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Merck

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

Chemical communications (Cambridge, England) (2013-06-19)
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
PMID23771150
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.

MATERIALS
Product Number
Brand
Product Description
40363
Supelco
Carbon disulfide solution, certified reference material, 5000 μg/mL in methanol
05-1560
Sigma-Aldrich
Carbon disulfide, CP
335266
Sigma-Aldrich
Carbon disulfide, anhydrous, ≥99%
270660
Sigma-Aldrich
Carbon disulfide, suitable for HPLC, ≥99.9%
676918
Sigma-Aldrich
Carbon disulfide, ACS reagent, ≥99.9%
180173
Sigma-Aldrich
Carbon disulfide, ACS reagent, ≥99.9%
342270
Sigma-Aldrich
Carbon disulfide, ReagentPlus®, low benzene, ≥99.9%
424641
Sigma-Aldrich
Carbon disulfide, ReagentPlus®, purified by redistillation, ≥99.9%
31627
Sigma-Aldrich
Carbon disulfide, suitable for IR spectroscopy, puriss. p.a., ACS reagent, reag. Ph. Eur., ≥99.9% (GC)