Issue 71, 2013
From the journal:

Chemical Communications

Evidence that the catenane form of CS2 hydrolase is not an artefact†

Mark B. van Eldijk,a   Iris van Leeuwen,ab   Victor A. Mikhailov,c   Lotte Neijenhuis,ab   Harry R. Harhangi,b   Jan C. M. van Hest,a   Mike S. M. Jetten,b   Huub J. M. Op den Camp,b   Carol V. Robinsonc  and  Jasmin Mecinović*a  

* Corresponding authors

a Institute for Molecules and Materials, Radboud University Nijmegen, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands
E-mail: j.mecinovic@science.ru.nl
Fax: +31 24 3653393
Tel: +31 24 3652381

b Department of Microbiology, Radboud University Nijmegen, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands

c Chemistry Research Laboratory, University of Oxford, Mansfield Road, OX1 3TA Oxford, UK

Abstract

CS2 hydrolase, a zinc-dependent enzyme that converts carbon disulfide to carbon dioxide and hydrogen sulfide, exists as a mixture of octameric ring and hexadecameric catenane forms in solution. A combination of size exclusion chromatography, multi-angle laser light scattering, and mass spectrometric analyses revealed that the unusual catenane structure is not an artefact, but a naturally occurring structure.

Graphical abstract: Evidence that the catenane form of CS2 hydrolase is not an artefact

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Article information

DOI
https://doi.org/10.1039/C3CC43219J
Article type
Communication
Submitted
01 May 2013
Accepted
31 May 2013
First published
03 Jun 2013
This article is Open Access
Creative Commons BY license

Chem. Commun., 2013,49, 7770-7772

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Evidence that the catenane form of CS2 hydrolase is not an artefact

M. B. van Eldijk, I. van Leeuwen, V. A. Mikhailov, L. Neijenhuis, H. R. Harhangi, J. C. M. van Hest, M. S. M. Jetten, H. J. M. Op den Camp, C. V. Robinson and J. Mecinović, Chem. Commun., 2013, 49, 7770 DOI: 10.1039/C3CC43219J

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