Spectroscopic Characterization of YedY: The Role of Sulfur Coordination in a Mo(V) Sulfite Oxidase Family Enzyme Form

摘要

The pyranopterin molybdenum enzymes are commonly grouped into the sulfite oxidase, DMSO reductase, and xanthine oxidase families on the basis of the type of reactions they catalyze, their active-site structures, and the nature of the overall protein fold. Members of the sulfite oxidase (SO) enzyme family possess a common SUOX protein fold and include vertebrate and plant SO (PSO), the sulfite dehydrogenase from Starkeya novella (SDH), assimilatory nitrate reductases, and bacterial YedY. High-resolution crystal structures, coupled with the results of resonance Raman and electron paramagnetic resonance (EPR) studies, are consistent with the active-site structures shown in Figure 1.