Role of the Flavin Domain Residues, His689 and Asn732, in the Catalytic Mechanism of Cellobiose Dehydrogenase from Phanerochaete Chrysosporium†

Biochemistry ◽  
2003 ◽  
Vol 42 (14) ◽  
pp. 4049-4056 ◽  
Author(s):  
Frederik A. J. Rotsaert ◽  
V. Renganathan ◽  
Michael H. Gold
Keyword(s):  
Phanerochaete Chrysosporium ◽  
Catalytic Mechanism ◽  
Cellobiose Dehydrogenase ◽  
Flavin Domain

Role of Lys-226 in the Catalytic Mechanism ofBacillus StearothermophilusSerine HydroxymethyltransferaseCrystal Structure and Kinetic Studies†,‡

Biochemistry ◽  
2005 ◽  
Vol 44 (18) ◽  
pp. 6929-6937 ◽  
Author(s):  
Siddegowda Bhavani ◽  
V. Trivedi ◽  
V. R. Jala ◽  
H. S. Subramanya ◽  
Purnima Kaul ◽  
...  
Keyword(s):  
Catalytic Mechanism ◽  
Kinetic Studies

Study of the catalytic mechanism of a non-heme Fe catalyst: The role of the spin state of the iron

2021 ◽  
Vol 764 ◽  
pp. 138282
Author(s):  
Aikaterini Gemenetzi ◽  
Panagiota Stathi ◽  
Yiannis Deligiannakis ◽  
Maria Louloudi
Keyword(s):  
Spin State ◽  
Catalytic Mechanism ◽  
Fe Catalyst

Crystal structure of the wild-type and D30A mutant thioredoxin h of Chlamydomonas reinhardtii and implications for the catalytic mechanism

2001 ◽  
Vol 359 (1) ◽  
pp. 65-75 ◽  
Author(s):  
Valeria MENCHISE ◽  
Catherine CORBIER ◽  
Claude DIDIERJEAN ◽  
Michele SAVIANO ◽  
Ettore BENEDETTI ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Proton Transfer ◽  
Chlamydomonas Reinhardtii ◽  
Catalytic Mechanism ◽  
Structural Data ◽  
Careful Analysis ◽  
Wild Type ◽  
Thioredoxin H ◽  
Dynamics Simulations

Thioredoxins are ubiquitous proteins which catalyse the reduction of disulphide bridges on target proteins. The catalytic mechanism proceeds via a mixed disulphide intermediate whose breakdown should be enhanced by the involvement of a conserved buried residue, Asp-30, as a base catalyst towards residue Cys-39. We report here the crystal structure of wild-type and D30A mutant thioredoxin h from Chlamydomonas reinhardtii, which constitutes the first crystal structure of a cytosolic thioredoxin isolated from a eukaryotic plant organism. The role of residue Asp-30 in catalysis has been revisited since the distance between the carboxylate OD1 of Asp-30 and the sulphur SG of Cys-39 is too great to support the hypothesis of direct proton transfer. A careful analysis of all available crystal structures reveals that the relative positioning of residues Asp-30 and Cys-39 as well as hydrophobic contacts in the vicinity of residue Asp-30 do not allow a conformational change sufficient to bring the two residues close enough for a direct proton transfer. This suggests that protonation/deprotonation of Cys-39 should be mediated by a water molecule. Molecular-dynamics simulations, carried out either in vacuo or in water, as well as proton-inventory experiments, support this hypothesis. The results are discussed with respect to biochemical and structural data.

Structure−Function Relationships in Human Glutathione-Dependent Formaldehyde Dehydrogenase. Role of Glu-67 and Arg-368 in the Catalytic Mechanism†,‡

Biochemistry ◽  
2006 ◽  
Vol 45 (15) ◽  
pp. 4819-4830 ◽  
Author(s):  
Paresh C. Sanghani ◽  
Wilhelmina I. Davis ◽  
LanMin Zhai ◽  
Howard Robinson
Keyword(s):  
Structure Function ◽  
Catalytic Mechanism ◽  
Formaldehyde Dehydrogenase

Crystallographic and Enzymic Investigations on the Role of Ser558, His610, and Asn614 in the Catalytic Mechanism of Azotobacter vinelandii Dihydrolipoamide Acetyltransferase (E2p)

Biochemistry ◽  
1995 ◽  
Vol 34 (13) ◽  
pp. 4287-4298 ◽  
Author(s):  
Joerg Hendle ◽  
Andrea Mattevi ◽  
Adrie H. Westphal ◽  
Johan Spee ◽  
Arie de Kok ◽  
...  
Keyword(s):  
Catalytic Mechanism ◽  
Azotobacter Vinelandii
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