Research

Cryogenic Electron Microscopy

We use cryogenic electron microscopy (cryoEM), a powerful tool to study the structure and structural dynamics of macromolecules. By applying a specimen to a grid (i) then flash freezing and imaging in an electron microscope (ii) we can obtain transmission images (iii). With computational analysis we can obtain the 3D structure of our proteins of interest (iv).

The Electron Transport Chain

A major focus of the Di Trani lab is to explore electron transport chain (ETC) complexes and supercomplexes through structural and biochemical analysis. Electron transport chains are responsible for establishing the proton motive force essential for ATP production in mitochondria and most bacteria. This proton motive force is created by the ETC through the coupling of electron transfer to the translocation of protons across the membrane. Intriguingly, ETC complexes can manifest as intricate multi-enzyme assemblies known as supercomplexes, providing a functional advantage for the entire chain.

Pseudomonas Aeruginosa

The initial interest of the group, is the ETC of the opportunistic pathogen, Pseudomonas aeruginosa. The ETC in this bacterium is intricately linked to its pathogenicity and its remarkable adaptability across various environments. Recent work towards this aim has led to the discovery of a supercomplex between the cytochrome bc1c4c5 complex and the cytochrome cbb3 complex. Significantly, both of these complexes play crucial roles in the bacterium's survival, and the existence of this supercomplex further underscores their collective importance.

The ETC of Pseudomonas aeruginosa. ETC enzymes are underlined, intermediate electron carriers and final electron acceptor reactions are represented with dashed and solid lines respectively.

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