4.6 Article

Temperature Dependence of Charge and Spin Transfer in Azurin

期刊

JOURNAL OF PHYSICAL CHEMISTRY C
卷 125, 期 18, 页码 9875-9883

出版社

AMER CHEMICAL SOC
DOI: 10.1021/acs.jpcc.1c01218

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资金

  1. National Institutes of Health [GM-48043]
  2. Minerva Foundation
  3. Israel Science Foundation
  4. NSF [CHE-1900078]
  5. National Institute of Diabetes and Digestive and Kidney Diseases of the National Institutes of Health [R01DK019038]

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The study found distinct mechanisms for charge and spin transfer within proteins using different Ru-modified azurin derivatives. The charge transfer yield shows weak temperature dependence, while the spin selectivity improves with increasing temperature. This suggests a new role for protein structure in biochemical redox processes.
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.

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