Enzymes can build bridges between carbon-containing molecules by forming carbon–carbon (C–C) bonds—the links that create a molecule’s carbon skeleton. In biocatalysis, these reactions can join smaller building blocks into more complex products, sometimes with useful control over stereochemistry. The title is best understood here as a guide to biocatalytic C–C bond formation, the subject of Schmidt, Eger and Kroutil’s 2016 perspective, rather than as a claim that one enzyme can make every kind of molecular connection.
Why C–C bond formation matters
Many organic molecules differ not only in their functional groups but in how their carbon atoms are connected. Forming a new C–C bond changes that underlying framework, making bond formation a central operation in organic synthesis. Enzymes offer a way to carry out some of these couplings under selective, biologically mediated conditions, and the resulting products can contain several useful functional groups.
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The 2016 perspective, Building Bridges: Biocatalytic C–C-Bond Formation toward Multifunctional Products, surveys enzyme-catalyzed transformations demonstrated as applicable to organic synthesis. A broader 2020 review considers the development of the field and highlights a key trade-off: enzymes can offer high selectivity, but the range of available biocatalytic C–C bond-forming reactions remains limited.
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The 2016 perspective covers several enzyme groups and reaction types. These are not interchangeable catalysts: substrate acceptance and the product formed depend on the particular enzyme and reaction.
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| Enzyme group or catalyst type | Context in the 2016 perspective |
|---|---|
| Aldolases | Catalyze aldol additions, including stereoselective carbon–carbon bond formation. |
| Thiamine-diphosphate (ThDP)-dependent carboligases | Included among the biocatalytic C–C bond-forming approaches surveyed. |
| Pictet–Spenglerases | Included among the enzyme classes discussed for carbon–carbon bond formation. |
| Oxidases | Included among the enzyme classes discussed in the perspective. |
| Prenyltransferases | Included among the enzyme classes discussed for C–C bond-forming transformations. |
| Squalene/hopene cyclases | Included among the enzyme classes discussed for building carbon frameworks. |
| Engineered hemoproteins | Discussed in connection with cyclopropanation. |
The review reports examples that produce α-hydroxy ketones, aminoalcohols, diols, 1,4-diketones, functionalized aromatic or heteroaromatic products, saturated carbocycles and cyclopropanes. These are product classes represented in the reviewed examples—not a promise that every enzyme in a listed group accepts arbitrary substrates.
How an aldolase builds a molecular bridge
An aldol addition joins a donor molecule to an acceptor, commonly an aldehyde, by making a new C–C bond. Aldolases catalyze reversible, stereoselective versions of this reaction. One useful case couples an α-hydroxy carbonyl donor with an aldehyde acceptor to form a 1,2-diol. The coupling step can establish two chiral centers, so the enzyme’s selectivity matters to the structure of the resulting product.
Schmidt, Eger and Kroutil describe aldol addition as “the most common C–C-bond-forming reaction in organic chemistry,” while qualifying that statement as “most likely.” The point is that aldol chemistry is a familiar and useful example of how an enzyme can join molecular fragments while influencing their three-dimensional arrangement.
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How to assess whether an enzyme route fits
A reaction family name alone does not establish that a route will work for a particular molecule. Compare candidate routes against the actual substrate and desired product:
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- Transformation and product: Identify which bond-forming reaction occurs and whether it gives the needed functional groups or ring system.
- Substrate fit: Check whether reported examples include the substrate class you want. The 2016 perspective stresses the need for suitable enzyme variants for specific reactions.
- Selectivity: Establish whether the reaction supports the needed chemical, site or regio, and stereochemical outcome; do not infer a desired stereoisomer merely from the enzyme family.
- Catalyst status: Distinguish native enzyme activity from an engineered catalyst or a strategy that modifies the substrate.
- Evidence of use: Separate reactions demonstrated as applicable to organic synthesis from suggestions that an enzyme might prove useful in future work.
What the “bridge-building” metaphor does—and does not—mean
“Building bridges” describes the creation of new C–C connections, not a universal enzymatic toolkit. The reviews describe a set of distinct transformations with different substrates, selectivities and products. Enzyme choice is therefore reaction-specific, and the field’s limited range of established C–C bond-forming transformations remains an important constraint even where selectivity is an advantage.
The 2016 perspective is a dated survey of examples and should not be read as a complete inventory of every enzyme, engineered variant or reaction reported since its publication. The 2020 review provides later field context, but neither source supports a claim that a single catalyst can build any desired carbon framework.
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Sources
- Schmidt, N. G.; Eger, E.; Kroutil, W., “Building Bridges: Biocatalytic C–C-Bond Formation toward Multifunctional Products,” ACS Catalysis (2016), 6(7), 4286–4311, published online June 8, 2016: https://doi.org/10.1021/acscatal.6b012.
- Zetzsche, L. E.; Narayan, A. R. H., “Broadening the scope of biocatalytic C–C bond formation,” Nature Reviews Chemistry (2020), 4, 334–346, published June 3, 2020: https://doi.org/10.1038/s41570-020-0183-z.
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