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S. B. Jennifer Kan, Russell D. Lewis, Kai Chen | Science | (2016)
Key Takeaways
Plain English Takeaway
Scientists changed a natural protein so it could help living cells make new types of silicon-based chemicals, something nature never did before.
Study Aim
The study set out to create an enzyme (a protein that speeds up chemical reactions) that can form bonds between carbon and silicon atoms. The authors wanted to show that it is possible to use directed evolution (a method for improving proteins by making and selecting mutations) to give living systems the ability to make organosilicon compounds, which are not found in nature.
Simply put: The researchers wanted to make a protein that lets living things build new silicon-containing chemicals.
Study Design
The researchers tested whether heme proteins (proteins containing an iron-based molecule called heme) could help join carbon and silicon atoms together. They started with cytochrome c from the bacterium Rhodothermus marinus and used directed evolution, introducing mutations to improve its ability to form carbon–silicon bonds. They screened different protein variants in bacteria and measured how well each one made organosilicon products, both in test tubes and inside living cells.
Simply put: The team changed a bacterial protein step by step and checked if it could help make new silicon-based chemicals.
Findings
The study demonstrates that the evolved cytochrome c enzyme can efficiently and selectively form carbon–silicon bonds, producing a wide range of organosilicon compounds as single mirror-image forms (enantiomers). The best mutant worked over 15 times better than the best chemical catalysts and could do the reaction inside living E. coli cells. The enzyme tolerated many different starting materials and worked under mild, environmentally friendly conditions. This work shows that proteins can be engineered to create new types of chemical bonds not found in nature, opening up new possibilities for making useful silicon-based molecules.
Simply put: The improved protein made many new silicon-containing chemicals quickly and cleanly, even inside living bacteria.
Abstract
Enzymes that catalyze carbon-silicon bond formation are unknown in nature, despite the natural abundance of both elements. Such enzymes would expand the catalytic repertoire of biology, enabling living systems to access chemical space previously only open to synthetic chemistry. We have discovered that heme proteins catalyze the formation of organosilicon compounds under physiological conditions via carbene insertion into silicon-hydrogen bonds. The reaction proceeds both in vitro and in vivo, accommodating a broad range of substrates with high chemo- and enantioselectivity. Using directed evolution, we enhanced the catalytic function of cytochrome c from Rhodothermus marinus to achieve more than 15-fold higher turnover than state-of-the-art synthetic catalysts. This carbon-silicon bond-forming biocatalyst offers an environmentally friendly and highly efficient route to producing enantiopure organosilicon molecules.
Referenced In
StarTalk Show Notes
24 days ago
Created: May 5, 2026