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

M.B. van Eldijk; Iris Van Leeuwen; Victor A. Mikhailov; Lotte Neijenhuis; Harry R. Harhangi; J.C.M. van Hest; M.S.M. Jetten; Huub J.M. op den Camp; Carol V. Robinson; Jasmin Mecinović

doi:10.1039/c3cc43219j

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

M.B. van Eldijk
, Iris Van Leeuwen
, Victor A. Mikhailov
, Lotte Neijenhuis
, Harry R. Harhangi
, J.C.M. van Hest
, M.S.M. Jetten
, Huub J.M. op den Camp
, Carol V. Robinson
, Jasmin Mecinović

Research output: Contribution to journal › Article › Academic › peer-review

25 Citations (Scopus)

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.

Original language	English
Pages (from-to)	7770-7772
Number of pages	3
Journal	Chemical Communications, ChemComm
Volume	49
Issue number	71
DOIs	https://doi.org/10.1039/c3cc43219j
Publication status	Published - 14 Sept 2013
Externally published	Yes

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10.1039/c3cc43219j

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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.",

author = "\{van Eldijk\}, M.B. and \{Van Leeuwen\}, Iris and Mikhailov, \{Victor A.\} and Lotte Neijenhuis and Harhangi, \{Harry R.\} and \{van Hest\}, J.C.M. and M.S.M. Jetten and \{op den Camp\}, \{Huub J.M.\} and Robinson, \{Carol V.\} and Jasmin Mecinovi{\'c}",

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doi = "10.1039/c3cc43219j",

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T1 - Evidence that the catenane form of CS2 hydrolase is not an artefact

AU - van Eldijk, M.B.

AU - Van Leeuwen, Iris

AU - Mikhailov, Victor A.

AU - Neijenhuis, Lotte

AU - Harhangi, Harry R.

AU - van Hest, J.C.M.

AU - Jetten, M.S.M.

AU - op den Camp, Huub J.M.

AU - Robinson, Carol V.

AU - Mecinović, Jasmin

PY - 2013/9/14

Y1 - 2013/9/14

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/84881407231

U2 - 10.1039/c3cc43219j

DO - 10.1039/c3cc43219j

M3 - Article

C2 - 23771150

AN - SCOPUS:84881407231

SN - 1359-7345

VL - 49

SP - 7770

EP - 7772

JO - Chemical Communications, ChemComm

JF - Chemical Communications, ChemComm

IS - 71

ER -

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

Abstract

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