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Royal Society of Chemistry, Chemical Communications, 71(49), p. 7770

DOI: 10.1039/c3cc43219j

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

Journal article published in 2013 by M. B. Eldijk, Mark B. van Eldijk, Iris van Leeuwen, I. van Leeuwen, Victor A. Mikhailov, Lotte Neijenhuis, R. H. Harhangi, Harry R. Harhangi, Jan C. M. van Hest, J. C. M. van Hest, Mike S. M. Jetten, H. J. M. op den Camp, Huub J. M. Op den Camp ORCID, Carol V. Robinson, Jasmin Mecinovic
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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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.