Abstract by Parag Gajjar
Chemistry and Biochemistry
Structural characterization of radical SAM enzyme complexes
Radical SAM enzymes use an iron sulfur cluster and SAM to generate a radical that enables difficult reactions. Ribonucleotide reductase activating enzyme (RNR-AE) is responsible for the activation of ribonucleotide reductase. We are working on finding the structure of RNR-AE and RNR bound to RNR-AE by X-ray crystallography and cryo-EM. This will give structural information like the interaction site of both enzymes and the bound position of the iron sulfur cluster in RNR-AE. We are also working on another radical SAM enzyme complex involving hydrogenase maturases. Hydrogenase uses a special H-cluster to form or reduce hydrogen and surprisingly this cluster is formed by three different maturase enzymes called Hyd E, F and G. We don’t have much information about how they interact and form the H-cluster during the maturation process. We are using cryo-EM and Mass spectrometry to find the structure and interactions between the Hydrogenase maturases respectively and these data may be help full to solve maturation mystery.