Controlling electron transfer between the two cofactor chains of photosystem i by the redox state of one of their components

Stefano Santabarbara, Bradford Bullock, Fabrice Rappaport, Kevin Redding

    Research output: Contribution to journalArticle

    6 Citations (Scopus)

    Abstract

    Two functional electron transfer (ET) chains, related by a pseudo-C2 symmetry, are present in the reaction center of photosystem I (PSI). Due to slight differences in the environment around the cofactors of the two branches, there are differences in both the kinetics of ET and the proportion of ET that occurs on the two branches. The strongest evidence that this is indeed the case relied on the observation that the oxidation rates of the reduced phylloquinone (PhQ) cofactor differ by an order of magnitude. Site-directed mutagenesis of residues involved in the respective PhQ-binding sites resulted in a specific alteration of the rates of semiquinone oxidation. Here, we show that the PsaA-F689N mutation results in an ∼100-fold decrease in the observed rate of PhQA- oxidation. This is the largest change of PhQA- oxidation kinetics observed so far for a single-point mutation, resulting in a lifetime that exceeds that of the terminal electron donor, P700+. This situation allows a second photochemical charge separation event to be initiated before PhQA- has decayed, thereby mimicking in PSI a situation that occurs in type II reaction centers. The results indicate that the presence of PhQA- does not impact the overall quantum yield and leads to an almost complete redistribution of the fractional utilization of the two functional ET chains, in favor of the one that does not bear the charged species. The evolutionary implications of these results are also briefly discussed.

    Original languageEnglish (US)
    Pages (from-to)1537-1547
    Number of pages11
    JournalBiophysical Journal
    Volume108
    Issue number6
    DOIs
    StatePublished - Mar 24 2015

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    Oxidation-Reduction
    Electrons
    Vitamin K 1
    Photosystem I Protein Complex
    Site-Directed Mutagenesis
    Point Mutation
    Binding Sites
    Mutation

    ASJC Scopus subject areas

    • Biophysics

    Cite this

    Controlling electron transfer between the two cofactor chains of photosystem i by the redox state of one of their components. / Santabarbara, Stefano; Bullock, Bradford; Rappaport, Fabrice; Redding, Kevin.

    In: Biophysical Journal, Vol. 108, No. 6, 24.03.2015, p. 1537-1547.

    Research output: Contribution to journalArticle

    Santabarbara, Stefano ; Bullock, Bradford ; Rappaport, Fabrice ; Redding, Kevin. / Controlling electron transfer between the two cofactor chains of photosystem i by the redox state of one of their components. In: Biophysical Journal. 2015 ; Vol. 108, No. 6. pp. 1537-1547.
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