2020/09/24 by Fedaa Ali, Shafaa W Medhat, Ali, Fedaa +4 · 1 citation
Biochemistry, Genetics and Molecular Biology · Energy · Physics and Astronomy · #Biological Physics (physics.bio-ph) #Electrocatalysts for Energy Conversion #FOS: Physical sciences #Metalloenzymes and iron-sulfur proteins #Photosynthetic Processes and Mechanisms #physics.bio-ph
paper · pdf · doi:10.48550/arxiv.2009.11681
arxiv created 2020/09/24 · openalex publication_date 2020/09/24 · arxiv updated 2020/09/25 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/28
Photosystem I is a light-driven electron transfer device. Available X-ray crystal structure from Thermosynechococcus elongatus, showed that electron transfer pathways consist of two nearly symmetric branches of cofactors converging at the first iron sulfur cluster FX, which is followed by two terminal iron sulfur clusters FA and FB. Experiments have shown that Fx has lower oxidation potential than FA and FB, which facilitate the electron transfer reaction. Here, we use Density Functional Theory and Multi-Conformer Continuum Electrostatics to explain the differences in the midpoint Em potentials of the Fx, FA and FB clusters. Our calculations show that Fx has the lowest oxidation potential compared to FA and FB due strong pair-wise electrostatic interactions with surrounding residues. These interactions are shown to dominated by the bridging sulfurs and cysteine ligands, which may be attributed to the shorter average bond distances between the oxidized Fe ion and ligating sulfurs for FX compared to FA and FB. Moreover, the electrostatic repulsion between the 4Fe-4S clusters and the positive potential of the backbone atoms is least for FX compared to both of FA and FB. These results agree with the experimental measurements from the redox titrations of low-temperature EPR signals and of room temperature recombination kinetics.