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

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Kinetic and thermodynamic properties of two barley thioredoxin h isozymes, HvTrxh1 and HvTrxh2. / Maeda, Kenji; Hägglund, Per; Björnberg, Olof; Winther, Jakob R; Svensson, Birte.

In: FEBS Letters, Vol. 584, No. 15, 2010, p. 3376-3380.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Maeda, K, Hägglund, P, Björnberg, O, Winther, JR & Svensson, B 2010, 'Kinetic and thermodynamic properties of two barley thioredoxin h isozymes, HvTrxh1 and HvTrxh2', FEBS Letters, vol. 584, no. 15, pp. 3376-3380. https://doi.org/10.1016/j.febslet.2010.06.028

APA

Maeda, K., Hägglund, P., Björnberg, O., Winther, J. R., & Svensson, B. (2010). Kinetic and thermodynamic properties of two barley thioredoxin h isozymes, HvTrxh1 and HvTrxh2. FEBS Letters, 584(15), 3376-3380. https://doi.org/10.1016/j.febslet.2010.06.028

Vancouver

Maeda K, Hägglund P, Björnberg O, Winther JR, Svensson B. Kinetic and thermodynamic properties of two barley thioredoxin h isozymes, HvTrxh1 and HvTrxh2. FEBS Letters. 2010;584(15):3376-3380. https://doi.org/10.1016/j.febslet.2010.06.028

Author

Maeda, Kenji ; Hägglund, Per ; Björnberg, Olof ; Winther, Jakob R ; Svensson, Birte. / Kinetic and thermodynamic properties of two barley thioredoxin h isozymes, HvTrxh1 and HvTrxh2. In: FEBS Letters. 2010 ; Vol. 584, No. 15. pp. 3376-3380.

Bibtex

@article{b86d2db0a15111df928f000ea68e967b,
title = "Kinetic and thermodynamic properties of two barley thioredoxin h isozymes, HvTrxh1 and HvTrxh2",
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, Cys(N), of the active site Trp-Cys(N)-Gly-Pro-Cys(C) motif has an apparent pK(a) 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.",
author = "Kenji Maeda and Per H{\"a}gglund and Olof Bj{\"o}rnberg and Winther, {Jakob R} and Birte Svensson",
note = "Keywords: Thioredoxin; Dithiol/disulfide exchange; Tryptophan fluorescence; Redox potential; Thiol pKa",
year = "2010",
doi = "10.1016/j.febslet.2010.06.028",
language = "English",
volume = "584",
pages = "3376--3380",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd",
number = "15",

}

RIS

TY - JOUR

T1 - Kinetic and thermodynamic properties of two barley thioredoxin h isozymes, HvTrxh1 and HvTrxh2

AU - Maeda, Kenji

AU - Hägglund, Per

AU - Björnberg, Olof

AU - Winther, Jakob R

AU - Svensson, Birte

N1 - Keywords: Thioredoxin; Dithiol/disulfide exchange; Tryptophan fluorescence; Redox potential; Thiol pKa

PY - 2010

Y1 - 2010

N2 - 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, Cys(N), of the active site Trp-Cys(N)-Gly-Pro-Cys(C) motif has an apparent pK(a) 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.

AB - 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, Cys(N), of the active site Trp-Cys(N)-Gly-Pro-Cys(C) motif has an apparent pK(a) 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.

U2 - 10.1016/j.febslet.2010.06.028

DO - 10.1016/j.febslet.2010.06.028

M3 - Journal article

C2 - 20594550

VL - 584

SP - 3376

EP - 3380

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 15

ER -

ID: 21234844