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Journal of Inorganic Biochemistry
|
April 19, 2005
Standard reduction potentials of all couples of the peroxidase cycle of lactoperoxidase
Paul Georg Furtmüller, Jürgen Arnhold, Walter Jantschko, et al.
Biochemical and Biophysical Research Communications
|
November 26, 2003
Direct conversion of ferrous myeloperoxidase to compound II by hydrogen peroxide: an anaerobic stopped-flow study
Walter Jantschko, Paul Georg Furtmüller, Martina Zederbauer, et al.
Japanese Journal of Infectious Diseases
|
October 28, 2004
Kinetics of interconversion of redox intermediates of lactoperoxidase, eosinophil peroxidase and myeloperoxidase
Paul Georg Furtmüller, Walter Jantschko, Martina Zederbauer, et al.
The Journal of Biological Chemistry
|
October 26, 2005
Role of the main access channel of catalase-peroxidase in catalysis
Christa Jakopitsch, Enrica Droghetti, Florian Schmuckenschlager, et al.
Biochemistry
|
July 18, 2002
New insights into the heme cavity structure of catalase-peroxidase: a spectroscopic approach to the recombinant synechocystis enzyme and selected distal cavity mutants
Hendrik A Heering, Chiara Indiani, Günther Regelsberger, et al.
Gene
|
June 15, 2007
Phylogenetic distribution of catalase-peroxidases: are there patches of order in chaos?
Filippo Passardi, Marcel Zamocky, Jocelyne Favet, et al.
Journal of Inorganic Biochemistry
|
July 18, 2002
Engineering the proximal heme cavity of catalase-peroxidase
Christa Jakopitsch, Günther Regelsberger, Paul Georg Furtmüller, et al.
European Journal of Biochemistry
|
February 27, 2003
The catalytic role of the distal site asparagine-histidine couple in catalase-peroxidases
Christa Jakopitsch, Markus Auer, Günther Regelsberger, et al.
Biochemistry
|
May 7, 2003
Distal site aspartate is essential in the catalase activity of catalase-peroxidases
Christa Jakopitsch, Markus Auer, Günther Regelsberger, et al.
Biochemistry
|
April 27, 2005
Role of the covalent glutamic acid 242-heme linkage in the formation and reactivity of redox intermediates of human myeloperoxidase
Martina Zederbauer, Walter Jantschko, Karin Neugschwandtner, et al.
Page
of 5
Search research articles
Search
Showing results (21-30 of 49) with videos related to
Sort By:
Page
of 5
Journal of Inorganic Biochemistry
|
April 19, 2005
Standard reduction potentials of all couples of the peroxidase cycle of lactoperoxidase
Paul Georg Furtmüller, Jürgen Arnhold, Walter Jantschko, et al.
Biochemical and Biophysical Research Communications
|
November 26, 2003
Direct conversion of ferrous myeloperoxidase to compound II by hydrogen peroxide: an anaerobic stopped-flow study
Walter Jantschko, Paul Georg Furtmüller, Martina Zederbauer, et al.
Japanese Journal of Infectious Diseases
|
October 28, 2004
Kinetics of interconversion of redox intermediates of lactoperoxidase, eosinophil peroxidase and myeloperoxidase
Paul Georg Furtmüller, Walter Jantschko, Martina Zederbauer, et al.
The Journal of Biological Chemistry
|
October 26, 2005
Role of the main access channel of catalase-peroxidase in catalysis
Christa Jakopitsch, Enrica Droghetti, Florian Schmuckenschlager, et al.
Biochemistry
|
July 18, 2002
New insights into the heme cavity structure of catalase-peroxidase: a spectroscopic approach to the recombinant synechocystis enzyme and selected distal cavity mutants
Hendrik A Heering, Chiara Indiani, Günther Regelsberger, et al.
Gene
|
June 15, 2007
Phylogenetic distribution of catalase-peroxidases: are there patches of order in chaos?
Filippo Passardi, Marcel Zamocky, Jocelyne Favet, et al.
Journal of Inorganic Biochemistry
|
July 18, 2002
Engineering the proximal heme cavity of catalase-peroxidase
Christa Jakopitsch, Günther Regelsberger, Paul Georg Furtmüller, et al.
European Journal of Biochemistry
|
February 27, 2003
The catalytic role of the distal site asparagine-histidine couple in catalase-peroxidases
Christa Jakopitsch, Markus Auer, Günther Regelsberger, et al.
Biochemistry
|
May 7, 2003
Distal site aspartate is essential in the catalase activity of catalase-peroxidases
Christa Jakopitsch, Markus Auer, Günther Regelsberger, et al.
Biochemistry
|
April 27, 2005
Role of the covalent glutamic acid 242-heme linkage in the formation and reactivity of redox intermediates of human myeloperoxidase
Martina Zederbauer, Walter Jantschko, Karin Neugschwandtner, et al.
Page
of 5