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

Fujieda, Nobutaka and Schätti, Jonas and Stuttfeld, Edward and Ohkubo, Kei and Maier, Timm and Fukuzumi, Shunichi and Ward, Thomas R.. (2015) Enzyme repurposing of a hydrolase as an emergent peroxidase upon metal binding. Chemical Science, 6 (7). pp. 4060-4065.

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Official URL: http://edoc.unibas.ch/dok/A6390817

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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 (kcat7.8 × 10−2 s−1, KM 1.1 × 10−5 M). Both X-ray crystallographic and EPR data of the copper-loaded enzyme Cu·6-PGLacreveal a bis-histidine coordination site, located within a shallow binding pocket capable of accommodating the o-dianisidine substrate.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Maier)
05 Faculty of Science > Departement Chemie
05 Faculty of Science > Departement Chemie > Chemie > Bioanorganische Chemie (Ward)
UniBasel Contributors:Schätti, Jonas and Stuttfeld, Edward and Maier, Timm and Ward, Thomas R. R.
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Royal Society of Chemistry
ISSN:2041-6520
e-ISSN:2041-6539
Note:Publication type according to Uni Basel Research Database: Journal article
Language:English
Identification Number:
Last Modified:01 Feb 2017 12:44
Deposited On:07 Aug 2015 12:06

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