Journal article
Kinetic and thermodynamic properties of two barley thioredoxin h isozymes, HvTrxh1 and HvTrxh2
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
Language: | English |
---|---|
Year: | 2010 |
Pages: | 3376-3380 |
ISSN: | 18733468 and 00145793 |
Types: | Journal article |
DOI: | 10.1016/j.febslet.2010.06.028 |
ORCIDs: | 0000-0001-6995-9154 and Svensson, Birte |