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Báo cáo thường niên
Tạp chí khoa học ĐHCT
Tạp chí tiếng anh ĐHCT
Tạp chí trong nước
Tạp chí quốc tế
Kỷ yếu HN trong nước
Kỷ yếu HN quốc tế
Book chapter
Bài báo - Tạp chí
18 (2017) Trang: 2451–2458
Tạp chí: chemphyschem

A recent study [Angew. Chem. Int. Ed201554, 7391–7394] has shown that horse heart myoglobin (HHM) is selectively hydrolyzed by a range of zirconium(IV)-substituted polyoxometalates (POMs) under mild conditions. In this study, the molecular interactions between the Zr-POM catalysts and HHM are investigated by using a range of complementary techniques, including circular dichroism (CD), UV/Vis spectroscopy, tryptophan fluorescence spectroscopy, and 1H and 31P NMR spectroscopy. A tryptophan fluorescence quenching study reveals that, among all examined Zr-POMs, the most reactive POM, 2:2 ZrIV-Keggin, exhibits the strongest interaction with HHM. 31P NMR spectroscopy studies show that this POM dissociates in solution, resulting in the formation of a monomeric 1:1 ZrIV-Keggin structure, which is likely to be a catalytically active species. In the presence of ZrIV-POMs, HHM does not undergo complete denaturation, as evidenced by CD, UV/Vis, tryptophan fluorescence, and 1H NMR spectroscopy. CD spectroscopy shows a gradual decrease in the α-helical content of HHM upon addition of ZrIV-POMs. The largest effect is observed in the presence of a large ZrIV-Wells–Dawson structure, whereas small ZrIV-Lindqvist POM has the least influence on the decrease in the α-helical content of HHM. In all cases, the Soret band at λ=409 nm is maintained in the presence of all examined Zr-POMs, which indicates that no conformational changes in the protein occur near the heme group.

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