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 approximately 60% higher for HvTrxh1 than HvTrxh2, while their redox potentials were very similar. The primary nucleophile, CysN, of the active site Trp-CysN-Gly-Pro-CysC motif has an apparent pKa of 7.6 in both isozymes, as found by iodoacetamide titration, but showed approximately 70% higher reactivity in HvTrxh1, suggesting significant functional difference between the isozymes.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Maeda K,Hägglund P,Björnberg O,Winther JR,Svensson Bdoi
10.1016/j.febslet.2010.06.028subject
Has Abstractpub_date
2010-08-04 00:00:00pages
3376-80issue
15eissn
0014-5793issn
1873-3468pii
S0014-5793(10)00523-5journal_volume
584pub_type
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