Saltar al contenido
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
RESUMEN

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.

MATERIALES
Referencia del producto
Marca
Descripción del producto

Sigma-Aldrich
Disulfuro de carbono, ACS reagent, ≥99.9%
Sigma-Aldrich
Disulfuro de carbono, suitable for HPLC, ≥99.9%
Sigma-Aldrich
Disulfuro de carbono, ReagentPlus®, low benzene, ≥99.9%
Sigma-Aldrich
Disulfuro de carbono, ACS reagent, ≥99.9%
Sigma-Aldrich
Disulfuro de carbono, suitable for IR spectroscopy, puriss. p.a., ACS reagent, reag. Ph. Eur., ≥99.9% (GC)
Supelco
Carbon disulfide solution, certified reference material, 5000 μg/mL in methanol
Sigma-Aldrich
Disulfuro de carbono, anhydrous, ≥99%
Sigma-Aldrich
Disulfuro de carbono, ReagentPlus®, purified by redistillation, ≥99.9%
Sigma-Aldrich
Disulfuro de carbono, CP