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
Descripción
Sumario: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 exhibits superior stability, particularly at the level of the heme pocket, compared to archetypical cytochromes in terms of thermal and chemical denaturation, alkaline transition and oxidative bleaching of the heme, which is further increased upon adsorption on biomimetic electrodes. Therefore, this protein is proposed as a suitable building block for electrochemical biosensing. As a proof of concept, we show that the immobilized Cyt-D exhibits good electrocatalytic activity towards H<inf>2</inf>O<inf>2</inf> reduction. Relevant thermodynamic and kinetic electron transfer parameters for Cyt-D and HiPIP are also reported, including reorganization energies of 0.33eV and 0.42eV, respectively. © 2015 Elsevier B.V.

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