The steady-state charge and spin transfer yields were measured for three different Ru-modified azurin derivatives in protein films on silver electrodes. While the charge-transfer yields exhibit weak temperature dependences, consistent with operation of a near activation-less mechanism, the spin selectivity of the electron transfer improves as temperature increases. This enhancement of spin selectivity with temperature is explained by a vibrationally induced spin exchange interaction between the Cu(II) and its chiral ligands. These results indicate that distinct mechanisms control charge and spin transfer within proteins. As with electron charge transfer, proteins deliver polarized electron spins with a yield that depends on the protein's structure. This finding suggests a new role for protein structure in biochemical redox processes.

Temperature Dependence of Charge and Spin Transfer in Azurin / Sang, Y.; Mishra, S.; Tassinari, F.; Karuppannan, S. K.; Carmieli, R.; Teo, R. D.; Migliore, A.; Beratan, D. N.; Gray, H. B.; Pecht, I.; Fransson, J.; Waldeck, D. H.; Naaman, R.. - In: JOURNAL OF PHYSICAL CHEMISTRY. C. - ISSN 1932-7447. - 125:18(2021), pp. 9875-9883. [10.1021/acs.jpcc.1c01218]

Temperature Dependence of Charge and Spin Transfer in Azurin

Tassinari F.;Migliore A.;Naaman R.
2021

Abstract

The steady-state charge and spin transfer yields were measured for three different Ru-modified azurin derivatives in protein films on silver electrodes. While the charge-transfer yields exhibit weak temperature dependences, consistent with operation of a near activation-less mechanism, the spin selectivity of the electron transfer improves as temperature increases. This enhancement of spin selectivity with temperature is explained by a vibrationally induced spin exchange interaction between the Cu(II) and its chiral ligands. These results indicate that distinct mechanisms control charge and spin transfer within proteins. As with electron charge transfer, proteins deliver polarized electron spins with a yield that depends on the protein's structure. This finding suggests a new role for protein structure in biochemical redox processes.
2021
125
18
9875
9883
Temperature Dependence of Charge and Spin Transfer in Azurin / Sang, Y.; Mishra, S.; Tassinari, F.; Karuppannan, S. K.; Carmieli, R.; Teo, R. D.; Migliore, A.; Beratan, D. N.; Gray, H. B.; Pecht, I.; Fransson, J.; Waldeck, D. H.; Naaman, R.. - In: JOURNAL OF PHYSICAL CHEMISTRY. C. - ISSN 1932-7447. - 125:18(2021), pp. 9875-9883. [10.1021/acs.jpcc.1c01218]
Sang, Y.; Mishra, S.; Tassinari, F.; Karuppannan, S. K.; Carmieli, R.; Teo, R. D.; Migliore, A.; Beratan, D. N.; Gray, H. B.; Pecht, I.; Fransson, J.; Waldeck, D. H.; Naaman, R.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11380/1261977
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