title: Evidence that the catenane form of CS2 hydrolase is not an artefact.
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.
authors.affiliation: Institute for Molecules and Materials, Radboud University Nijmegen, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands.
authors.forename: Mark B
authors.initials: MB
authors.lastname: van Eldijk
authors.forename: Iris
authors.initials: I
authors.lastname: van Leeuwen
authors.forename: Victor A
authors.initials: VA
authors.lastname: Mikhailov
authors.forename: Lotte
authors.initials: L
authors.lastname: Neijenhuis
authors.forename: Harry R
authors.initials: HR
authors.lastname: Harhangi
authors.forename: Jan C M
authors.initials: JC
authors.lastname: van Hest
authors.forename: Mike S M
authors.initials: MS
authors.lastname: Jetten
authors.forename: Huub J M
authors.initials: HJ
authors.lastname: Op den Camp
authors.forename: Carol V
authors.initials: CV
authors.lastname: Robinson
authors.forename: Jasmin
authors.initials: J
authors.lastname: Mecinović
mesh_terms: D041541:Acidianus / Q000201:enzymology; D000873:Anthracenes / Q000737:chemistry / Q000378:metabolism*; D019843:Archaeal Proteins / Q000737:chemistry / Q000378:metabolism; D002246:Carbon Disulfide / Q000737:chemistry / Q000378:metabolism; D006867:Hydrolases / Q000737:chemistry / Q000378:metabolism*; D008027:Light; D020836:Protein Structure, Quaternary; D012542:Scattering, Radiation
chemical_list: D000873:Anthracenes; D019843:Archaeal Proteins; C467767:catenane; D006867:Hydrolases; D002246:Carbon Disulfide