Catenane versus ring: do both assemblies of CS2 hydrolase exhibit the same stability and catalytic activity?

Content Provider	Semantic Scholar
Author	Eldijk, Mark B. Van Pieters, Bas Mikhailov, Victor A. Robinson, Carol V. Hest, Jan Cornelis Maria Van Mecinović, Jasmin
Copyright Year	2014
Abstract	Catenane structures, in which two or more rings are mechanically interlocked, have historically occupied one of the central places in the field of supramolecular chemistry. In contrast to synthetic small-molecule catenanes, examples of naturally-occurring catenanes are scarce. Here, we report thermodynamic and enzymatic studies on CS2 hydrolase, which exists in solution as a mixture of unique hexadecameric catenane and octameric ring forms. A combination of field-flow fractionation coupled to multi-angle laser light scattering (FFF-MALLS) and native mass spectrometric analyses revealed that the catenane form is converted into the ring form at elevated temperatures, whereas the ring does not assemble into the catenane under the same conditions. Measurements of the enzyme kinetics for the conversion of CS2 into COS and H2S showed that the ring form of CS2 hydrolase possesses higher enzyme efficiency (per monomer) than the catenane form, whereas the catenane form is overall more active (per assembly).
Starting Page	2879
Ending Page	2884
Page Count	6
File Format	PDF HTM / HTML
DOI	10.1039/C4SC00059E
Volume Number	5
Alternate Webpage(s)	http://www.rsc.org/suppdata/sc/c4/c4sc00059e/c4sc00059e1.pdf
Alternate Webpage(s)	https://doi.org/10.1039/C4SC00059E
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article