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In 2016, researchers reported the first enzyme they had engineered to forge carbon–silicon bonds. By evolving cytochrome c from the bacterium Rhodothermus marinus, they created a catalyst that inserts a carbon-based carbene into a silicon–hydrogen bond. The result was a new enzyme-catalyzed reaction—not evidence of a commercially deployed process.
What the enzyme does
The reaction makes a carbon–silicon (C–Si) bond by inserting a carbene into a silicon–hydrogen (Si–H) bond. In the 2016 study, the researchers screened heme proteins and found that cytochrome c from Rhodothermus marinus (Rma cyt c) could catalyze this chemistry. The protein’s known native role was electron transfer; the bond-forming reaction was a new catalytic function.
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The initial Rma cyt c reaction produced the desired chiral product with 97% enantiomeric excess (ee), a measure of how strongly a reaction favors one mirror-image form over the other. That result gave the team a starting point for directed evolution: repeated cycles of genetic modification and testing to select enzyme variants with improved properties. The study’s full text describes the experiments.
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Repair Windows errors before they cause bigger problemsFix Now →Scan for outdated or missing drivers - takes under a minuteDriver Scan →How directed evolution improved the catalyst
The researchers modified the cytochrome c and selected variants that performed the new reaction more effectively. One evolved variant, V75T/M100D/M103E, was reported to form twenty silicon-containing products across the study’s substrate scope. Most were obtained cleanly as single enantiomers, according to the authors. These findings apply to the substrates and experimental conditions they tested; they do not establish performance across every possible Si–H compound.
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The study also reported activity in living cells, as well as in vitro. That demonstrates the reaction was possible in both experimental settings used by the team, not that the enzyme was ready for manufacturing or broadly deployed in industry.
How it compared with synthetic catalysts
The authors reported that directed evolution gave the enzyme more than 15-fold higher turnover than the state-of-the-art synthetic catalysts they used as their benchmark. Turnover measures how many product molecules a catalyst forms relative to the amount of catalyst. This is the authors’ comparison in their 2016 paper, not a current, independently verified comparison with all synthetic catalysts.
The result mattered because it showed that an enzyme could catalyze a reaction that had been associated with synthetic chemistry, while also offering high selectivity in the tested reactions. It should be understood as a research result under the paper’s conditions, rather than a general claim that enzymes outperform synthetic catalysts or a report of industrial-scale production.
What the 2016 result does—and does not—establish
- Established in the paper: Rma cytochrome c catalyzed carbene insertion into Si–H bonds; directed evolution produced an improved variant; the team reported twenty silicon-containing products, high selectivity for most of them, and activity in vitro and in vivo.
- Not established by those results: broad industrial deployment, current commercial availability, a present-day performance advantage over the full range of synthetic catalysts, or independent replication.
The Caltech institutional record says a provisional patent application was filed based on the results. That record does not establish that a patent was later issued, that the work was commercialized, or that an enzyme product is available. Caltech’s repository record includes the filing note.
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Paper and authors
The study, “Enzymatic construction of carbon–silicon bonds,” was published by S. B. Jennifer Kan, Russell D. Lewis, Kai Chen, and Frances H. Arnold in Science on November 25, 2016 (volume 354, issue 6315, pages 1048–1051; DOI 10.1126/science.aah6219). PubMed’s record provides the publication details and abstract.
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