Stability, redox parameters and electrocatalytic activity of a cytochrome domain from a new subfamily

We report a spectroscopic, electrochemical and spectroelectrochemical characterization of the soluble cytochrome c domain (Cyt-D) from the Rhodothermus marinus caa<inf>3</inf> terminal oxygen reductase and its putative electron donor, a high potential [4Fe-4S] protein (HiPIP). Cyt-D exhi...

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Detalles Bibliográficos
Autores principales:	Molinas, M.F., Benavides, L., Castro, M.A., Murgida, D.H.
Formato:	JOUR
Materias:	Heme proteins Hydrogen peroxide sensing Iron-sulfur proteins Protein electron transfer SERR spectroelectrochemistry Alkalinity Biomimetics Chemical stability Electron transitions Porphyrins Spectroelectrochemistry Electrocatalytic activity Electrochemical biosensing Electron transfer Reorganization energies Spectroelectrochemical characterization Proteins cytochrome heme iron sulfur protein oxidoreductase Article bleaching catalysis electrochemistry electron transport enzyme activity enzyme denaturation enzyme immobilization enzyme stability nonhuman oxidation reduction reaction Rhodothermus thermodynamics chemistry electrochemical analysis kinetics metabolism Rhodothermus marinus Catalysis Cytochromes Electrochemical Techniques Enzyme Stability Kinetics Oxidation-Reduction Thermodynamics
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_15675394_v105_n_p25_Molinas
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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