NL repository
menu
검색
Library
Browse
Communities & Collections
By Date
Authors
Titles
Subject
My Repository
My Account
Receive email updates
Edit Profile
DSpace at EWHA
자연과학대학
화학·나노과학전공
Journal papers
View : 600 Download: 290
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 Fukuzumi
;
Kei Okubo
SCOPUS Author ID
Shunichi Fukuzumi
; Kei Okubo
Issue Date
2015
Journal Title
Chemical Science
ISSN
2041-6520
Citation
Chemical Science vol. 6, no. 7, pp. 4060 - 4065
Publisher
Royal Society of Chemistry
Indexed
SCI; SCIE; SCOPUS
Document Type
Article
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
Appears in Collections:
자연과학대학
>
화학·나노과학전공
>
Journal papers
Files in This Item:
001.pdf
(1.63 MB)
Download
Export
RIS (EndNote)
XLS (Excel)
XML
Show full item record
Find@EWHA
트윗하기
BROWSE
Communities & Collections
By Date
Authors
Titles
Subject