In Germany, researchers at the Ruhr-Universität Bochum found that certain enzymes, such as the hydrogen-producing hydrogenases, are unstable in the presence of oxygen and have clarified this at the atomic level.
Using X-ray diffraction, they showed how certain iron atoms in the center of the enzyme change in the presence of oxygen, which gradually leads to the decay of the entire center.
The researchers stored several samples of the enzyme with oxygen for different lengths of time. Subsequently, they examined by X-ray structure analysis how the three-dimensional structure of the proteins had changed. “This method is very complex and complicated, but helped us to follow the destructive process at the atomic level,” says Julian Esselborn.
Incubation with oxygen changed only single atoms of the enzyme, namely certain iron atoms of the cofactor. This gradually led to the disintegration of the entire active center. By understanding which iron atoms are particularly affected, the researchers hope to be able to better protect biotechnologically interesting proteins against oxygen in the future.