Active-site dynamics and large-scale domain motions of sulfite oxidase: a molecular dynamics study.


The physiologically vital enzyme sulfite oxidase employs rapid intramolecular electron transfer between a molybdenum ion in the C-terminal domain (the site of sulfite oxidation) and a heme moeity in the N-terminal domain to complete its catalytic cycle. Crystal structures of the enzyme show C- and N-terminal domain orientations that are not consistent with… (More)
DOI: 10.1021/jp908731f


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