Probing Variable Amine/Amide Ligation in NiIIN2S2 Complexes Using Sulfur K-Edge and Nickel L-Edge X-ray Absorption Spectroscopies: Implications for the Active Site of Nickel Superoxide Dismutase

Journal Article · Tue Jan 01 04:00:00 EST 2008 · Inorganic Chemistry

DOI:https://doi.org/10.1021/ic7019878· OSTI ID:959862

Shearer, J; Dehestani, A; Abanda, F

Nickel superoxide dismutase (NiSOD) is a recently discovered metalloenzyme that catalyzes the disproportionation of O2* into O2 and H2O2. In its reduced state, the mononuclear NiII ion is ligated by two cis-cysteinate sulfurs, an amine nitrogen (from the protein N-terminus), and an amide nitrogen (from the peptide backbone). Unlike many small molecule and metallopeptide-based NiN2S2 complexes, S-based oxygenation is not observed in NiSOD. Herein we explore the spectroscopic properties of a series of three NiIIN2S2 complexes (bisamine-ligated (bmmp-dmed)NiII, amine/amide-ligated (NiII(BEAAM)), and bisamide-ligated (NiII(emi))2) with varying amine/amide ligation to determine the origin of the dioxygen stability of NiSOD. Ni L-edge X-ray absorption spectroscopy (XAS) demonstrates that there is a progression in ligand-field strength with (bmmp-dmed)NiII having the weakest ligand field and (NiII(emi)2) having the strongest ligand field. Furthermore, these Ni L-edge XAS studies also show that all three complexes are highly covalent with (NiII(BEEAM)) having the highest degree of metal-ligand covalency of the three compounds studied. S K-edge XAS also shows a high degree of NiS covalency in all three complexes. The electronic structures of the three complexes were probed using both hybrid-DFT and multiconfigurational SORCI calculations. These calculations demonstrate that the nucleophilic Ni(3d)/S()* HOMO of these NiN2S2 complexes progressively decreases in energy as the amide-nitrogens are replaced with amine nitrogens. This decrease in energy of the HOMO deactivates the Ni-center toward O2 reactivity. Thus, the NiS bond is protected from S-based oxygenation explaining the enhanced stability of the NiSOD active-site toward oxygenation by dioxygen.

• Research Organization: Brookhaven National Laboratory (BNL) National Synchrotron Light Source
• Sponsoring Organization: Doe - Office Of Science
• DOE Contract Number: AC02-98CH10886
• OSTI ID: 959862
• Report Number(s): BNL--82848-2009-JA
• Journal Information: Inorganic Chemistry, Journal Name: Inorganic Chemistry Journal Issue: 7 Vol. 47; ISSN 0020-1669; ISSN INOCAJ
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
99 GENERAL AND MISCELLANEOUS
ABSORPTION
ABSORPTION SPECTROSCOPY
AMIDES
AMINES
COVALENCE
ELECTRONIC STRUCTURE
NICKEL
NITROGEN
ORIGIN
OXIDATION
PEPTIDES
PROTEINS
STABILITY
SULFUR
SUPEROXIDE DISMUTASE
national synchrotron light source