Abstract：
:The molybdenum-containing enzyme sulfite oxidase catalyzes the conversion of sulfite to sulfate, the terminal step in the oxidative degradation of cysteine and methionine. Deficiency of this enzyme in humans usually leads to major neurological abnormalities and early death. The crystal structure of chicken liver sulfite oxidase at 1.9 A resolution reveals that each monomer of the dimeric enzyme consists of three domains. At the active site, the Mo is penta-coordinated by three sulfur ligands, one oxo group, and one water/hydroxo. A sulfate molecule adjacent to the Mo identifies the substrate binding pocket. Four variants associated with sulfite oxidase deficiency have been identified: two mutations are near the sulfate binding site, while the other mutations occur within the domain mediating dimerization.
journal_name
Celljournal_title
Cellauthors
Kisker C,Schindelin H,Pacheco A,Wehbi WA,Garrett RM,Rajagopalan KV,Enemark JH,Rees DCdoi
10.1016/s0092-8674(00)80488-2subject
Has Abstractpub_date
1997-12-26 00:00:00pages
973-83issue
7eissn
0092-8674issn
1097-4172pii
S0092-8674(00)80488-2journal_volume
91pub_type
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