Temperature Dependence of Charge and Spin Transfer in Azurin.

Journal Article (Journal Article)

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.

Full Text

Duke Authors

Cited Authors

  • Sang, Y; Mishra, S; Tassinari, F; Karuppannan, SK; Carmieli, R; Teo, RD; Migliore, A; Beratan, DN; Gray, HB; Pecht, I; Fransson, J; Waldeck, DH; Naaman, R

Published Date

  • May 1, 2021

Published In

Volume / Issue

  • 125 / 18

Start / End Page

  • 9875 - 9883

PubMed ID

  • 34055128

Pubmed Central ID

  • PMC8154855

Electronic International Standard Serial Number (EISSN)

  • 1932-7455

International Standard Serial Number (ISSN)

  • 1932-7447

Digital Object Identifier (DOI)

  • 10.1021/acs.jpcc.1c01218


  • eng