Structure and mechanism of copper, zinc superoxide dismutase

  title={Structure and mechanism of copper, zinc superoxide dismutase},
  author={John A. Tainer and Elizabeth D. Getzoff and Jane. S. Richardson and David C. Richardson},
Copper, zinc superoxide dismutase (SOD) catalyses the very rapid two-step dismutation of the toxic superoxide radical (O− 2) to molecular oxygen and hydrogen peroxide through the alternate reduction and oxidation of the active-site copper1. We report here that after refitting and further refinement of the previous 2 Å structure of SOD2, analysis of the new model and its calculated molecular surface shows an extensive surface topography of sequence-conserved residues stabilized by underlying… 
Mechanism and atomic structure of superoxide dismutase.
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Probing enzyme-substrate recognition and catalytic mechanism in Cu,Zn superoxide dismutase.
This remarkably high catalytic rate makes the enzyme a simple model system in which to study the role of electrostatic forces in molecular recognition and the evolution of an optimal active site for the recognition and chemical catalysis of the substrate by the enzyme.
Cu, Zn Superoxide dismutase: distorted active site binds substrate without significant energetic cost
Copper, Zinc superoxide dismutase (CuZnSOD) catalyzes the dismutation of the toxic superoxide radical into molecular oxygen and hydrogen peroxide. Dismutation is achieved by reduction and
Copper-Zinc Superoxide Dismutase: Mechanistic and Biological Studies
Copper-zinc superoxide dismutase (CuZnSOD) is one of a class of enzymes known to be excellent catalysts of the disproportionation of superoxide (2 O 2 - + 2 H+ → O2 + H2O2). An unusual aspect of the
Oxygen-dependent activation of Cu,Zn-superoxide dismutase-1.
The processes involved in Sod1 activation are reviewed with a focus on copper ion insertion and disulfide bond formation.
Contribution of human manganese superoxide dismutase tyrosine 34 to structure and catalysis.
Structural and catalytic roles of the highly conserved active-site residue Tyr34 are examined, based upon structure-function studies of MnSOD enzymes with mutations at this site, and an intermediate in catalysis is observed, which has not been reported previously.
On the coordination and oxidation states of the active-site copper ion in prokaryotic Cu,Zn superoxide dismutases.
The results are in line with previous studies on the eukaryotic Cu,Zn superoxide dismutases and suggest the conservation of an identical catalytic mechanism in both the prokaryotic and eUKaryotic enzymes.
The Active Site of Cu,Zn Superoxide Dismutase as Studied by EXAFS: The Binding of Chloride to the Reduced Enzyme
Bovine erithrocyte copper-zinc superoxide dismutase Cu(11)-Zn(11)SOD is a dimer made of two equivalent subunits each containing one copper and one zinc atom. X-ray diffraction study (1) on crystals


Superoxide dismutase, a study of the electronic properties of the copper and zinc by X-ray absorption spectroscopy.
Analysis of the x-ray absorption for copper and zinc in oxidized and reduced superoxide dismutase, as well as in various model compounds, suggests that the copper is not simply ligated to four imidazoles.
Competitive inhibition of Cu, Zn superoxide dismutase by monovalent anions.
Potentiometric titrations and oxidation-reduction potentials of manganese and copper-zinc superoxide dismutases.
Bovine erythrocyte superoxide dismutase exhibits anomalous behavior in the coulometric titration curves, which is indicative of two nonequivalent copper centers in the enzyme.
The involvement of the bridging imidazolate in the catalytic mechanism of action of bovine superoxide dismutase.
The pulse-radiolysis method has been used to study the catalytic mechanism of O2 leads to dismutation by the Co(II)-substituted bovine erythrocuprein (superoxide dismutase, EC Catalysis is
Some sulfhydryl properties and primary structure of human erythrocyte superoxide dismutase.
Human Cu-Zn superoxide dismutase prepared by different methods shows varying properties relevant to its sulfhydryl chemistry. A cysteine residue not found in the analogous bovine enzyme appears to be
Coupling between oxidation state and hydrogen bond conformation in heme proteins.
The conclusions are that the strength of this hydrogen bond in heme proteins is sensitive to both the oxidation state of the iron atom and to geometry changes on the order of those obtained from the x-ray coordinates.
Amino acid sequence of copper-zinc superoxide dismutase from horse liver.