Protein-likeprotonexchangeina重点.PDFVIP

Protein-like proton exchange in a synthetic host cavity a,b a,b c a,b,1 a,b,1 William M. Hart-Cooper , Carmelo Sgarlata , Charles L. Perrin , F. Dean Toste , Robert G. Bergman , and Kenneth N. Raymonda,b,1 aChemical Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720; bDepartment of Chemistry, University of California, Berkeley, CA 94720; and cDepartment of Chemistry Biochemistry, University of California, San Diego, La Jolla, CA 92093 Edited by Ronald Breslow, Columbia University, New York, NY, and approved November 3, 2015 (received for review August 6, 2015) The mechanism of proton exchange in a metal–ligand enzyme active in polypeptides, preferentially stabilize the desired tetrahedral site mimic (compound 1) is described through amide hydrogen– supramolecular structure over other conformers (35). Com- deuterium exchange kinetics. The type and ratio of cationic guest pound 1 and related hosts have been shown to catalyze several to host in solution affect the rate of isotope exchange, suggesting important chemical reactions with sizable rate accelerations (up that the rate of exchange is driven by a host whose cavity is to 106) and unusual selectivity reminiscent of enzyme catalysis occupied by water. Rate constants for acid-, base-, and water- (34, 36–41). Unlike most enzymes, the reactions catalyzed by 1 mediated proton exchange vary by orders of magnitude depend- are functionally and mechanistically very diverse. Despite these ing on the guest, and differ by up to 200 million-fold relative to an differences, those reactions proceeding with the la