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Updated: Aug 7, 2026
Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues
Published on: November 22, 2014
Rational design of an artificial hydrolytic nuclease by introduction of a sodium copper chlorophyllin in L29E
Yao Dong1, Yu-Mei Chen1, Xiang-Jun Kong1
1School 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.
Abstract:
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 O2. In addition, Mg2+ 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 Mg2+ and the ligand Glu29 are critical for the nuclease activity and the artificial nuclease of Mg2+-CuCP-L29E Mb may have potential applications in the future.
