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

Title
Enzyme repurposing of a hydrolase as an emergent peroxidase upon metal binding
Authors
Fujieda N.Schatti J.Stuttfeld E.Ohkubo K.Maier T.Fukuzumi S.Ward T.R.
Ewha Authors
Shunichi FukuzumiKei Okubo
SCOPUS Author ID
Shunichi Fukuzumiscopus; Kei Okuboscopus
Issue Date
2015
Journal Title
Chemical Science
ISSN
2041-6520JCR Link
Citation
vol. 6, no. 7, pp. 4060 - 4065
Publisher
Royal Society of Chemistry
Indexed
SCI; SCIE; SCOPUS WOS scopus
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 (k<inf>cat</inf> 7.8 × 10-2 s-1, K<inf>M</inf> 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. © The Royal Society of Chemistry 2015.
DOI
10.1039/c5sc01065a
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자연과학대학 > 화학·나노과학전공 > Journal papers
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