We are a young but feareless team that aim to combine computational modeling with experimental validation to understand and design new biocatalytic processes.
To do so, we have established collaborations with experimental and computational groups around the world from who we are learning every day.

Our research involves the application of computational methods for the study and design of new biochemical processes mainly related to (metallo)enzymatic catalysis.


“Through the lens of a computational microscope”

See: Adrian Romero-Rivera, Marc Garcia-Borràs, Sílvia Osuna, “Computational tools for the evaluation of laboratory-engineered biocatalysts“, Chem. Commun., vol.53, iss.2, p.284-297, (2017) . DOI: 10.1039/C6CC06055B (Open Access)


Our approach for enzyme design and development of new biocatalysts:

Enzymes are highly efficient biocatalysts, biodegradable, operate under biological conditions, and can offer kcat/kuncat accelerations of several orders of magnitude. However, only few processes have a natural enzyme to accelerate the corresponding chemical reactions. Consequently, the design of new specific enzymes for catalyzing non-natural reactions is highly attractive. Among other strategies, this can be achieved by taking advantage of the intrinsic catalytic promiscuity that natural enzymes exhibit and by introducing specific amino acid changes (i.e. mutations) into their sequences. Catalytic promiscuity refers to the ability of an enzyme to catalyze, in addition to its native function, reactions involving different substrates and that proceed via different transition states and different reaction pathways.

Enzymatic reactive intermediates are species involved in biocatalytic cycles that are not so stable and exhibit short lifetimes. These species are sometimes found to be the source of enzyme catalytic promiscuity, since different potential reaction pathways can diverge from these generated species. Consequently, controlling the behavior of such reactive species could provide a new route to access to new non-natural biocatalytic functions.

In this project new computational protocols to study and characterize reactive intermediates formed over the course of enzyme catalytic pathways will be developed. The new protocol will rely on different multiscale computational approaches that will be combined to account for different factors that interplay key roles on the formation and stabilization of enzymatic reactive intermediates.

In addition to that, experimental work in the molecular biology lab together with structural chemical characterization of the product outcomes of the biocatalytic transformations will be carried out to validate the computational predictions and provide further guidance for computational modelling.

Finally, the knowledge acquired will be used to computationally design and engineer new enzyme variants to access to new-to-nature reactions, in a more rational and efficient manner.


Other research lines of the team involve the study of:

  • Study and design of supramolecular nanocapsules for encapsulating fullerene compounds and its selective functionalization
  • Supramolecular interactions and formation of Host-Guest complexes
  • Chemical reactivity and Structure of (endohedral) fullerene compounds
  • Development and application of new computational methods for the evaluation of electronic and vibrational Nonlinear Optical properties (NLOp)