Predicting the Biological Function of [FeFe]-hydrogenases in Bacteria using Genome Analysis

Sammanfattning

Hydrogenases are metalloenzymes that catalyze the reversible redox reaction of hydrogen. [FeFe]-hydrogenases are particularly efficient catalysts, which makes them interesting in the context of developing efficient biomimetic catalysts. In bacteria, [FeFe]-hydrogenases can be separated into four phylogenetic groups called A, B, C, and D. The biological role of [FeFe]-hydrogenases is not fully known, though group A is the most well understood group. The function of a protein can sometimes be deduced by studying the function of proteins that have genes on the same operon. The functionality of proteins can often be classified into COG categories. This project has used explorative data analysis to predict the structures of operons that have [FeFe]-hydrogenase genes on them and the function of the [FeFe]-hydrogenases based on the function of the proteins whose genes are predicted to be on the same operon. This has included identifying subgroups of group A, B, C, and D, and analysing how the operon structures and neighbouring genes differ between them. A deeper study of group D, whose predicted operons tended to contain the largest number of neighbouring genes, showed that the proteins that the neighbouring genes encoded often contain certain domains. DRTGG was the most well conserved domain for these proteins, but the purpose of the DRTGG domain is currently unknown.