Enzyme repurposing of a hydrolase as an emergent peroxidase upon metal binding

Nobutaka Fujieda, Jonas Schätti, Edward Stuttfeld, Kei Ohkubo, Timm Maier, Shunichi Fukuzumi, Thomas R. Ward

Research output: Contribution to journalArticlepeer-review

23 Scopus citations

Abstract

As an alternative to Darwinian evolution relying on catalytic promiscuity, a protein may acquire auxiliary function upon metal binding, thus providing it with a novel catalytic machinery. Here we show that addition of cupric ions to a 6-phosphogluconolactonase 6-PGLac bearing a putative metal binding site leads to the emergence of peroxidase activity (kcat 7.8 × 10-2 s-1, KM 1.1 × 10-5 M). Both X-ray crystallographic and EPR data of the copper-loaded enzyme Cu·6-PGLac reveal a bis-histidine coordination site, located within a shallow binding pocket capable of accommodating the o-dianisidine substrate.

Original languageEnglish
Pages (from-to)4060-4065
Number of pages6
JournalChemical Science
Volume6
Issue number7
DOIs
StatePublished - 1 Jul 2015

Bibliographical note

Publisher Copyright:
© The Royal Society of Chemistry 2015.

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