Serial femtosecond crystallography approaches to understanding catalysis in iron enzymes

Enzymes with iron-containing active sites play crucial roles in catalysing a myriad of oxidative reactions essential to aerobic life. Defining the three-dimensional structures of iron enzymes in resting, oxy-bound intermediate and substrate-bound states is particularly challenging, not least because of the extreme susceptibility of the Fe(III) and Fe(IV) redox states to radiationinduced chemistry caused by intense X-ray or electron beams. The availability of novel sources such as X-ray free electron lasers has enabled structures that are effectively free of the effects of radiation-induced chemistry and allows time-resolved structures to be determined. Important to both applications is the ability to obtain in crystallo spectroscopic data to identify the redox state of the iron in any particular structure or timepoint.

Automated summary

Enzymes with iron-containing active sites are crucial for aerobic organisms, but their structural studies are challenging due to radiation-induced chemistry. Novel light source technologies have overcome this issue and allow for time-resolved structural analysis.