Structure advantage and peroxidase activity enhancement of deuterohemin-peptide-inorganic hybrid nanoflowers

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Structure advantage and peroxidase activity enhancement of deuterohemin-peptide-inorganic hybrid nanoflowers

【Author】

Zijian Zhao;Ji Zhang;Zhengqiang Li;

【Abstract】

<正>Introduction Deuterohemin-P-Ala-His-Thr-Val-Glu-Lys(DhHP-6)is an artificial synthesized heme-peptide.In DhHP-6,a short length peptide of six amino acid residues(AlaHisThrValGluLys)referred to the residues of microperoxidase modifies on the propionic acid side chain of iron porphyrin.DhHP-6 as a peroxidase mimic shows a high peroxidase enzyme activity.However,DhHP-6 has a tendency to aggregate in aqueous

【Keywords】

Lys;Structure advantage and peroxidase activity enhancement of deuterohemin-peptide-inorganic hybrid nanoflowers;

The 14th China-Japan-Korea Joint Symposium on Enzyme Engineering Conference Proceeding

References

To explore the background and basis of the node document

Total: 3 articles

[1] Qing-Guang Dong;;Yong Zhang;;Meng-Shu Wang;;Jiao Feng;;Hai-Hong Zhang;;Yong-Ge Wu;;Tie-Jun Gu;;Xiang-Hui Yu;;Chun-Lai Jiang;;Yan Chen;;Wei Li;;Wei Kong, Improvement of enzymatic stability and intestinal permeability of deuterohemin-peptide conjugates by specific multi-site N-methylation, Amino Acids,
[2] Zhao Z;Wang D;Wang M,et al, Proximal environment controlling the reactivity between inorganic sulfide and heme-peptide model, Rsc Advances,
[3] Zhao Z;Wang D;Wang M,et al, Proximal environment controlling the reactivity between inorganic sulfide and heme-peptide model, Rsc Advances,

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