Pulsed EPR analysis of tartrate dehydrogenase active-site complexes

Biochemistry ◽  
1991 ◽  
Vol 30 (3) ◽  
pp. 739-744 ◽  
Author(s):  
Peter A. Tipton ◽  
Jack Peisach
Keyword(s):  
Active Site ◽  
Pulsed Epr

Pulsed EPR study of imidazole-coordinated oxovanadium(IV) complexes relevant to the active-site structure of vanadium bromoperoxidase

1997 ◽  
Vol 67 (1-4) ◽  
pp. 392
Author(s):  
K. Fukui ◽  
H. Ohya-Nishiguchi ◽  
H. Kamada
Keyword(s):  
Active Site ◽  
Site Structure ◽  
Pulsed Epr ◽  
Active Site Structure

CW and pulsed EPR spectroscopy reveal a new structural motif for the active site Mo centre and an unusual [4Fe-4S]+ cluster in dimethylsulfide dehydrogenase

2003 ◽  
Vol 96 (1) ◽  
pp. 142
Author(s):  
Graeme R. Hanson ◽  
Christopher J. Noble ◽  
Christopher A. McDevitt ◽  
Alastair G. McEwan
Keyword(s):  
Epr Spectroscopy ◽  
Active Site ◽  
Structural Motif ◽  
Pulsed Epr

Pulsed EPR Studies of Nonexchangeable Protons near the Mo(V) Center of Sulfite Oxidase:  Direct Detection of the α-Proton of the Coordinated Cysteinyl Residue and Structural Implications for the Active Site

2002 ◽  
Vol 124 (21) ◽  
pp. 6109-6118 ◽  
Author(s):  
Andrei V. Astashkin ◽  
Arnold M. Raitsimring ◽  
Changjian Feng ◽  
Jean L. Johnson ◽  
K. V. Rajagopalan ◽  
...  
Keyword(s):  
Active Site ◽  
Direct Detection ◽  
Sulfite Oxidase ◽  
Pulsed Epr ◽  
Cysteinyl Residue

Evidence for Changes in the Nucleotide Conformation in the Active Site of H+-ATPase As Determined by Pulsed EPR Spectroscopy

Biochemistry ◽  
2000 ◽  
Vol 39 (50) ◽  
pp. 15500-15512 ◽  
Author(s):  
Benoît Schneider ◽  
Claude Sigalat ◽  
Toyoki Amano ◽  
Jean-Luc Zimmermann
Keyword(s):  
Epr Spectroscopy ◽  
Active Site ◽  
Pulsed Epr ◽  
Nucleotide Conformation

Locating Al in the DABCO catalyst before and after Al extraction

1990 ◽  
Vol 48 (4) ◽  
pp. 265-267
Author(s):  
Kathleen B. Reuter
Keyword(s):  
Active Site ◽  
Inverse Relationship ◽  
Transverse Direction ◽  
Reaction Rate ◽  
Acid Phosphate ◽  
Fracture Surfaces ◽  
Al Content ◽  
Before And After ◽  
Relationship Of

The reaction rate and efficiency of piperazine to 1,4-diazabicyclo-octane (DABCO) depends on the Si/Al ratio of the MFI topology catalysts. The Al was shown to be the active site, however, in the Si/Al range of 30-200 the reaction rate increases as the Si/Al ratio increases. The objective of this work was to determine the location and concentration of Al to explain this inverse relationship of Al content with reaction rate.Two silicalite catalysts in the form of 1/16 inch SiO2/Al2O3 bonded extrudates were examined: catalyst A with a Si/Al of 83; and catalyst B, the acid/phosphate Al extracted form of catalyst A, with a Si/Al of 175. Five extrudates from each catalyst were fractured in the transverse direction and particles were obtained from the fracture surfaces near the center of the extrudate diameter. Particles were also obtained from the outside surfaces of five extrudates.

Structures of c-di-GMP/cGAMP degrading phosphodiesterase VcEAL: identification of a novel conformational switch and its implication

2019 ◽  
Vol 476 (21) ◽  
pp. 3333-3353 ◽  
Author(s):  
Malti Yadav ◽  
Kamalendu Pal ◽  
Udayaditya Sen
Keyword(s):  
Active Site ◽  
Metal Binding ◽  
Metal Ion ◽  
Triosephosphate Isomerase ◽  
Catalytic Mechanism ◽  
Degradation Mechanism ◽  
Structural Basis ◽  
Conserved Residues ◽  
Phosphodiester Bond ◽  
Cyclic Dinucleotides

Cyclic dinucleotides (CDNs) have emerged as the central molecules that aid bacteria to adapt and thrive in changing environmental conditions. Therefore, tight regulation of intracellular CDN concentration by counteracting the action of dinucleotide cyclases and phosphodiesterases (PDEs) is critical. Here, we demonstrate that a putative stand-alone EAL domain PDE from Vibrio cholerae (VcEAL) is capable to degrade both the second messenger c-di-GMP and hybrid 3′3′-cyclic GMP–AMP (cGAMP). To unveil their degradation mechanism, we have determined high-resolution crystal structures of VcEAL with Ca2+, c-di-GMP-Ca2+, 5′-pGpG-Ca2+ and cGAMP-Ca2+, the latter provides the first structural basis of cGAMP hydrolysis. Structural studies reveal a typical triosephosphate isomerase barrel-fold with substrate c-di-GMP/cGAMP bound in an extended conformation. Highly conserved residues specifically bind the guanine base of c-di-GMP/cGAMP in the G2 site while the semi-conserved nature of residues at the G1 site could act as a specificity determinant. Two metal ions, co-ordinated with six stubbornly conserved residues and two non-bridging scissile phosphate oxygens of c-di-GMP/cGAMP, activate a water molecule for an in-line attack on the phosphodiester bond, supporting two-metal ion-based catalytic mechanism. PDE activity and biofilm assays of several prudently designed mutants collectively demonstrate that VcEAL active site is charge and size optimized. Intriguingly, in VcEAL-5′-pGpG-Ca2+ structure, β5–α5 loop adopts a novel conformation that along with conserved E131 creates a new metal-binding site. This novel conformation along with several subtle changes in the active site designate VcEAL-5′-pGpG-Ca2+ structure quite different from other 5′-pGpG bound structures reported earlier.

Contributions of the substrate-binding arginine residues to maleate-induced closure of the active site of Escherichia coli aspartate aminotransferase

2001 ◽  
Vol 268 (6) ◽  
pp. 1640-1645
Author(s):  
Annelise Matharu ◽  
Hideyuki Hayashi ◽  
Hiroyuki Kagamiyama ◽  
Bruno Maras ◽  
Robert A. John
Keyword(s):  
Escherichia Coli ◽  
Active Site ◽  
Aspartate Aminotransferase ◽  
Substrate Binding ◽  
Arginine Residues

Alkane upgrading effected by silica-supported pincer-iridium catalysts: Evidence of a shared active site with solution-phase species

2020 ◽  
Author(s):  
Alan Goldman ◽  
Boris Sheludko ◽  
Fuat Celik ◽  
Cristina Castro
Keyword(s):  
Active Site ◽  
Solution Phase ◽  
Iridium Catalysts

Active site-inhibited seven: Mechanism of action including signal transduction

2001 ◽  
Vol 38 (4F) ◽  
pp. 39-42 ◽  
Author(s):  
Lars C. Petersen
Keyword(s):  
Signal Transduction ◽  
Mechanism Of Action ◽  
Active Site
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