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

Publication: Research - peer-reviewJournal article – Annual report year: 2010

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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
Publication date2010
Volume584
Issue15
Pages3376-3380
ISSN0014-5793
DOIs
StatePublished
CitationsWeb of Science® Times Cited: 6

Keywords

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