arXiv subjects

Gergely Katona

Publications and source records attributed to Gergely Katona.

3 recordsLinked to original sources

arXiv2026

Hamiltonian model for energy condensation in classical systems: Relevance to proteins

Recent experimental evidence for collective protein vibrations in the terahertz (THz) domain indicates that energy in biomolecular systems can self-organize in an orderly manner, as anticipated by Fröhlich's theory of condensates within a quantum framework. As a first step to bridge THz experiments with theory, we study the Hamiltonian dynamics of a classical network of coupled normal modes representing Fröhlich-type systems. Our results demonstrate that biologically relevant condensates can emerge at room temperature under appropriate nonlinear coupling schemes. The condensation mechanism remains robust also when the original Fröhlich resonance conditions are relaxed.

physics.bio-ph↗

arXiv2024

Unveiling Long-Range Forces in Light Harvesting Proteins: Pivotal Roles of Temperature and Light

Electrodynamic interactions between biomolecules are of potential biological interest for signaling warranting investigation of their activation through various mechanisms in living systems. Here, using as model system a light harvesting protein within the phycobilisome antenna system of red algae, we proved that not only light exposure but also thermal energy alone can trigger attractive electrodynamic interactions up to hundreds of nanometer. The latter are sustained by low frequency collective modes and while the second mode appears only upon illumination, the fundamental one can be activated by temperature alone. Activation of such collective modes and ED interactions might influence conformational rearrangements and energy transport within the phycobilisome antenna system. This is a paradigm-shift that underscores the immense potential of biological systems in exploiting different forms of input energy to achieve optimal energy transfer.

physics.bio-ph↗

arXiv2014

Raman-assisted crystallography reveals end-on peroxide intermediates in a nonheme iron enzyme

Iron-peroxide intermediates are central in the reaction cycle of many iron-containing biomolecules. We trapped iron(III)-(hydro)peroxo species in crystals of superoxide reductase (SOR), a nonheme mononuclear iron enzyme that scavenges superoxide radicals. X-ray diffraction data at 1.95 angstrom resolution and Raman spectra recorded in crystallo revealed iron-(hydro)peroxo intermediates with the (hydro)peroxo group bound end-on. The dynamic SOR active site promotes the formation of transient hydrogen bond networks, which presumably assist the cleavage of the iron-oxygen bond in order to release the reaction product, hydrogen peroxide.

q-bio.BM↗