Formate dehydrogenase from Desulfovibrio desulfuricans ATCC 27774: isolation and spectroscopic characterization of the active sites (heme, iron-sulfur centers and molybdenum)

1997 ◽  
Vol 2 (2) ◽  
pp. 198-208 ◽  
Author(s):  
Cristina Costa ◽  
Miguel Teixeira ◽  
Jean LeGall ◽  
José J. G. Moura ◽  
I. Moura
Keyword(s):  
Active Sites ◽  
Formate Dehydrogenase ◽  
Desulfovibrio Desulfuricans ◽  
Spectroscopic Characterization ◽  
Heme Iron ◽  
Iron Sulfur

ChemInform Abstract: UV Raman Spectroscopic Characterization of Catalysts and Catalytic Active Sites

ChemInform ◽  
2015 ◽  
Vol 46 (8) ◽  
pp. no-no
Author(s):  
Shaoqing Jin ◽  
Zhaochi Feng ◽  
Fengtao Fan ◽  
Can Li
Keyword(s):  
Active Sites ◽  
Spectroscopic Characterization ◽  
Raman Spectroscopic ◽  
Catalytic Active Sites ◽  
Uv Raman

scholarly journals Functional, structural, and spectroscopic characterization of a glutathione-ligated [2Fe–2S] cluster in poplar glutaredoxin C1

2007 ◽  
Vol 104 (18) ◽  
pp. 7379-7384 ◽  
Author(s):  
Nicolas Rouhier ◽  
Hideaki Unno ◽  
Sibali Bandyopadhyay ◽  
Lluis Masip ◽  
Sung-Kun Kim ◽  
...  
Keyword(s):  
Intracellular Localization ◽  
Spectroscopic Characterization ◽  
Spectroscopic Studies ◽  
Iron Sulfur Cluster ◽  
X Ray Crystallography ◽  
Iron Sulfur ◽  
Catalytic Cysteine ◽  
A Subunit ◽  
Stress Sensing

When expressed in Escherichia coli, cytosolic poplar glutaredoxin C1 (CGYC active site) exists as a dimeric iron–sulfur-containing holoprotein or as a monomeric apoprotein in solution. Analytical and spectroscopic studies of wild-type protein and site-directed variants and structural characterization of the holoprotein by using x-ray crystallography indicate that the holoprotein contains a subunit-bridging [2Fe–2S] cluster that is ligated by the catalytic cysteines of two glutaredoxins and the cysteines of two glutathiones. Mutagenesis data on a variety of poplar glutaredoxins suggest that the incorporation of an iron–sulfur cluster could be a general feature of plant glutaredoxins possessing a glycine adjacent to the catalytic cysteine. In light of these results, the possible involvement of plant glutaredoxins in oxidative stress sensing or iron–sulfur biosynthesis is discussed with respect to their intracellular localization.

scholarly journals UV Raman Spectroscopic Characterization of Catalysts and Catalytic Active Sites

2014 ◽  
Vol 145 (1) ◽  
pp. 468-481 ◽  
Author(s):  
Shaoqing Jin ◽  
Zhaochi Feng ◽  
Fengtao Fan ◽  
Can Li
Keyword(s):  
Active Sites ◽  
Spectroscopic Characterization ◽  
Raman Spectroscopic ◽  
Catalytic Active Sites ◽  
Uv Raman

scholarly journals Cage effects control the mechanism of methane hydroxylation in zeolites

Science ◽  
2021 ◽  
Vol 373 (6552) ◽  
pp. 327-331
Author(s):  
Benjamin E. R. Snyder ◽  
Max L. Bols ◽  
Hannah M. Rhoda ◽  
Dieter Plessers ◽  
Robert A. Schoonheydt ◽  
...  
Keyword(s):  
Active Sites ◽  
Density Functional ◽  
Density Functional Theory Calculations ◽  
Spectroscopic Characterization ◽  
Single Turnover ◽  
Small Pore ◽  
Conversion Of Methane ◽  
Hindered Diffusion ◽  
Cage Effects

Catalytic conversion of methane to methanol remains an economically tantalizing but fundamentally challenging goal. Current technologies based on zeolites deactivate too rapidly for practical application. We found that similar active sites hosted in different zeolite lattices can exhibit markedly different reactivity with methane, depending on the size of the zeolite pore apertures. Whereas zeolite with large pore apertures deactivates completely after a single turnover, 40% of active sites in zeolite with small pore apertures are regenerated, enabling a catalytic cycle. Detailed spectroscopic characterization of reaction intermediates and density functional theory calculations show that hindered diffusion through small pore apertures disfavors premature release of CH3 radicals from the active site after C-H activation, thereby promoting radical recombination to form methanol rather than deactivated Fe-OCH3 centers elsewhere in the lattice.

Biochemical and spectroscopic characterization of the high molecular weight cytochrome c from Desulfovibrio vulgaris Hildenborough expressed in Desulfovibrio desulfuricans G200

Biochemistry ◽  
1992 ◽  
Vol 31 (12) ◽  
pp. 3281-3288 ◽  
Author(s):  
Mireille Bruschi ◽  
Patrick Bertrand ◽  
Claude More ◽  
Gisele Leroy ◽  
Jacques Bonicel ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Cytochrome C ◽  
High Molecular Weight ◽  
Desulfovibrio Desulfuricans ◽  
Spectroscopic Characterization ◽  
Desulfovibrio Vulgaris ◽  
Desulfovibrio Vulgaris Hildenborough

scholarly journals Spectroscopic characterization of the novel iron-sulfur cluster in Pyrococcus furiosus ferredoxin.

1990 ◽  
Vol 265 (15) ◽  
pp. 8533-8541
Author(s):  
R C Conover ◽  
A T Kowal ◽  
W G Fu ◽  
J B Park ◽  
S Aono ◽  
...  
Keyword(s):  
Pyrococcus Furiosus ◽  
Spectroscopic Characterization ◽  
The Novel ◽  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
Iron Sulfur
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