Environmental Chemistry at BESSY II: Radicals in waterways

How do radicals form in aqueous solutions when exposed to UV light? This question is important for health research and environmental protection, for example with regard to the overfertilisation of water bodies by intensive agriculture. A team at BESSY II has now developed a new method of investigating hydroxyl radicals in solution. By using a clever trick, the scientists gained surprising insights into the reaction pathway.

Hydroxyl radicals (OH·) are found everywhere, from the troposphere to the cells of the human body. There, they cause oxidative stress and accelerate the ageing process. They are also increasingly present in rivers and lakes, where they are formed by the photolysis of nitrogen oxides that have entered the water from over-fertilised soils. When UV radiation from sunlight strikes nitrogen oxides, hydroxyl radicals and a range of other radicals are generated. The chemistry of these radicals is extremely difficult to characterise accurately, as they react very quickly

A team led by Professor Alexander Föhlisch of the HZB has investigated the chemistry of hydroxyl radicals formed from nitrogen oxides in water using X-ray absorption spectroscopy at the BESSY II X-ray source.

Read more on the HZB website

Image: How the radical scavenger TEMPO traps a hydroxyl radical OH·. The proton of the hydroxyl radical reacts with TEMPO first. Colour coding: grey for C (carbon), white for H (hydrogen), red for O (oxygen) and blue for N (nitrogen)

Credit: © HZB

Taking candid shots of radical proteins

Scientists capture how radical electrons influence protein structure before they have time to react

Some enzymes in the body carry radicals, chemical groups with highly reactive unpaired electrons, to catalyse biochemical reactions, but it has proven challenging to study the structure of these enzymes with the radicals intact. The X-ray crystallography techniques conventionally used to study protein structure introduce ‘X-ray damage’ that would neutralise radicals and alter the protein structure. To study how radicals influence proteins, researchers turned to a ribonucleotide reductase enzyme subunit called R2 that uses a radical to synthesise DNA bases. The team previously used X-ray crystallography at beamline I24 and small angle X-ray scattering at beamline B21 of the Diamond Light Source to solve the structure of this enzyme without safeguarding the radical. In the recent study, they harnessed X-ray free electron laser (XFEL) serial femtosecond crystallography at the Linac Coherent Light Source in collaboration with Diamond’s XFEL Hub to zero in on the radical. With XFEL, they used X-rays to rapidly capture the structure of the protein within femtoseconds — 1015 times quicker than a second and too quick for X-rays to neutralise the radical or distort protein structure. By comparing the enzyme with and without the radical, they revealed that the presence of the unpaired electron greatly influences the structure of the enzyme’s active site. Their research will allow them to explore the workings of this and related enzymes in finer detail and holds promise for designing drugs that target radical enzymes in cancer cells and infectious microbes.

Read more on the Diamond website

Image credit: Martin Högbom