Directed Evolution Will Design Enzymes That Don't Exist in Nature — And Solve Carbon Capture in the Process
Frances Arnold won the Nobel Prize for directed evolution in 2018. Since then, the field has been quietly doing something extraordinary: creating enzymes for reactions that biology never invented.
Natural evolution samples a tiny fraction of sequence space — constrained by historical contingency, metabolic context, and the glacial pace of random mutation. Directed evolution removes all three constraints. You can screen 10^8 variants per round, select for any function you want, and iterate in weeks rather than millennia.
The frontier: enzymes that catalyze reactions with no biological precedent. Carbene and nitrene transfer (Kan et al., 2016, Science). Silicon-carbon bond formation (Kan et al., 2016, Nature). And most provocatively — CO2 fixation at rates 100x faster than RuBisCO, the sluggish enzyme that all photosynthetic life depends on.
RuBisCO is evolution's greatest bottleneck. It's slow (3 reactions/second vs. 1000+ for typical enzymes), error-prone (30% oxygenation side reactions), and ubiquitous. If directed evolution produces a superior carbon fixation enzyme, synthetic organisms equipped with it could capture CO2 at transformative rates.
Testable prediction: Within 5 years, a directed-evolution-designed CO2 fixation enzyme will achieve >10x RuBisCO's catalytic rate with <5% oxygenation side reaction, and engineered cyanobacteria expressing it will show >5x the carbon fixation rate of wild-type.
This is synthetic biology's Manhattan Project. And it's happening in labs right now.
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