Document Detail


Formation of silicones mediated by the sponge enzyme silicatein-α.
MedLine Citation:
PMID:  20396816     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The sponge-restricted enzyme silicatein-α catalyzes in vivo silica formation from monomeric silicon compounds from sea water (i.e. silicic acid) and plays the pivotal role during synthesis of the siliceous sponge spicules. Recombinant silicatein-α, which was cloned from the demosponge Suberites domuncula (phylum Porifera), is shown to catalyze in vitro condensation of alkoxy silanes during a phase transfer reaction at neutral pH and ambient temperature to yield silicones like the straight-chained polydimethylsiloxane (PDMS). The reported condensation reaction is considered to be the first description of an enzymatically enhanced organometallic condensation reaction.
Authors:
Stephan E Wolf; Ute Schlossmacher; Anna Pietuch; Bernd Mathiasch; Heinz-C Schröder; Werner E G Müller; Wolfgang Tremel
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-04-15
Journal Detail:
Title:  Dalton transactions (Cambridge, England : 2003)     Volume:  39     ISSN:  1477-9234     ISO Abbreviation:  Dalton Trans     Publication Date:  2010 Oct 
Date Detail:
Created Date:  2010-09-29     Completed Date:  2011-01-18     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101176026     Medline TA:  Dalton Trans     Country:  England    
Other Details:
Languages:  eng     Pagination:  9245-9     Citation Subset:  IM    
Affiliation:
Institute for Inorganic Chemistry, Johannes Gutenberg-University, Duesbergweg 10-14, 55099, Mainz, Germany.
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MeSH Terms
Descriptor/Qualifier:
Animals
Biocatalysis
Cathepsins / genetics,  metabolism*
Dimethylpolysiloxanes / chemistry
Magnetic Resonance Spectroscopy
Porifera / enzymology*
Recombinant Proteins / genetics,  metabolism
Silanes / chemistry
Silicones / chemistry*
Chemical
Reg. No./Substance:
0/Dimethylpolysiloxanes; 0/Recombinant Proteins; 0/Silanes; 0/Silicones; 0/silicatein alpha; 63148-62-9/baysilon; EC 3.4.-/Cathepsins

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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