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.
Highlights
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
Well established synthetic pathways have facilitated the preparation of diverse sets of catenane architectures which have found an important place in material sciences as molecular switches, electronic devices and sensors.[1,2]
Only a few proteins have been observed to exist in catenane forms: (i) a bacteriophage HK97 capsid in which the catenane structure is maintained via a covalent isopeptide bond between Lys[169] and Asn[356,6,7] (ii) a thermophile Pyrobaculum aerophilum citrate synthase (PaCS) in which the disulfide formation leads to catenation,[8] (iii) a Cys168Ser variant of mitochondrial peroxiredoxin III,[9] (iv) RecR, an enzyme involved in the DNA repair,[10] and (v) E. coli Ia class of ribonucleotide reductase (RNR).[11]
Summary
COMMUNICATION Jasmin Mecinović et al Evidence that the catenane form of CS2 hydrolase is not an artefact 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.
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
