Anion binding to bovine erythrocyte superoxide dismutase studied by x-ray absorption spectroscopy. A detailed structural analysis of the native enzyme and the azido and cyano derivatives using a multiple-scattering approach

1987 ◽  
Vol 109 (23) ◽  
pp. 7162-7170 ◽  
Author(s):  
Ninian J. Blackburn ◽  
Richard W. Strange ◽  
Loretta M. McFadden ◽  
S. Samar Hasnain
Keyword(s):  
Superoxide Dismutase ◽  
Structural Analysis ◽  
Multiple Scattering ◽  
Absorption Spectroscopy ◽  
Anion Binding ◽  
Bovine Erythrocyte ◽  
X Ray ◽  
Detailed Structural Analysis ◽  
Erythrocyte Superoxide Dismutase ◽  
X Ray Absorption

scholarly journals Direct structural information for the copper site of dopamine β-mono-oxygenase obtained by using extended X-ray-absorption fine structure

1984 ◽  
Vol 221 (2) ◽  
pp. 545-548 ◽  
Author(s):  
S S Hasnain ◽  
G P Diakun ◽  
P F Knowles ◽  
N Binsted ◽  
C D Garner ◽  
...  
Keyword(s):  
Aqueous Solution ◽  
Superoxide Dismutase ◽  
Fine Structure ◽  
Structural Information ◽  
Bovine Erythrocyte ◽  
X Ray ◽  
Absorption Fine ◽  
Copper Site ◽  
Erythrocyte Superoxide Dismutase ◽  
X Ray Absorption

Copper K-edge e.x.a.f.s (extended X-ray-absorption fine structure) was measured for dopamine beta-mono-oxygenase in aqueous solution. Comparison with the Cu K-edge e.x.a.f.s. of bovine erythrocyte superoxide dismutase shows a close resemblance. Detailed analysis of the e.x.a.f.s. indicates that the copper atom is bound to four imidazole groups at 0.201 nm with one or two oxygen atoms at 0.23 nm.

scholarly journals Photoinduced anisotropic distortion as the electron trapping site of tungsten trioxide by ultrafast W L1-edge X-ray absorption spectroscopy with full potential multiple scattering calculations

2020 ◽  
Vol 22 (5) ◽  
pp. 2615-2621 ◽  
Author(s):  
Akihiro Koide ◽  
Yohei Uemura ◽  
Daiki Kido ◽  
Yuki Wakisaka ◽  
Satoru Takakusagi ◽  
...  
Keyword(s):  
Multiple Scattering ◽  
Absorption Spectroscopy ◽  
Tungsten Trioxide ◽  
Structure Change ◽  
Trapping Site ◽  
Electron Trapping ◽  
Full Potential ◽  
Anisotropic Structure ◽  
X Ray ◽  
X Ray Absorption

Ultrafast XANES spectra and full-potential multiple scattering reveal the anisotropic structure change of photoexcited WO3.

scholarly journals Encapsulation of lead sulfide molecular clusters into solid matrixes. Structural analysis with x-ray absorption spectroscopy

1989 ◽  
Vol 28 (15) ◽  
pp. 2914-2919 ◽  
Author(s):  
Karin Moller ◽  
Thomas Bein ◽  
Norman Herron ◽  
Walter Mahler ◽  
Ying Wang
Keyword(s):  
Structural Analysis ◽  
Absorption Spectroscopy ◽  
Lead Sulfide ◽  
Molecular Clusters ◽  
X Ray ◽  
X Ray Absorption

Superoxide dismutase, a study of the electronic properties of the copper and zinc by x-ray absorption spectroscopy

Biochemistry ◽  
1978 ◽  
Vol 17 (10) ◽  
pp. 1842-1846 ◽  
Author(s):  
W. E. Blumberg ◽  
J. Peisach ◽  
P. Eisenberger ◽  
J. A. Fee
Keyword(s):  
Superoxide Dismutase ◽  
Electronic Properties ◽  
Absorption Spectroscopy ◽  
X Ray ◽  
Copper And Zinc ◽  
X Ray Absorption

X-ray Absorption Spectroscopy of Hemes and Hemeproteins in Solution: Multiple Scattering Analysis

2008 ◽  
Vol 47 (21) ◽  
pp. 9905-9918 ◽  
Author(s):  
Paola D’Angelo ◽  
Andrea Lapi ◽  
Valentina Migliorati ◽  
Alessandro Arcovito ◽  
Maurizio Benfatto ◽  
...  
Keyword(s):  
Multiple Scattering ◽  
Absorption Spectroscopy ◽  
X Ray ◽  
X Ray Absorption

scholarly journals An extended-X-ray-absorption-fine-structure study of bovine erythrocyte superoxide dismutase in aqueous solution. Direct evidence for three-co-ordinate Cu(I) in reduced enzyme

1984 ◽  
Vol 219 (3) ◽  
pp. 985-990 ◽  
Author(s):  
N J Blackburn ◽  
S S Hasnain ◽  
N Binsted ◽  
G P Diakun ◽  
C D Garner ◽  
...  
Keyword(s):  
Aqueous Solution ◽  
Superoxide Dismutase ◽  
Structure Study ◽  
Reduced Form ◽  
Edge Structure ◽  
X Ray ◽  
Absorption Fine ◽  
Copper Site ◽  
Erythrocyte Superoxide Dismutase ◽  
X Ray Absorption

Copper and zinc K-edge e.x.a.f.s. (extended X-ray-absorption fine structures) were measured for the metal sites of oxidized and reduced bovine superoxide dismutase in aqueous solution. Detailed analysis of the spectra indicates that the copper site of the enzyme changes on reduction and is most probably co-ordinated to three imidazole groups at a shorter distance Cu-N(alpha) = 0.194 nm (1.94 A) in the reduced form compared with a co-ordination of four imidazole groups at 0.199 nm (1.99 A) and an oxygen atom from solvent water at 0.224 nm (2.24 A) in the oxidized form. Examination of the edge, near-edge structure and e.x.a.f.s. of the zinc sites indicates that the stereochemical changes at copper that accompany reduction introduce minimal perturbation on the stereochemistry at zinc.

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