Crystal structure of bovine Cu, Zn SOD to 1.7 Angstrom (3 of 3)

Conformational Variability of the Cu Site in One Subunit of Bovine Cuzn Superoxide Dismutase: The Importance of Mobility in the Glu119-Leu142 Loop Region for Catalytic Function.

ATSAVCVLSGDGPVQGTIHFEAKGDTVVVTGSITGLTEGDHGFHVHQFGDNTQGCTSAGPHFNPLSKKHGGPSDEERHVG
DLGNVTADSNGVAIVDIVDPLISLSGEYSIIGRTMVVHEKPDDLGRGGNEESTKTGNAGSRLACGVIGIAS

ATSAVCVLSGDGPVQGTIHFEASGDTVVVTGSITGLTEGDHGFHVHQFGDNTQGCTSAGPHFNPLSKKHGGPSDDERHVG
DLGNVTADKNGVAIVDIVDPLISLSGEYSIIGRTMVVHEKPDDLGRGGNEESTSTGNAGSRLACGVIGIAS

CRYSTAL STRUCTURE OF COPPER, ZINC SUPEROXIDE DISMUTASE

CRYSTAL STRUCTURE OF BOVINE SUPEROXIDE DISMUTASE CRYSTAL.

CRYSTAL STRUCTURE OF BOVINE SOD - 1 OF 3

CRYSTAL STRUCTURE OF BOVINE CU ZN SOD - (1 OF 3)

REDUCED BOVINE SUPEROXIDE DISMUTASE AT PH 5.0

REDUCED BOVINE SUPEROXIDE DISMUTASE AT PH 5.0 COMPLEXED WITH THIOCYANATE

REDUCED BOVINE SUPEROXIDE DISMUTASE AT PH 5.0 COMPLEXED WITH AZIDE

DESTROYS RADICALS TOXIC TO BIOLOGICAL SYSTEMS WHICH ARE NORMALLY
PRODUCED WITHIN THE CELLS
2 PEROXIDE RADICAL + 2 H(+) = O(2) + H(2)O(2).

OXIDOREDUCTASE, SOD, ENZYME, SUPEROXIDE, ASYMMETRY