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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todo:paper_15675394_v105_n_p25_Molinas2023-10-03T16:26:37Z Stability, redox parameters and electrocatalytic activity of a cytochrome domain from a new subfamily Molinas, M.F. Benavides, L. Castro, M.A. Murgida, D.H. 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 Heme proteins Hydrogen peroxide sensing Iron-sulfur proteins Reorganization energies Spectroelectrochemical characterization Proteins cytochrome heme iron sulfur protein oxidoreductase cytochrome Article bleaching catalysis electrochemistry electron transport enzyme activity enzyme denaturation enzyme immobilization enzyme stability nonhuman oxidation reduction reaction Rhodothermus thermodynamics catalysis chemistry electrochemical analysis enzyme stability kinetics metabolism oxidation reduction reaction Rhodothermus marinus Catalysis Cytochromes Electrochemical Techniques Enzyme Stability Kinetics Oxidation-Reduction Thermodynamics 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. Fil:Molinas, M.F. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Murgida, D.H. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_15675394_v105_n_p25_Molinas |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
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 Heme proteins Hydrogen peroxide sensing Iron-sulfur proteins Reorganization energies Spectroelectrochemical characterization Proteins cytochrome heme iron sulfur protein oxidoreductase cytochrome Article bleaching catalysis electrochemistry electron transport enzyme activity enzyme denaturation enzyme immobilization enzyme stability nonhuman oxidation reduction reaction Rhodothermus thermodynamics catalysis chemistry electrochemical analysis enzyme stability kinetics metabolism oxidation reduction reaction Rhodothermus marinus Catalysis Cytochromes Electrochemical Techniques Enzyme Stability Kinetics Oxidation-Reduction Thermodynamics |
| spellingShingle |
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 Heme proteins Hydrogen peroxide sensing Iron-sulfur proteins Reorganization energies Spectroelectrochemical characterization Proteins cytochrome heme iron sulfur protein oxidoreductase cytochrome Article bleaching catalysis electrochemistry electron transport enzyme activity enzyme denaturation enzyme immobilization enzyme stability nonhuman oxidation reduction reaction Rhodothermus thermodynamics catalysis chemistry electrochemical analysis enzyme stability kinetics metabolism oxidation reduction reaction Rhodothermus marinus Catalysis Cytochromes Electrochemical Techniques Enzyme Stability Kinetics Oxidation-Reduction Thermodynamics Molinas, M.F. Benavides, L. Castro, M.A. Murgida, D.H. Stability, redox parameters and electrocatalytic activity of a cytochrome domain from a new subfamily |
| topic_facet |
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 Heme proteins Hydrogen peroxide sensing Iron-sulfur proteins Reorganization energies Spectroelectrochemical characterization Proteins cytochrome heme iron sulfur protein oxidoreductase cytochrome Article bleaching catalysis electrochemistry electron transport enzyme activity enzyme denaturation enzyme immobilization enzyme stability nonhuman oxidation reduction reaction Rhodothermus thermodynamics catalysis chemistry electrochemical analysis enzyme stability kinetics metabolism oxidation reduction reaction Rhodothermus marinus Catalysis Cytochromes Electrochemical Techniques Enzyme Stability Kinetics Oxidation-Reduction Thermodynamics |
| description |
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. |
| format |
JOUR |
| author |
Molinas, M.F. Benavides, L. Castro, M.A. Murgida, D.H. |
| author_facet |
Molinas, M.F. Benavides, L. Castro, M.A. Murgida, D.H. |
| author_sort |
Molinas, M.F. |
| title |
Stability, redox parameters and electrocatalytic activity of a cytochrome domain from a new subfamily |
| title_short |
Stability, redox parameters and electrocatalytic activity of a cytochrome domain from a new subfamily |
| title_full |
Stability, redox parameters and electrocatalytic activity of a cytochrome domain from a new subfamily |
| title_fullStr |
Stability, redox parameters and electrocatalytic activity of a cytochrome domain from a new subfamily |
| title_full_unstemmed |
Stability, redox parameters and electrocatalytic activity of a cytochrome domain from a new subfamily |
| title_sort |
stability, redox parameters and electrocatalytic activity of a cytochrome domain from a new subfamily |
| url |
http://hdl.handle.net/20.500.12110/paper_15675394_v105_n_p25_Molinas |
| work_keys_str_mv |
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| _version_ |
1807321182676975616 |