Literature DB >> 11133076

Design, synthesis and peroxidase-like activity of 3alpha-helix proteins covalently bound to heme.

I Obataya1, T Kotaki, S Sakamoto, A Ueno, H Mihara.   

Abstract

As a model of artificial peroxidase, de novo designed three-alpha-helix proteins, 3alpha-H9 and 3alpha-H12, covalently bound to Fe(III)-mesoporphyrin IX were synthesized and examined for a peroxidase-like activity. The activity was regulated according to the positions of His residues in the proteins, and the His residues played a role in an acid-base catalytic function.

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Year:  2000        PMID: 11133076     DOI: 10.1016/s0960-894x(00)00564-3

Source DB:  PubMed          Journal:  Bioorg Med Chem Lett        ISSN: 0960-894X            Impact factor:   2.823


  3 in total

1.  Modulation of function in a minimalist heme-binding membrane protein.

Authors:  Sandip Shinde; Jeanine M Cordova; Brian W Woodrum; Giovanna Ghirlanda
Journal:  J Biol Inorg Chem       Date:  2012-02-04       Impact factor: 3.358

2.  Controlling and fine tuning the physical properties of two identical metal coordination sites in de novo designed three stranded coiled coil peptides.

Authors:  Olga Iranzo; Saumen Chakraborty; Lars Hemmingsen; Vincent L Pecoraro
Journal:  J Am Chem Soc       Date:  2010-12-16       Impact factor: 15.419

3.  Hydrogen-bonded organic framework biomimetic entrapment allowing non-native biocatalytic activity in enzyme.

Authors:  Guosheng Chen; Linjing Tong; Siming Huang; Shuyao Huang; Fang Zhu; Gangfeng Ouyang
Journal:  Nat Commun       Date:  2022-08-16       Impact factor: 17.694

  3 in total

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