Lecture will be held in English

Hosted by

Zbyněk Prokop

About the lecture

Partners in Catalysis: Enzymes and Their Cofactors

To perform the vast array of chemical transformations required for life, enzymes often rely on the help of cofactors—molecular partners that expand the catalytic repertoire of enzymes beyond what amino acids alone can achieve. In fact, the majority of enzymes require a cofactor to function. These cofactors can range from simple metal ions, such as magnesium or iron, to a wide variety of complex organic molecules. Among the latter, flavin cofactors stand out as one of the most versatile and widely used cofactor type in nature.
Flavin-dependent enzymes (flavoenzymes) participate in an extraordinary range of biological processes, including light emission in bioluminescent organisms, magnetosensing in birds, electron transfer in respiration, halogenation reactions in natural product biosynthesis, and highly selective oxidation reactions. Over the past few decades, the study of these enzymes has revealed not only their impressive diversity but also their potential as biocatalysts for industrial applications. Advances in enzyme engineering have allowed researchers to fine-tune flavoenzymes, making them increasingly attractive for biotechnology.
In my research group, we focus on a fundamental question: how are flavins recognized and bound by their target apo proteins, and how do these interactions influence catalytic behaviour? By examining the molecular details of protein–cofactor binding, we aim to uncover how subtle changes in these interactions can dramatically shape enzyme reactivity. In this lecture, I will present some of our recent findings on covalent flavin attachment to proteins and discuss how this knowledge can be used to design new and more efficient biocatalytic systems.

Registration for lunch with the speaker /for Ph.D. students/

The sponsored lunch usually takes place in the Campus River restaurant. Please meet the speaker and other students at 12:45 at the reception desk at the main entrance (building B22, see the map below).