Spatial model of anaerobic methacrylate reductase system

The high structural similarities of methacrylate reductase (Mrd) and cytochrome c (Mcc) (of the methacrylate redox system) from Geobacter sulfurreducens AM-1 with the soluble fumarate reductases of Shewanella were revealed by the computer modelling. Mrd repeates two C-terminal catalytic domains of these fumarate reductases - FAD-binding and clamp domains - both sequence and structure. Mcc is similar to small N-terminal heme-containing domain of the periplasmic fumarate reductases of Shewanella. The assumption of spatial interaction of the conservative amino acids from Mrd, involved in catalysis and substrate binding, is discussed.