Nickel superoxide dismutase structure and mechanism.

@article{Barondeau2004NickelSD,
  title={Nickel superoxide dismutase structure and mechanism.},
  author={David P. Barondeau and Carey J Kassmann and Cami K Bruns and John A. Tainer and Elizabeth D. Getzoff},
  journal={Biochemistry},
  year={2004},
  volume={43 25},
  pages={
          8038-47
        }
}
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 interactions critical for metal binding and catalysis, and thus will likely be diagnostic of NiSODs… Expand
Nickel superoxide dismutase: structural and functional roles of His1 and its H-bonding network.
TLDR
The results indicate that the Glu17-His1 H-bond plays an important structural role in the proper folding of the "Ni-hook" motif that is a critical feature of the active site of nickel-dependent superoxide dismutases. Expand
Insight into the structure and mechanism of nickel-containing superoxide dismutase derived from peptide-based mimics.
  • J. Shearer
  • Chemistry, Medicine
  • Accounts of chemical research
  • 2014
TLDR
Using small NiN2S2 complexes and metallopeptide-based NiSOD mimics, it was shown that the unusual nitrogen donor atoms protect the cysteinates from oxidative damage by fine-tuning the electronic structure of the nickel center. Expand
Nickel superoxide dismutase: structural and functional roles of Cys2 and Cys6
TLDR
X-ray absorption spectroscopic studies of the Cys mutants revealed that the nickel active-site structure for each mutant resembles that of C2S/C6S-NiSOD and demonstrate that mutation of either Cys2 or Cys6 inhibits coordination of the remaining Cys residue. Expand
Cysteinate protonation and water hydrogen bonding at the active-site of a nickel superoxide dismutase metallopeptide-based mimic: implications for the mechanism of superoxide reduction.
TLDR
Results strongly suggest that maquettes derived from the primary sequence of NiSOD are mechanistically distinct from NiS OD itself despite the similarities in the structure and physical properties of the metalloenzyme vs the NiSod metallopeptide-based models. Expand
Dipeptide-based models of nickel superoxide dismutase: solvent effects highlight a critical role to Ni-S bonding and active site stabilization.
TLDR
Spectroscopic and electrochemical measurements suggest that 2-5 successfully simulate many of the electronic features of Ni-SOD(red) and aqueous studies reveal a dynamic behavior with regard to RS(-) lability and bridging interactions, suggesting a stabilizing role brought about by the protein architecture. Expand
pH Dependent Reversible Formation of a Binuclear Ni2 Metal-Center within a Peptide Scaffold
A disulfide-bridged peptide containing two Ni2+ binding sites based on the nickel superoxide dismutase protein, {Ni2(SODmds)} has been prepared. At physiological pH (7.4), it was found that the metalExpand
A Bioinspired NiII Superoxide Dismutase Catalyst Designed on an ATCUN-like Binding Motif.
TLDR
A bioinspired NiII complex built on an ATCUN-like binding motif modulated with one cysteine is reported, which demonstrates catalytic SOD activity in water and proposes that O2·- interacts first with the complex outer sphere through a H-bond with the peptide scaffold in a [NiIIO 2·-] species. Expand
Solution Structure of a Functional Biomimetic and Mechanistic Implications for Nickel Superoxide Dismutases
TLDR
The nickel complex of a synthetic nonapeptide (HCDLPCFVY‐NH2) is capable of catalytically disproportionating O2 and is thus a functional biomimetic for nickel superoxide dismutases and is reduced to a functional minimal motif of only six amino acids (ACAAPC‐ NH2). Expand
Embedding the Ni-SOD mimetic Ni-NCC within a polypeptide sequence alters the specificity of the reaction pathway.
TLDR
It is demonstrated that the chiral inversion chemistry does not occur when NCC is embedded in a longer polypeptide sequence, and the superoxide scavenging reactivity of the embedded Ni-NCC module is similar to that of the chirally inverted tripeptic complex, which suggests that the charge of the complex could affect the SOD activity as much as a change in the primary coordination sphere. Expand
New insight into the mode of action of nickel superoxide dismutase by investigating metallopeptide substrate models.
TLDR
The results are a clear indication in favor of the inner-sphere electron-transfer mechanism for the disproportionation of the O(2)(*-) ion, whereby the substrate is attached to the Ni atom in the active site of the NiSOD. Expand
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