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Chem Commun (Camb) ; 49(71): 7770-2, 2013 Sep 14.
Article in English | MEDLINE | ID: mdl-23771150

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.


Subject(s)
Anthracenes/metabolism , Hydrolases/metabolism , Acidianus/enzymology , Anthracenes/chemistry , Archaeal Proteins/chemistry , Archaeal Proteins/metabolism , Carbon Disulfide/chemistry , Carbon Disulfide/metabolism , Hydrolases/chemistry , Light , Protein Structure, Quaternary , Scattering, Radiation
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