Peroxidase activity of an antibody–ferric porphyrin complex

Kawamura-Konishi, Yasuko; Asano, Atuko; Yamazaki, Masaaki; Tashiro, Hiroyuki; Suzuki, Haruo

doi:10.1016/s1381-1177(97)00032-5

Cited by 32 publications

(33 citation statements)

References 32 publications

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“…These observations presumably reflect the fact that the amino acid substitutions all occur in the general region of the distal heme binding pocket and that the surface of the protein with which the substrate probably interacts is not changed greatly in any of the variants from that of the wild-type protein. Of interest, a recent analysis of the peroxidase activity of an antibody-heme complex resulted primarily from improved interaction with the substrate (increased k 3 ) with little change in reactivity with peroxide (49) Molecular Design Considerations. The present study establishes the feasibility of enhancing the peroxidase activity of myoglobin by in vitro evolution.…”

Section: Discussionmentioning

confidence: 99%

In vitro evolution of horse heart myoglobin to increase peroxidase activity

Wan

Twitchett

Eltis

et al. 1998

Proc. Natl. Acad. Sci. U.S.A.

105

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Random mutagenesis and screening for enzymatic activity has been used to engineer horse heart myoglobin to enhance its intrinsic peroxidase activity. A chemically synthesized gene encoding horse heart myoglobin was subjected to successive cycles of PCR random mutagenesis. The mutated myoglobin gene was expressed in Escherichia coli LE392, and the variants were screened for peroxidase activity with a plate assay.

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Section: Discussionmentioning

confidence: 99%

In vitro evolution of horse heart myoglobin to increase peroxidase activity

Wan

Twitchett

Eltis

et al. 1998

Proc. Natl. Acad. Sci. U.S.A.

105

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“…Antibodies have been elicited against mesocarboxyaryl substituted- [52,57,62,65e68,70,72,73], N-substituted [55,56,61,63,64,68,74], tin- [56,58] or palladium-porphyrins [59,60]. Several antibodies raised against N-substituted porphyrins [55,61,68] and mesocarboxyphenyl-substituted porphyrins [62,65] have shown, in the presence of their iron-porphyrin cofactor, a significant peroxidase activity.…”

Section: Comparison Of the Kinetic Parameters For The Peroxidase Reacmentioning

confidence: 99%

“…Several antibodies raised against N-substituted porphyrins [55,61,68] and mesocarboxyphenyl-substituted porphyrins [62,65] have shown, in the presence of their iron-porphyrin cofactor, a significant peroxidase activity.…”

Section: Comparison Of the Kinetic Parameters For The Peroxidase Reacmentioning

confidence: 99%

“…The same N-methylmesoporphyrin IX hapten was also used by two other groups, [61,68] which, respectively, got two monoclonal antibodies 2B4 and 9A5. When associated with the Fe(III)-MPIX cofactor, those two antibodies were found to have a peroxidase activity: the 9A5eFe(III)-MPIX complex was found to be able to catalyze the oxidation of pyrogallol by H 2 O 2 [61] and the 2B4eFe(III)-MPIX catalyzed that of o-dianisidine and ABTS, but neither that of pyrogallol nor that of hydroquinone by H 2 O 2 [68].…”

Section: Comparison Of the Kinetic Parameters For The Peroxidase Reacmentioning

confidence: 99%

“…The kinetic parameters for the oxidation of various co-substrates by H 2 O 2 , catalyzed by Fe-porphyrine antibody complexes or by the corresponding free Fe(III)-porphyrins are compared in Table 1 with those reported for horseradish peroxidase [68,82,83].…”

Section: Comparison Of the Kinetic Parameters For The Peroxidase Reacmentioning

confidence: 99%

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This review covers recent advances in metalloprotein design, with focus on different approaches to the design. Impressive progress has been made in designing metal‐binding sites in peptides, de novo designed proteins, and native protein scaffolds. The approach can be rational or combinatorial. Under rational design, redesigning an existing metal‐binding site to a new site with dramatically different structure and function complements well the design of new metal‐binding sites by revealing the role of specific residues responsible for a particular structural or functional feature of the metal‐binding site of interest. To create a new metal‐binding site, several approaches have been used, including design based on structural homology, by inspection, using automated computer search algorithms, or combination of the above approaches. In addition, modular approach by transplanting a conserved structural unit from one protein into another has also been shown to be effective. Design through combinatorial and evolution methods has also been successful as it requires little prior knowledge of the protein structure. Finally, introducing unnatural amino acids or nonnative metal ions/prosthetic groups to expand the repertoires of metalloproteins have been demonstrated. Successful examples of each of the approaches are given; advantages and disadvantages of the approaches are discussed; the outlook for future research is also presented.

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Peroxidase activity of an antibody–ferric porphyrin complex

Cited by 32 publications

References 32 publications

In vitro evolution of horse heart myoglobin to increase peroxidase activity

In vitro evolution of horse heart myoglobin to increase peroxidase activity

New biocatalysts mimicking oxidative hemoproteins: Hemoabzymes

Metalloprotein Design & Engineering

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