These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
2. Disruption of the H-bond network in the main access channel of catalase-peroxidase modulates enthalpy and entropy of Fe(III) reduction. Vlasits J, Bellei M, Jakopitsch C, De Rienzo F, Furtmüller PG, Zamocky M, Sola M, Battistuzzi G, Obinger C. J Inorg Biochem; 2010 Jun; 104(6):648-56. PubMed ID: 20347488 [Abstract] [Full Text] [Related]
6. Kinetics of interconversion of ferrous enzymes, compound II and compound III, of wild-type synechocystis catalase-peroxidase and Y249F: proposal for the catalatic mechanism. Jakopitsch C, Wanasinghe A, Jantschko W, Furtmüller PG, Obinger C. J Biol Chem; 2005 Mar 11; 280(10):9037-42. PubMed ID: 15637065 [Abstract] [Full Text] [Related]
7. Redox thermodynamics of the Fe(III)/Fe(II) couple of human myeloperoxidase in its high-spin and low-spin forms. Battistuzzi G, Bellei M, Zederbauer M, Furtmüller PG, Sola M, Obinger C. Biochemistry; 2006 Oct 24; 45(42):12750-5. PubMed ID: 17042493 [Abstract] [Full Text] [Related]
9. Comparison between catalase-peroxidase and cytochrome c peroxidase. The role of the hydrogen-bond networks for protein stability and catalysis. Santoni E, Jakopitsch C, Obinger C, Smulevich G. Biochemistry; 2004 May 18; 43(19):5792-802. PubMed ID: 15134453 [Abstract] [Full Text] [Related]
10. Protein-based radicals in the catalase-peroxidase of synechocystis PCC6803: a multifrequency EPR investigation of wild-type and variants on the environment of the heme active site. Ivancich A, Jakopitsch C, Auer M, Un S, Obinger C. J Am Chem Soc; 2003 Nov 19; 125(46):14093-102. PubMed ID: 14611246 [Abstract] [Full Text] [Related]