| Literature DB >> 29711800 |
Yan Zhou1, Katsuhiko Shimizu1, Jennifer N Cha2, Galen D Stucky3, Daniel E Morse4.
Abstract
A protein isolated from a biosilica (shown schematically) catalyzes alkoxysilane polycondensation at neutral pH values and low temperatures. Replacement of either of two specific side chain functionalities (Ser-26 and His-165) significantly diminishes catalysis, supporting a reaction mechanism analogous to that of a well-known enzyme that is highly homologous to the silica protein. These results may be useful in the development of synthetic catalysts for environmentally benign synthesis of polysiloxanes. © 1999 WILEY-VCH Verlag GmbH, Weinheim, Fed. Rep. of Germany.Entities:
Keywords: Enzyme catalysis; Polymerizations; Polysiloxanes; Proteins; Silica
Year: 1999 PMID: 29711800 DOI: 10.1002/(SICI)1521-3773(19990315)38:6<779::AID-ANIE779>3.0.CO;2-#
Source DB: PubMed Journal: Angew Chem Int Ed Engl ISSN: 1433-7851 Impact factor: 15.336