Lysozyme-catalyzed formation of a conjugated polyacetylene

D. L. Morris; A. P. Zampino; A. A. Taraboletti; L. P. Shriver; T. C. Leeper; C. J. Ziegler

doi:10.1039/c7py01250k

Lysozyme-catalyzed formation of a conjugated polyacetylene

D. L. Morris
, A. P. Zampino
, A. A. Taraboletti
, L. P. Shriver
, T. C. Leeper
, C. J. Ziegler

Department of Chemistry

Research output: Contribution to journal › Article › peer-review

5 Scopus citations

Abstract

Hen egg white lysozyme catalyzes the polymerization of 2-ethynylpyridine in water as the singular protein catalyst. Inhibition and NMR spectroscopy studies support the hypothesis that polymerization takes place in the active site cleft of the protein. This discovery marks the first time a metal-free hydrolase has been observed activating the formation for a conjugated polymer.

Original language	English
Pages (from-to)	6344-6348
Number of pages	5
Journal	Polymer Chemistry
Volume	8
Issue number	41
DOIs	https://doi.org/10.1039/c7py01250k
State	Published - Nov 7 2017

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title = "Lysozyme-catalyzed formation of a conjugated polyacetylene",

abstract = "Hen egg white lysozyme catalyzes the polymerization of 2-ethynylpyridine in water as the singular protein catalyst. Inhibition and NMR spectroscopy studies support the hypothesis that polymerization takes place in the active site cleft of the protein. This discovery marks the first time a metal-free hydrolase has been observed activating the formation for a conjugated polymer.",

author = "Morris, \{D. L.\} and Zampino, \{A. P.\} and Taraboletti, \{A. A.\} and Shriver, \{L. P.\} and Leeper, \{T. C.\} and Ziegler, \{C. J.\}",

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doi = "10.1039/c7py01250k",

language = "English",

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T1 - Lysozyme-catalyzed formation of a conjugated polyacetylene

AU - Morris, D. L.

AU - Zampino, A. P.

AU - Taraboletti, A. A.

AU - Shriver, L. P.

AU - Leeper, T. C.

AU - Ziegler, C. J.

PY - 2017/11/7

Y1 - 2017/11/7

N2 - Hen egg white lysozyme catalyzes the polymerization of 2-ethynylpyridine in water as the singular protein catalyst. Inhibition and NMR spectroscopy studies support the hypothesis that polymerization takes place in the active site cleft of the protein. This discovery marks the first time a metal-free hydrolase has been observed activating the formation for a conjugated polymer.

AB - Hen egg white lysozyme catalyzes the polymerization of 2-ethynylpyridine in water as the singular protein catalyst. Inhibition and NMR spectroscopy studies support the hypothesis that polymerization takes place in the active site cleft of the protein. This discovery marks the first time a metal-free hydrolase has been observed activating the formation for a conjugated polymer.

UR - https://www.scopus.com/pages/publications/85032433773

U2 - 10.1039/c7py01250k

DO - 10.1039/c7py01250k

M3 - Article

AN - SCOPUS:85032433773

SN - 1759-9954

VL - 8

SP - 6344

EP - 6348

JO - Polymer Chemistry

JF - Polymer Chemistry

IS - 41

ER -

Lysozyme-catalyzed formation of a conjugated polyacetylene

Abstract

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