Processive enzyme mimic: Kinetics and thermodynamics of the threading and sliding process

被引：52

作者：

Coumans, Ruud G. E. ^{[1
]}

Elemans, Johannes A. A. W. ^{[1
]}

Nolte, Roeland J. M. ^{[1
]}

Rowan, Alan E. ^{[1
]}

机构：

[1] Radboud Univ Nijmegen, Inst Mol & Mat, NL-6525 ED Nijmegen, Netherlands

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2006年 / 103卷 / 52期

关键词：

biomimetic; physical organic; rotaxanes; supramolecular chemistry;

D O I：

10.1073/pnas.0603036103

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The kinetics and thermodynamics of the treading and dethreading process of polymers through the cavity of a synthetic toroidal host is investigated by studying its complexation with a series of end-functionalized polymers of different lengths containing an end group that is selectively recognized by the host. The system is designed in such a way that complexation is only observed if the host has traveled all of the way across the complete polymer. Detailed kinetic investigations using fluorescence spectroscopy have revealed that the barrier for this process is length dependent and most likely related to the stretching of the polymer. Moreover, the results indicate that our previously reported processive enzyme mimic most likely operates by randomly sliding along its macromolecular substrate.

引用

页码：19647 / 19651

页数：5

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