Extended X-Ray Absorption Fine Structure Evidence for a Single Metal Binding Domain inXenopus laevisNucleotide Excision Repair Protein XPA

1999 ◽  
Vol 254 (1) ◽  
pp. 109-113 ◽  
Author(s):  
Garry W. Buchko ◽  
Lilia M. Iakoucheva ◽  
Michael A. Kennedy ◽  
Eric J. Ackerman ◽  
Nancy J. Hess
Keyword(s):  
Fine Structure ◽  
Metal Binding ◽  
Excision Repair ◽  
Binding Domain ◽  
X Ray ◽  
Absorption Fine ◽  
Repair Protein ◽  
Metal Binding Domain ◽  
X Ray Absorption

scholarly journals Human nucleotide excision repair protein XPA: Extended X-ray absorption fine-structure evidence for a metal-binding domain

1998 ◽  
Vol 7 (9) ◽  
pp. 1970-1975 ◽  
Author(s):  
Nancy J. Hess ◽  
Garry W. Buchko ◽  
Shuisong Ni ◽  
Brian D. Thrall ◽  
Michael A. Kennedy ◽  
...  
Keyword(s):  
Fine Structure ◽  
Nucleotide Excision Repair ◽  
Metal Binding ◽  
Excision Repair ◽  
X Ray ◽  
Repair Protein ◽  
Metal Binding Domain ◽  
Nucleotide Excision ◽  
X Ray Absorption ◽  
Nucleotide Excision Repair Protein

Neptunium(IV) complexation by humic substances studied by X-ray absorption fine structure spectroscopy

2005 ◽  
Vol 93 (4) ◽  
Author(s):  
K. Schmeide ◽  
T. Reich ◽  
S. Sachs ◽  
V. Brendler ◽  
K. H. Heise ◽  
...  
Keyword(s):  
Fine Structure ◽  
Metal Binding ◽  
Cation Exchange Resin ◽  
Fulvic Acids ◽  
Coordination Environment ◽  
X Ray ◽  
Xafs Spectroscopy ◽  
Absorption Fine ◽  
Carboxylic Groups ◽  
X Ray Absorption

SummaryWe studied the coordination environment of neptunium(IV) in complexes with various natural and synthetic humic and fulvic acids at pH 1 by X-ray absorption fine structure (XAFS) spectroscopy. The results were compared to those obtained for the interaction of neptunium(IV) with Bio-Rex70, a cation exchange resin having solely carboxylic groups as metal binding functional groups. In both neptunium humate complexes and neptunium Bio-Rex70 sorbates, Np

scholarly journals An extended-X-ray-absorption-fine-structure study of freeze-dried and solution ovotransferrin. Evidence for water co-ordination at the metal-binding sites

1987 ◽  
Vol 247 (2) ◽  
pp. 369-375 ◽  
Author(s):  
S S Hasnain ◽  
R W Evans ◽  
R C Garratt ◽  
P F Lindley
Keyword(s):  
Fine Structure ◽  
Metal Binding ◽  
Binding Sites ◽  
Structure Study ◽  
Humid Atmosphere ◽  
Edge Structure ◽  
X Ray ◽  
Absorption Fine ◽  
Freeze Dried ◽  
X Ray Absorption

Our previous extended-X-ray-absorption-fine-structure (e.x.a.f.s.) study has shown that the probable iron environment in chicken ovotransferrin involves two low-Z ligands (consistent with phenolate linkages) at 0.185(1) nm and four low-Z ligands at 0.204(1) nm [Garratt, Evans, Hasnain & Lindley (1986) Biochem. J. 233, 479-484]. Herein we provide additional information from the e.x.a.f.s. and near-edge structure suggestive of a decrease in the co-ordination number of ovotransferrin-bound iron upon freeze-drying. These effects are reversible, and exposure of the freeze-dried material to a humid atmosphere results in reversion to the solution spectra. Progressive rehydration was monitored by using e.p.r. spectroscopy and was confirmed by recording the high-resolution X-ray-absorption near-edge structure (x.a.n.e.s.). The results suggest the presence of a labile water molecule at the iron-binding sites of ovotransferrin in solution.

Structure of magnetic thin films and nanostructures studied by extended X-ray absorption fine structure

2000 ◽  
Vol 454-456 ◽  
pp. 723-728 ◽  
Author(s):  
H. Magnan ◽  
P. Le Fèvre ◽  
A. Midoir ◽  
D. Chandesris ◽  
H. Jaffrès ◽  
...  
Keyword(s):  
Thin Films ◽  
Fine Structure ◽  
Magnetic Thin Films ◽  
X Ray ◽  
Absorption Fine ◽  
X Ray Absorption
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