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

Mark B van Eldijk; Iris van Leeuwen; Victor A Mikhailov; Lotte Neijenhuis; Harry R Harhangi; Jan C M van Hest; Mike S M Jetten; Huub J M Op den Camp; Carol V Robinson; Jasmin Mecinović

doi:10.1039/c3cc43219j

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

Chem Commun (Camb). 2013 Sep 14;49(71):7770-2. doi: 10.1039/c3cc43219j.

Authors

Mark B van Eldijk¹, Iris van Leeuwen, Victor A Mikhailov, Lotte Neijenhuis, Harry R Harhangi, Jan C M van Hest, Mike S M Jetten, Huub J M Op den Camp, Carol V Robinson, Jasmin Mecinović

Affiliation

¹ Institute for Molecules and Materials, Radboud University Nijmegen, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands.

PMID: 23771150
DOI: 10.1039/c3cc43219j

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Acidianus / enzymology
Anthracenes / chemistry
Anthracenes / metabolism*
Archaeal Proteins / chemistry
Archaeal Proteins / metabolism
Carbon Disulfide / chemistry
Carbon Disulfide / metabolism
Hydrolases / chemistry
Hydrolases / metabolism*
Light
Protein Structure, Quaternary
Scattering, Radiation

Substances

Anthracenes
Archaeal Proteins
catenane
Hydrolases
Carbon Disulfide