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.