New structural insights into the iron-molybdenum cofactor from Azotobacter vinelandii nitrogenase through sulfur K and molybdenum L x-ray absorption edge studies

1988 ◽  
Vol 110 (12) ◽  
pp. 3798-3805 ◽  
Author(s):  
Britt. Hedman ◽  
Patrick. Frank ◽  
Stephen F. Gheller ◽  
A. Lawrence. Roe ◽  
William E. Newton ◽  
...  
Keyword(s):  
Absorption Edge ◽  
Azotobacter Vinelandii ◽  
Molybdenum Cofactor ◽  
X Ray ◽  
Iron Molybdenum Cofactor ◽  
X Ray Absorption ◽  
Structural Insights

scholarly journals Comparison of Iron-Molybdenum Cofactor-deficient Nitrogenase MoFe Proteins by X-ray Absorption Spectroscopy

2004 ◽  
Vol 279 (27) ◽  
pp. 28276-28282 ◽  
Author(s):  
Mary C. Corbett ◽  
Yilin Hu ◽  
Farzad Naderi ◽  
Markus W. Ribbe ◽  
Britt Hedman ◽  
...  
Keyword(s):  
Absorption Spectroscopy ◽  
Molybdenum Cofactor ◽  
X Ray ◽  
Iron Molybdenum Cofactor ◽  
X Ray Absorption

scholarly journals Selenol binds to iron in nitrogenase iron-molybdenum cofactor: an extended x-ray absorption fine structure study.

1994 ◽  
Vol 91 (4) ◽  
pp. 1290-1293 ◽  
Author(s):  
S. D. Conradson ◽  
B. K. Burgess ◽  
W. E. Newton ◽  
A. Di Cicco ◽  
A. Filipponi ◽  
...  
Keyword(s):  
Fine Structure ◽  
Structure Study ◽  
Molybdenum Cofactor ◽  
X Ray ◽  
Absorption Fine ◽  
Iron Molybdenum Cofactor ◽  
X Ray Absorption

scholarly journals Small-angle x-ray scattering studies of the iron-molybdenum cofactor from Azotobacter vinelandii nitrogenase.

1993 ◽  
Vol 268 (28) ◽  
pp. 20953-20957
Author(s):  
D Eliezer ◽  
P Frank ◽  
N Gillis ◽  
W.E. Newton ◽  
S Doniach ◽  
...  
Keyword(s):  
Small Angle ◽  
Azotobacter Vinelandii ◽  
Molybdenum Cofactor ◽  
X Ray ◽  
X Ray Scattering ◽  
Iron Molybdenum Cofactor ◽  
Ray Scattering

The molybdenum site of nitrogenase. 2. A comparative study of molybdenum-iron proteins and the iron-molybdenum cofactor by x-ray absorption spectroscopy

1978 ◽  
Vol 100 (12) ◽  
pp. 3814-3819 ◽  
Author(s):  
Stephen P. Cramer ◽  
William O. Gillum ◽  
Keith O. Hodgson ◽  
Leonard E. Mortenson ◽  
Edward I. Stiefel ◽  
...  
Keyword(s):  
Comparative Study ◽  
Absorption Spectroscopy ◽  
Molybdenum Cofactor ◽  
X Ray ◽  
Iron Proteins ◽  
Iron Molybdenum Cofactor ◽  
X Ray Absorption

scholarly journals Iron K-edge X-ray absorption spectroscopy of the iron-molybdenum cofactor of nitrogenase from Klebsiella pneumoniae

1988 ◽  
Vol 252 (2) ◽  
pp. 421-425 ◽  
Author(s):  
J M Arber ◽  
A C Flood ◽  
C D Garner ◽  
C A Gormal ◽  
S S Hasnain ◽  
...  
Keyword(s):  
Klebsiella Pneumoniae ◽  
Long Range ◽  
Absorption Spectroscopy ◽  
Molybdenum Cofactor ◽  
Published Data ◽  
Absorption Data ◽  
X Ray ◽  
Chemical Models ◽  
Iron Molybdenum Cofactor ◽  
X Ray Absorption

Iron K-edge X-ray absorption data for the iron-molybdenum cofactor (‘FeMoco’) from Klebsiella pneumoniae reported here provide the first evidence for long-range structural order in the cofactor [Fe…Fe(Mo) = 0.368 nm in addition to Fe…S = 0.22 nm and Fe…Fe(Mo) = 0.27 nm] and, in contrast with previously published data [Antonio, Teo, Orme-Johnson, Nelson, Groh, Lindahl, Kauzlarich & Averill (1982) J. Am. Chem. Soc. 104, 4703-4705], indicate that most of the iron centres are not co-ordinated to light (oxygen, nitrogen) atoms. This demonstrates that presently available chemical models for FeMoco are inadequate.

X-Ray absorption edge elemental imaging of B. thuringienis

1989 ◽  
Vol 47 ◽  
pp. 212-213
Author(s):  
R. L. Stears
Keyword(s):  
Absorption Edge ◽  
Elemental Distribution ◽  
X Rays ◽  
Differential Absorption ◽  
Synchrotron Source ◽  
High Brightness ◽  
X Ray ◽  
Elemental Imaging ◽  
Cellular Integrity ◽  
X Ray Absorption

Because of the nature of the bacterial endospore, little work has been done on analyzing their elemental distribution and composition in the intact, living, hydrated state. The majority of the qualitative analysis entailed intensive disruption and processing of the endospores, which effects their cellular integrity and composition.Absorption edge imaging permits elemental analysis of hydrated, unstained specimens at high resolution. By taking advantage of differential absorption of x-ray photons in regions of varying elemental composition, and using a high brightness, tuneable synchrotron source to obtain monochromatic x-rays, contact x-ray micrographs can be made of unfixed, intact endospores that reveal sites of elemental localization. This study presents new data demonstrating the application of x-ray absorption edge imaging to produce elemental information about nitrogen (N) and calcium (Ca) localization using Bacillus thuringiensis as the test specimen.

Protonation and Sulfido versus Oxo Ligation Changes at the Molybdenum Cofactor in Xanthine Dehydrogenase (XDH) Variants Studied by X-ray Absorption Spectroscopy

2017 ◽  
Vol 56 (4) ◽  
pp. 2165-2176 ◽  
Author(s):  
Stefan Reschke ◽  
Stefan Mebs ◽  
Kajsa G. V. Sigfridsson-Clauss ◽  
Ramona Kositzki ◽  
Silke Leimkühler ◽  
...  
Keyword(s):  
Absorption Spectroscopy ◽  
Xanthine Dehydrogenase ◽  
Molybdenum Cofactor ◽  
X Ray ◽  
X Ray Absorption
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