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Outbyte PC Repair FREERepair Windows errors before they cause bigger problemsFix Now →Outbyte Driver Updater FREEFix the driver behind crashes, sound loss and screen glitchesFind Drivers →In a 2016 study, researchers engineered a heme protein to make carbon–silicon bonds by inserting a carbene into a silicon–hydrogen bond. The enzyme, derived from cytochrome c of Rhodothermus marinus, worked in laboratory experiments and living cells; the authors reported more than 15-fold higher turnover than the synthetic catalysts they compared it with.
How the enzyme makes a carbon–silicon bond
The reaction joins carbon and silicon through a process called carbene insertion. A carbene—a reactive carbon species—enters a silicon–hydrogen (Si–H) bond, replacing the hydrogen and forming a carbon–silicon (C–Si) bond. The study demonstrated that a heme protein could catalyze this transformation, a reaction that had been carried out using synthetic catalysts.
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The starting point was cytochrome c from Rhodothermus marinus, or Rma cyt c. Its known natural role was electron transfer, not carbon–silicon bond formation. The researchers tested heme proteins and found that Rma cyt c catalyzed the new reaction with 97% enantiomeric excess (ee), a measure of preference for one of two mirror-image product forms. That initial activity gave the team a platform to improve through directed evolution.
What directed evolution changed
Directed evolution uses successive rounds of protein variation and selection to improve a chosen function. In this case, the team altered Rma cyt c to improve its ability to catalyze the carbene-insertion reaction. The paper reports a triple mutant, V75T/M100D/M103E, that produced twenty silicon-containing products across the tested substrate set. Most were obtained cleanly as single enantiomers.
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The reported substrate range and selectivity show what the evolved enzyme could do under the study’s experimental conditions; they do not establish performance for every possible substrate or process.
What the study’s performance comparison means
Kan, Lewis, Chen, and Arnold reported that the evolved enzyme achieved more than 15-fold higher turnover than the state-of-the-art synthetic catalysts they used as a benchmark. This is the authors’ comparison in their 2016 paper, not a current, independently verified ranking of enzyme and synthetic catalysts. The available publication record does not establish an independent replication or a present-day commercial comparison.
The study also reports catalytic activity in living cells as well as in vitro. Those results are evidence that the reaction was possible in both experimental settings; they do not demonstrate broad industrial deployment or a commercially available process.
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The paper by S. B. Jennifer Kan, Russell D. Lewis, Kai Chen, and Frances H. Arnold appeared in Science on November 25, 2016, volume 354, issue 6315, pages 1048–1051. Its DOI is 10.1126/science.aah6219. Read the full article on PubMed Central or see its PubMed record.
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A Caltech repository record notes that a provisional patent application was filed based on the results. That record does not establish whether a patent was later issued, whether the work was commercialized, or whether a product is currently available.
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