Processive enzyme mimic: Kinetics and thermodynamics of the threading and sliding process.
The kinetics and thermodynamics of the threading 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.
Coumans
Ruud G E
RG
Institute for Molecules and Materials, Radboud University Nijmegen, Toernooiveld 1, 6525ED Nijmegen, The Netherlands.
Elemans
Johannes A A W
JA
Nolte
Roeland J M
RJ
Rowan
Alan E
AE
D040761:Biomimetic Materials / Q000737:chemistry* / Q000378:metabolism*; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D008345:Manganese / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D008968:Molecular Conformation; D008970:Molecular Weight; D010084:Oxidation-Reduction; D011166:Porphyrins / Q000737:chemistry / Q000378:metabolism; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013379:Substrate Specificity; D013816:Thermodynamics
D011166:Porphyrins; D011506:Proteins; D008345:Manganese