| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10797714 | Biochimica et Biophysica Acta (BBA) - Biomembranes | 2011 | 9 Pages |
Abstract
⺠TcHMA4, a Cd/Zn-ATPase has been purified from roots in its native state. ⺠TcHMA4 displayed highest activity with submicromolar concentrations of Cd2+, Cu2+ and Zn2+. ⺠Concentration-dependent changes in activation energy were different for the three metals tested. ⺠The temperature optimum for ATPase activity was reached at approximately 40 °C for all tested metals. ⺠EXAFS measurements showed that Cd in TcHMA4 is bound by S from cysteines and not by N from histidines.
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Authors
Barbara Leitenmaier, Annelie Witt, Annabell Witzke, Anastasia Stemke, Wolfram Meyer-Klaucke, Peter M.H. Kroneck, Hendrik Küpper,