo-imine molecular wires a transition from temperature-independent to -dependent electron transport, ETp, was reported at similar to 4 nm wire length. In the similar to 6 nm long phR, the similar to 4 nm 50-carbon conjugated bacterioruberin is bound parallel to the alpha-helices of the peptide backbone. This places bacterioruberin's ends proximal to the two electrodes that contact the protein; thus, coupling to these electrodes may facilitate the activation-less current across the contacts. Oxidation of bacterioruberin eliminates its conjugation, causing the ETp to become temperature dependent (>180 K). Remarkably, even elimination of the retinal-protein covalent bond, with the fully conjugated bacterioruberin still present, leads to temperature-dependent ETp (>180 K). These results suggest that ETp via phR is cooperatively affected by both retinal and bacterioruberin cofactors.
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