國家衛生研究院 NHRI:Item 3990099045/2357
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    題名: Thermoinactivaion analysis of vacuolar H+-pyrophosphatase
    作者: Yang, SH;Jiang, SS;Hsiao, YY;Van, RC;Pan, YJ;Pan, RL
    貢獻者: Division of Molecular and Genomic Medicine
    摘要: Vacuolar H+-translocating pyrophosphatase (H+-PPase- EC 3.6.1.1) catalyzes both the hydrolysis of PPi and the electrogenic translocation of proton from the cytosol to the lumen of the vacuole. Vacuolar H+-PPase, purified from etiolated hypocotyls of mung bean (Vigna radiata L.), is a homodimer with a molecular mass of 145 kDa. To investigate the relationship between structure and function of this W-translocating enzyme, thermoinactivation analysis was employed. Thermoinactivation studies suggested that vacuolar H+-PPase consists of two distinct states upon heat treatment and exhibited different transition temperatures in the presence and absence of ligands (substrate and inhibitors). Substrate protection of H+-PPase stabilizes enzyme structure by increasing activation energy from 54.9 to 70.2 kJ/mol. We believe that the conformation of this enzyme was altered in the presence of substrate to protect against the thermoinactivation. In contrast, the modification of H+-PPase by inhibitor (fluorescein 5'-isothiocyanate; FITC) augmented the inactivation by heat treatment. The native, substrate-bound, and FITC-labeled vacuolar H+-PPases possess probably distinct conformation and show different modes of susceptibility to thermoinactivation. Our results also indicate that the structure of one subunit of this homodimer exerts long distance effect on the other, suggesting a specific subunit-subunit interaction in vacuolar H+-PPase. A working model was proposed to interpret the relationship of the structure and function of vacuolar H+-PPase. (C) 2004 Elsevier B.V. All rights reserved.
    關鍵詞: Biochemistry & Molecular Biology;Biophysics
    日期: 2004-06-07
    關聯: Biochimica Et Biophysica Acta-Bioenergetics. 2004 Jun;1656(2-3):88-95.
    Link to: http://dx.doi.org/10.1016/j.bbabio.2004.02.001
    JIF/Ranking 2023: http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=NHRI&SrcApp=NHRI_IR&KeyISSN=0005-2728&DestApp=IC2JCR
    Cited Times(WOS): https://www.webofscience.com/wos/woscc/full-record/WOS:000222220500002
    Cited Times(Scopus): http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=3142657551
    顯示於類別:[江士昇] 期刊論文

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