Structure ofBacillus subtilissuperoxide dismutase

Nickel superoxide dismutase structure and mechanism.

The 1.30 A resolution crystal structure of nickel superoxide dismutase (NiSOD) identifies a novel SOD fold, assembly, and Ni active site. NiSOD is a hexameric assembly of right-handed 4-helix bundles of up-down-up-down topology with N-terminal hooks chelating the active site Ni ions. This newly identified nine-residue Ni-hook structural motif (His-Cys-X-X-Pro-Cys-Gly-X-Tyr) provides almost all ...

Subunit structure of human superoxide dismutase.

A subunit structure for human superoxide dismutase has been demonstrated by sedimentation equilibrium, agarose gel filtration, and sodium dodecyl sulfate polyacrylamide gel electrophoretic studies. This protein appears to be composed of 2 subunits, not linked by covalent bonds, each with a molecular weight about 16,000. Dissociation of the subunits is facilitated by alkylation of the two sulfhy...

Sequence of the N-Terminal Half ofBacillus amyloliquefaciens a-Amylase

Bacillus amyloliquefaciens a-amylase (1,4-a-D-glucan glucanohydrolase. EC 3.2.1.1), which is commercially supplied as 'Bacillus subtilis a-amylase' does not cross-react immunologically with B. subtilis a-amylase. This enzyme (from B. amyloliquefaciens) was cleaved by treatment with CNBr into seven fragments. Peptide A was selected for sequence determination. It is the longest one, containing 18...

Superoxide dismutase Superoxide dismutase

A structure-based mechanism for copper-zinc superoxide dismutase.

A reaction cycle is proposed for the mechanism of copper-zinc superoxide dismutase (CuZnSOD) that involves inner sphere electron transfer from superoxide to Cu(II) in one portion of the cycle and outer sphere electron transfer from Cu(I) to superoxide in the other portion of the cycle. This mechanism is based on three yeast CuZnSOD structures determined by X-ray crystallography together with ma...