School of Chemistry and Chemical Engineering, Laboratory of Protein Structure and Function, Hunan Key Laboratory for the Design and Application of Actinide Complexes, University of South China, Hengyang 421001, China.
School of Chemistry and Chemical Engineering, Laboratory of Protein Structure and Function, Hunan Key Laboratory for the Design and Application of Actinide Complexes, University of South China, Hengyang 421001, China.
J Inorg Biochem. 2022 Oct;235:111943. doi: 10.1016/j.jinorgbio.2022.111943. Epub 2022 Jul 25.
Heme proteins have recently emerged as promising artificial metalloenzymes for catalyzing diverse reactions. In this report, L29E Mb, a single mutant of myoglobin (Mb), was reconstituted by replacing the heme with a sodium copper cholorophyllin (CuCP) to form a new green artificial enzyme (named CuCP-L29E Mb). The reconstituted protein CuCP-L29E Mb was found to exhibit hydrolytic DNA cleavage activity, which was not depending on O. In addition, Mg ion could effectively promote the DNA cleavage activity of CuCP-L29E Mb. Wild-type (WT) Mb reconstituted with CuCP (named CuCP-WT Mb) did not show DNA cleavage activity under the same conditions. This study suggests that both Mg and the ligand Glu29 are critical for the nuclease activity and the artificial nuclease of Mg-CuCP-L29E Mb may have potential applications in the future.
血红素蛋白最近已成为有前途的人工金属酶，可用于催化多种反应。在本报告中，肌红蛋白（Mb）的单点突变 L29E Mb 通过用钠铜叶绿素（CuCP）取代血红素来重新构成，形成一种新的绿色人工酶（命名为 CuCP-L29E Mb）。发现该重组蛋白 CuCP-L29E Mb 具有水解 DNA 切割活性，该活性不依赖于 O。此外，Mg 离子可有效促进 CuCP-L29E Mb 的 DNA 切割活性。在相同条件下，用 CuCP 重新构成的野生型（WT）Mb（命名为 CuCP-WT Mb）没有显示 DNA 切割活性。本研究表明，Mg 和配体 Glu29 对于核酸酶活性都是至关重要的，并且 Mg-CuCP-L29E Mb 的人工核酸酶可能在未来具有潜在的应用。
