1.8.2.1	Iron	enzyme contains 3.17 mol of iron per mol of enzyme	394084	
1.8.2.1	Iron	enzyme contains nonheme iron	394081	
1.8.2.1	Iron	Mo-based and Fe-based voltametric responses from the enzyme in the absence of substrate	658970	
1.8.2.1	Mg2+	1 mM, 150% increase in activity	394084	
1.8.2.1	Mn2+	1 mM, 127% increase in activity	394084	
1.8.2.1	Mo	consists of a single molybdenum atom coordinated through the dithiolene group of a single molybdopterin molecule	667714	
1.8.2.1	Mo	does not play a rate defining role in the catalytic mechanism of SDH before turnover	691057	
1.8.2.1	Mo	Mo-PPT binding catalytic subunit (SorA) comprised of an SUOX fold and a dimerization domain	694023	
1.8.2.1	Mo4+	molybdenum enzyme. Sulfite oxidizing enzymes (regardless of origin) share a common active site comprising a dioxido-MoVI moiety chelated by a molybdopterin dithiolene ligand in addition to a cysteinyl S-donor. The equatorial oxido ligand is the one transferred to sulfite during its 2-electron O-atom transfer reaction	743146	
1.8.2.1	Molybdenum	-	667744, 722663