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

2003 ◽  
Vol 96 (1) ◽  
pp. 142
Author(s):  
Graeme R. Hanson ◽  
Christopher J. Noble ◽  
Christopher A. McDevitt ◽  
Alastair G. McEwan


1999 ◽  
Vol 343 (1) ◽  
pp. 185-190 ◽  
Author(s):  
Laura REQUENA ◽  
Stephen BORNEMANN

Oxalate oxidase (EC 1.2.3.4) catalyses the conversion of oxalate and dioxygen into CO2 and H2O2. The barley (Hordeum vulgare) seedling root enzyme was purified to homogeneity and shown by metal analysis and EPR spectroscopy to contain Mn(II) at up to 0.80 atom per subunit. The involvement of Mn and neither flavin, Cu nor Fe in the direct conversion of dioxygen to H2O2 makes oxalate oxidase unique. A model of the active site of the holoenzyme based on a homology model of the apoenzyme is proposed.



1997 ◽  
Vol 250 (2) ◽  
pp. 539-548 ◽  
Author(s):  
Haripada Maity ◽  
Gotam K. Jarori


PLoS ONE ◽  
2016 ◽  
Vol 11 (6) ◽  
pp. e0157944 ◽  
Author(s):  
Marcos de Oliveira ◽  
Robert Knitsch ◽  
Muhammad Sajid ◽  
Annika Stute ◽  
Lisa-Maria Elmer ◽  
...  


2019 ◽  
Vol 116 (3) ◽  
pp. 56a
Author(s):  
Gary A. Lorigan ◽  
Indra D. Sahu ◽  
Daniel L. Drew ◽  
Gunjan Dixit ◽  
Tanbir Ahammad


2020 ◽  
Vol 22 (11) ◽  
pp. 6457-6467 ◽  
Author(s):  
Philip Charles ◽  
Vidmantas Kalendra ◽  
Zhihui He ◽  
Mohammad Hassan Khatami ◽  
John H. Golbeck ◽  
...  

Using pulsed EPR spectroscopy and isotopic labeling we demonstrate that reaction centers of Chloracidobacterium thermophilum have an unusual primary donor that is a dimer of Zn-bacteriochlorophyll aP′ molecules.



2012 ◽  
Vol 376 (32) ◽  
pp. 2195-2199 ◽  
Author(s):  
Pengbo Feng ◽  
Ya Wang ◽  
Xing Rong ◽  
Ji-Hu Su ◽  
Chenyong Ju ◽  
...  


Sign in / Sign up

Export Citation Format

Share Document