Abstract
Spin transport in a molecule was recently examined to discuss the chiral-induced spin selectivity (CISS) effect. This effect has been particularly reported in metalloproteins because the presence of transition metals improves spin polarization in a helical peptide structure. Among metalloproteins, iron-sulfur proteins have ubiquitous redox properties in photosynthesis and respiration. Iron can enhance spin polarization. In this study, the coherent spin transport in an Fe-S protein was investigated using first-principles calculations based on the Landauer formula. Proteins containing the [4Fe-4S] cluster were used for the calculations. The results of the spin transmission pathway revealed spin flow via Fe-S clusters.
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