Document Detail

Evidence that the catenane form of CS2 hydrolase is not an artefact.
MedLine Citation:
PMID:  23771150     Owner:  NLM     Status:  MEDLINE    
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.
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
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Chemical communications (Cambridge, England)     Volume:  49     ISSN:  1364-548X     ISO Abbreviation:  Chem. Commun. (Camb.)     Publication Date:  2013 Sep 
Date Detail:
Created Date:  2013-08-09     Completed Date:  2014-02-18     Revised Date:  2014-02-20    
Medline Journal Info:
Nlm Unique ID:  9610838     Medline TA:  Chem Commun (Camb)     Country:  England    
Other Details:
Languages:  eng     Pagination:  7770-2     Citation Subset:  IM    
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MeSH Terms
Acidianus / enzymology
Anthracenes / chemistry,  metabolism*
Archaeal Proteins / chemistry,  metabolism
Carbon Disulfide / chemistry,  metabolism
Hydrolases / chemistry,  metabolism*
Protein Structure, Quaternary
Scattering, Radiation
Grant Support
G1000819//Medical Research Council
Reg. No./Substance:
0/Anthracenes; 0/Archaeal Proteins; 0/catenane; EC 3.-/Hydrolases; S54S8B99E8/Carbon Disulfide

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