Totally microperoxidase synthetic-11

Junichi Tanabe, Koji Nakano, Ryutaro Hirata, Toshiki Himeno, Ryoichi Ishimatsu, Toshihiko Imato, Hirotaka Okabe, Naoki Matsuda

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Abstract

A totally synthetic microperoxidase-11 (MP-11) is reported. Accordingly, the undecapeptide (VQKCAQCHTVE) was synthesized by solid-phase peptide synthesis followed by the thiol-ene click reaction with haemin for reconstitution. High-speed atomic force microscopy measurement conducted in water confirmed the protein reconstitution by visualizing the morphological differences as animated molecular images. The synthetic MP-11 showed a considerable magnitude of catalytic activity (27%) against the natural MP-11 in the oxidation of 3,3',5,5'-tetramethylbenzidine by hydrogen peroxide, whereas it showed very low (2.7%) activity of a synthetic variant with a point mutation (VQKCAQCMTVE, H8M). Slab waveguide spectroscopic measurements revealed that the ferrous/ferric redox reaction occurred by the direct electron transfer with specific spectral changes. Indeed, if hydrogen peroxide existed in the solution phase, the peroxidase-modified electrode showed catalytic current–voltage behaviour regardless of whether it was prepared using natural MP-11 or the synthetic MP-11. If a substrate recycling reaction was assumed, computer simulation well reproduced the experimental curves to give a global set of electrocatalytic reaction parameters. In any of the experiments, the synthetic MP-11 and natural MP-11 gave almost identical results. Our approach will be a convenient means of preparing MP-11, as well as its mutants, that does not rely on nature.

Original languageEnglish
Article number172311
JournalRoyal Society Open Science
Volume5
Issue number5
DOIs
Publication statusPublished - May 2018

All Science Journal Classification (ASJC) codes

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    Tanabe, J., Nakano, K., Hirata, R., Himeno, T., Ishimatsu, R., Imato, T., Okabe, H., & Matsuda, N. (2018). Totally microperoxidase synthetic-11. Royal Society Open Science, 5(5), [172311]. https://doi.org/10.1098/rsos.172311