Kinetic and thermodynamic properties of two barley thioredoxin h isozymes, HvTrxh1 and HvTrxh2

Kenji Maeda, Per Hägglund, Olof Björnberg, J.R. Winther, Birte Svensson

    Research output: Contribution to journalJournal articleResearchpeer-review

    Abstract

    Barley thioredoxin h isozymes 1 (HvTrxh1) and barley thioredoxin h isozymes 2 (HvTrxh2) show distinct spatiotemporal distribution in germinating seeds. Using a novel approach involving measurement of bidirectional electron transfer rates between Escherichia coli thioredoxin, which exhibits redox-dependent fluorescence, and the barley isozymes, reaction kinetics and thermodynamic properties were readily determined. The reaction constants were 60% higher for HvTrxh1 than HvTrxh2, while their redox potentials were very similar. The primary nucleophile, Cys(N), of the active site Trp-Cys(N)-Gly-Pro-Cys
    Original languageEnglish
    JournalF E B S Letters
    Volume584
    Issue number15
    Pages (from-to)3376-3380
    ISSN0014-5793
    DOIs
    Publication statusPublished - 2010

    Keywords

    • Thioredoxin
    • Tryptophan fluorescence
    • Thiol pK(a)
    • Redox potential
    • Dithiol/disulflele exchange

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