Ultrafast Charge-Transfer Dynamics in the Iron-Sulfur Complex of Rhodobacter capsulatus Ferredoxin VI

Ziliang Mao, Elizabeth C. Carroll, Peter W. Kim, Stephen P. Cramer, Delmar S. Larsen

    Research output: Contribution to journalArticleScientificpeer-review

    5 Citations (Scopus)

    Abstract

    Iron-sulfur proteins play essential roles in various biological processes. Their electronic structure and vibrational dynamics are key to their rich chemistry but nontrivial to unravel. Here, the first ultrafast transient absorption and impulsive coherent vibrational spectroscopic (ICVS) studies on 2Fe-2S clusters in Rhodobacter capsulatus ferreodoxin VI are characterized. Photoexcitation initiated populations on multiple excited electronic states that evolve into each other in a long-lived charge-transfer state. This suggests a potential light-induced electron-transfer pathway as well as the possibility of using iron-sulfur proteins as photosensitizers for light-dependent enzymes. A tyrosine chain near the active site suggests potential hole-transfer pathways and affirms this electron-transfer pathway. The ICVS data revealed vibrational bands at 417 and 484 cm-1, with the latter attributed to an excited-state mode. The temperature dependence of the ICVS modes suggests that the temperature effect on protein structure or conformational heterogeneities needs to be considered during cryogenic temperature studies.

    Original languageEnglish
    Pages (from-to)4498-4503
    Number of pages6
    JournalThe Journal of Physical Chemistry Letters
    Volume8
    Issue number18
    DOIs
    Publication statusPublished - 21 Sep 2017

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