Thermal Stability of α-Phycoerythrocyanin |
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Institution: | 1. Faculty of Technology, University of Nis, Bulevar oslobođenja 124, 16 000, Leskovac, Serbia;;2. State Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan 430070, P.R. China;;3. Department of Biologie II, Ludwig-Maximilians Universitat, 80638 Munchen, Germany |
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Abstract: | The α-subunit of the phycobiliprotein, phycoerythrocyanin (α-PEC), from Mastigocladus laminosus shows photoreversible photochromism that is based on the Z ↔ E isomerization of the phycoviolobilin (PVB) chromophore. Thermal stability of the photochemistry and chromoprotein secondary structure have been studied by absorption and circular dichroism (CD) spectroscopy. Both photoisomers are stable and photoconvertible up to ∼ 70 °C. At T > 75 °C, photochemistry ceases because the E-state reverts rapidly thermally to the Z–state. The chromoprotein melts at 72 °C, the apoprotein already at 55 °C, indicating a considerable stabilization of the protein secondary structure by the chromophore. |
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Keywords: | Denaturation photoisomerization phycobiliprotein phycoerythrocyanin protein stabilization by chromophore renaturation |
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