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Evolutionary Approaches to Study Cytochrome c Peroxidase
CHIMIA, 2001 Directed molecular evolution of enzymes and proteins has emerged as an extremely powerful method to create proteins with novel properties, both for practical applications as well as for mechanistic studies.
André Iffland +3 more
doaj +6 more sources
Cytochrome c-peroxidase modulates ROS homeostasis to regulate the sexual mating of Sporisorium scitamineum [PDF]
Microbiology Spectrum, 2023 Sugarcane smut, caused by the basidiomycetous fungus Sporisorium scitamineum, is a global fungal disease resulting in substantial economic losses. Our previous research has highlighted the significant role of reactive oxide species (ROS) in the sexual ...
Enping Cai +7 more
doaj +2 more sources
Studies on Cytochrome c Peroxidase
Journal of Biological Chemistry, 1966 The peroxidatic oxidation of ferrocytochrome c catalyzed by yeast cytochrome c peroxidase was studied kinetically in the following combinations of substrates: H2O2-horse heart cytochrome c, C2H5OOH-horse heart cytochome c, H2O2-bakers' yeast cytochrome c, and C2H5OOH-bakers' yeast cytochrome c.
Takashi Yonetani, Gisela S. Ray
+14 more sources
Leishmania major peroxidase is a cytochrome c peroxidase. [PDF]
Biochemistry, 2012 Leishmania major peroxidase (LmP) exhibits both ascorbate and cytochrome c peroxidase activities. Our previous results illustrated that LmP has a much higher activity against horse heart cytochrome c than ascorbate, suggesting that cytochrome c may be the biologically important substrate.
Jasion VS, Poulos TL.
europepmc +6 more sources
Studies on Cytochrome c Peroxidase [PDF]
Journal of Biological Chemistry, 1969 Abstract Protoporphyrin monomethyl ester and protoheme monomethyl ester were recombined with apocytochrome c per-oxidase. The iron-free porphyrin-protein complex has absorption maxima at 408, 511, 547, 576, and 629 nm. The complex has no peroxidase activity. The protoheme monomethyl ester complex reacts with a stoichiometric amount of hydrogen peroxide
Takashi Yonetani, Toshio Asakura
+13 more sources
In-silico assessment of protein-protein electron transfer. a case study: cytochrome c peroxidase--cytochrome c. [PDF]
PLoS Computational Biology, 2013 The fast development of software and hardware is notably helping in closing the gap between macroscopic and microscopic data. Using a novel theoretical strategy combining molecular dynamics simulations, conformational clustering, ab-initio quantum ...
Frank H Wallrapp +2 more
doaj +2 more sources
Two-dimensional infrared spectroscopic study of cytochrome c peroxidase activity in deep eutectic solvent [PDF]
Structural Dynamics, 2019 Deep eutectic solvents (DESs) prepared by mixing hydrogen-bond donor and acceptor molecules have been found to be of use in several applications. Recently, it was shown that DESs can enhance the peroxidation activity of cytochrome c.
Koji Osawa +4 more
doaj +2 more sources
Studies on Cytochrome c Peroxidase
Journal of Biological Chemistry, 1967 Abstract The reaction of ferrimyoglobin with H2O2 was investigated by a combination of spectrophotometric and electron paramagnetic resonance measurements and enzymic assay of of hydroperoxide by the cytochrome c peroxidase system. On the addition of an excess of H2O2 to ferrimyoglobin, approximately 1.5 moles of H2O2 were consumed per mole of the ...
Takashi Yonetani
+6 more sources
Order-to-Disorder and Disorder-to-Order Transitions of Proteins upon Binding to Phospholipid Membranes: Common Ground and Dissimilarities [PDF]
BiomoleculesCytochrome c is one of the most prominent representatives of peripheral membrane proteins. Besides functioning as an electron transfer carrier in the mitochondrial respiratory chain, it can acquire peroxidase capability, promote the self-assembly of α ...
Reinhard Schweitzer-Stenner
doaj +2 more sources
Kinetic and equilibrium studies of acrylonitrile binding to cytochrome c peroxidase and oxidation of acrylonitrile by cytochrome c peroxidase compound I. [PDF]
Biochem Biophys Res Commun, 2014 Ferric heme proteins bind weakly basic ligands and the binding affinity is often pH dependent due to protonation of the ligand as well as the protein. In an effort to find a small, neutral ligand without significant acid/base properties to probe ligand binding reactions in ferric heme proteins we were led to consider the organonitriles.
Chinchilla D +3 more
europepmc +5 more sources