Thermodynamics of substrate binding to the metal site in homoprotocatechuate 2,3-dioxygenase: Using ITC under anaerobic conditions to study enzyme-substrate interactions
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- 作者：Kate L. Henderson ; Danielle H. Francis ; Edwin A. Lewis ; elewis@ichemsitry.msstate.edu" class="auth_mail" title="E-mail the corresponding author ; Joseph P. Emerson ; jemerson@chemistry.msstate.edu" class="auth_mail" title="E-mail the corresponding author
- 关键词：Nonheme iron(II) ; Extradiol dioxygenase ; Manganese(II) ; 4-nitrocatechol ; Homoprotocatechuate
- 刊名：Biochimica et Biophysica Acta (BBA) - General Subjects
- 出版年：2016
- 出版时间：May 2016
- 年：2016
- 卷：1860
- 期：5
- 页码：910-916
- 全文大小：653 K
文摘
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Fe(II) and Mn(II) HPCD proteins are used to probe substrate binding to the metal.
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HPCA and 4NC bind to Fe(II)HPCD with similar high affinity, ΔG ≈ − 11 kcal/mol.
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HPCA and 4NC bind to Mn(II)HPCD with lower affinity, ΔG ≈ − 4 kcal/mol.
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HPCA and 4NC binding to metallated HPCD exhibits ΔS/ΔH compensation.
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Both HPCA and 4NC bind to the metal ion in HPCD as dianions.