scholarly journals Hydrogen peroxide‐mediated conversion of coproheme to heme b by HemQ—lessons from the first crystal structure and kinetic studies

FEBS Journal ◽  
2016 ◽  
Vol 283 (23) ◽  
pp. 4386-4401 ◽  
Author(s):  
Stefan Hofbauer ◽  
Georg Mlynek ◽  
Lisa Milazzo ◽  
Dominic Pühringer ◽  
Daniel Maresch ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Hydrogen Peroxide ◽  
Kinetic Studies

scholarly journals The crystal structure of hydrogen peroxide

1951 ◽  
Vol 4 (1) ◽  
pp. 15-20 ◽  
Author(s):  
S. C. Abrahams ◽  
R. L. Collin ◽  
W. N. Lipscomb
Keyword(s):  
Crystal Structure ◽  
Hydrogen Peroxide

Structure and hydration of polyvinylpyrrolidone-hydrogen peroxide

2021 ◽  
Author(s):  
Luke I. Chambers ◽  
Dimitrii S. Yufit ◽  
Mark A Fox ◽  
Osama Musa ◽  
Jonathan W Steed
Keyword(s):  
Crystal Structure ◽  
Hydrogen Peroxide ◽  
Commercially Important

The structure of the commercially important polyvinylpyrrolidone-hydrogen peroxide complex can be understood by reference to the co-crystal structure of a hydrogen peroxide complex and its mixed hydrates of a two-monomer...

scholarly journals Structure of theMycobacterium tuberculosisd-Alanine:d-Alanine Ligase, a Target of the Antituberculosis Drug d-Cycloserine

2010 ◽  
Vol 55 (1) ◽  
pp. 291-301 ◽  
Author(s):  
John B. Bruning ◽  
Ana C. Murillo ◽  
Ofelia Chacon ◽  
Raúl G. Barletta ◽  
James C. Sacchettini
Keyword(s):  
Crystal Structure ◽  
Binding Site ◽  
Kinetic Studies ◽  
Structural Rearrangement ◽  
Peptidoglycan Biosynthesis ◽  
Binding Cavity ◽  
Binding Pockets ◽  
Loop Regions ◽  
Discrete Domains ◽  
Alanine Dipeptide

ABSTRACTd-Alanine:d-alanine ligase (EC 6.3.2.4; Ddl) catalyzes the ATP-driven ligation of twod-alanine (d-Ala) molecules to form thed-alanyl:d-alanine dipeptide. This molecule is a key building block in peptidoglycan biosynthesis, making Ddl an attractive target for drug development.d-Cycloserine (DCS), an analog ofd-Ala and a prototype Ddl inhibitor, has shown promise for the treatment of tuberculosis. Here, we report the crystal structure ofMycobacterium tuberculosisDdl at a resolution of 2.1 Å. This structure indicates that Ddl is a dimer and consists of three discrete domains; the ligand binding cavity is at the intersection of all three domains and conjoined by several loop regions. TheM. tuberculosisapo Ddl structure shows a novel conformation that has not yet been observed in Ddl enzymes from other species. The nucleotide andd-alanine binding pockets are flexible, requiring significant structural rearrangement of the bordering regions for entry and binding of both ATP andd-Ala molecules. Solution affinity and kinetic studies showed that DCS interacts with Ddl in a manner similar to that observed ford-Ala. Each ligand binds to two binding sites that have significant differences in affinity, with the first binding site exhibiting high affinity. DCS inhibits the enzyme, with a 50% inhibitory concentration (IC50) of 0.37 mM under standard assay conditions, implicating a preferential and weak inhibition at the second, lower-affinity binding site. Moreover, DCS binding is tighter at higher ATP concentrations. The crystal structure illustrates potential drugable sites that may result in the development of more-effective Ddl inhibitors.

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