A theoretical study of the near-edge x-ray absorption spectra of some larger amino acids

1998 ◽  
Vol 109 (4) ◽  
pp. 1456-1464 ◽  
Author(s):  
Vincenzo Carravetta ◽  
Oleksandr Plashkevych ◽  
Hans Ågren
Keyword(s):  
Amino Acids ◽  
Absorption Spectra ◽  
Theoretical Study ◽  
X Ray ◽  
X Ray Absorption

scholarly journals Theoretical study of the X-ray absorption spectra of small formic acid clusters

2006 ◽  
Vol 419 (4-6) ◽  
pp. 501-505 ◽  
Author(s):  
Osamu Takahashi ◽  
Saiko Yamanouchi ◽  
Keisuke Yamamoto ◽  
Kiyohiko Tabayashi
Keyword(s):  
Formic Acid ◽  
Absorption Spectra ◽  
Theoretical Study ◽  
X Ray ◽  
X Ray Absorption

scholarly journals The iron ligand sphere geometry of mammalian 15-lipoxygenases

1998 ◽  
Vol 332 (1) ◽  
pp. 237-242 ◽  
Author(s):  
Ralf Jürgen KUBAN ◽  
Rainer WIESNER ◽  
Jörg RATHMAN ◽  
Gerrit VELDINK ◽  
Hans NOLTING ◽  
...  
Keyword(s):  
Amino Acids ◽  
Absorption Spectra ◽  
Ferrous Iron ◽  
Structural Model ◽  
Structural Information ◽  
Reference Compound ◽  
X Ray ◽  
Inhibitor Complex ◽  
Sphere Geometry ◽  
X Ray Absorption

We investigated the geometry of the iron ligand sphere of the native rabbit 15-lipoxygenase (15-LOX) by X-ray absorption spectroscopy using synchrotron radiation. The soybean LOX-1 was used as a reference compound because its iron ligand sphere is well characterized. For structural information the X-ray absorption spectra were evaluated using the Excurve Program (CCLRC Daresbury Laboratory, Warrington, U.K.). From the positions of the absorption edges and from the intensities of the 1s–3d pre-edge transition peaks a six-coordinate ferrous iron was concluded for the rabbit 15-LOX. Evaluation of the extended region of the absorption spectra suggested six nitrogen and/or oxygen atoms as direct iron ligands, and the following binding distances were determined (means±S.D.; estimated accuracy is ±0.001 nm for bond distances, on the basis of more than 22 X-ray absorption spectra): 0.213±0.001 nm, 0.213±0.001 nm, 0.236±0.001 nm, 0.293±0.001 nm, 0.189±0.001 nm and 0.242±0.001. Lyophilization of the LOX altered the binding distances but did not destroy the octahedral iron ligand sphere. For construction of a structural model of the iron ligand sphere the binding distances extracted from the X-ray spectra were assigned to specific amino acids (His-360, -365, -540, -544 and the C-terminal Ile-662) by molecular modelling using the crystal coordinates of the soybean LOX-1 and of a rabbit 15-LOX–inhibitor complex.

Electronic Structure and X-ray Absorption Spectra of Rutile TiO2 Using First-Principles Calculations

2014 ◽  
Vol 52 (12) ◽  
pp. 1025-1029
Author(s):  
Min-Wook Oh ◽  
Tae-Gu Kang ◽  
Byungki Ryu ◽  
Ji Eun Lee ◽  
Sung-Jae Joo ◽  
...  
Keyword(s):  
Electronic Structure ◽  
Absorption Spectra ◽  
First Principles ◽  
First Principles Calculations ◽  
Rutile Tio2 ◽  
X Ray ◽  
X Ray Absorption
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