Structure, electrocatalysis and dynamics of immobilized cytochrome PccH and its microperoxidase

Geobacter sulfurreducens cells have the ability to exchange electrons with conductive materials, and the periplasmic cytochrome PccH plays an essential role in the direct electrode-to-cell electron transfer in this bacterium. It has atypically low redox potential and unique structural features that...

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Detalles Bibliográficos
Autor principal: Murgida, Daniel Horacio
Publicado: 2017
Materias:
bacterial protein
cytochrome c
peroxidase
adsorption
electrode
electron
Geobacter
metabolism
Raman spectrometry
thermodynamics
Adsorption
Bacterial Proteins
Cytochromes c
Electrodes
Electrons
Peroxidases
Spectrum Analysis, Raman
Thermodynamics
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_14639076_v19_n13_p8908_Silveira
http://hdl.handle.net/20.500.12110/paper_14639076_v19_n13_p8908_Silveira
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id paper:paper_14639076_v19_n13_p8908_Silveira
record_format dspace
spelling paper:paper_14639076_v19_n13_p8908_Silveira2023-06-08T16:16:30Z Structure, electrocatalysis and dynamics of immobilized cytochrome PccH and its microperoxidase Murgida, Daniel Horacio bacterial protein cytochrome c peroxidase adsorption electrode electron Geobacter metabolism Raman spectrometry thermodynamics Adsorption Bacterial Proteins Cytochromes c Electrodes Electrons Geobacter Peroxidases Spectrum Analysis, Raman Thermodynamics Geobacter sulfurreducens cells have the ability to exchange electrons with conductive materials, and the periplasmic cytochrome PccH plays an essential role in the direct electrode-to-cell electron transfer in this bacterium. It has atypically low redox potential and unique structural features that differ from those observed in other c-type cytochromes. We report surface enhanced resonance Raman spectroscopic and electrochemical characterization of the immobilized PccH, together with molecular dynamics simulations that allow for the rationalization of experimental observations. Upon attachment to electrodes functionalized with partially or fully hydrophobic self-assembled monolayers, PccH displays a distribution of native and non-native heme spin configurations, similar to those observed in horse heart cytochrome c. The native structural and thermodynamic features of PccH are preserved upon attachment mixed hydrophobic (-CH 3 /-NH 2 ) surfaces, while pure -OH, -NH 2 and -COOH surfaces do not provide suitable platforms for its adsorption, indicating that its still unknown physiological redox partner might be membrane integrated. Neither of the employed immobilization strategies results in electrocatalytically active PccH capable of the reduction of hydrogen peroxide. Pseudoperoxidase activity is observed in immobilized microperoxidase, which is enzymatically produced from PccH and spectroscopically characterized. Further improvement of PccH microperoxidase stability is required for its application in electrochemical biosensing of hydrogen peroxide. © the Owner Societies. Fil:Murgida, D.H. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2017 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_14639076_v19_n13_p8908_Silveira http://hdl.handle.net/20.500.12110/paper_14639076_v19_n13_p8908_Silveira
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic bacterial protein
cytochrome c
peroxidase
adsorption
electrode
electron
Geobacter
metabolism
Raman spectrometry
thermodynamics
Adsorption
Bacterial Proteins
Cytochromes c
Electrodes
Electrons
Geobacter
Peroxidases
Spectrum Analysis, Raman
Thermodynamics
spellingShingle bacterial protein
cytochrome c
peroxidase
adsorption
electrode
electron
Geobacter
metabolism
Raman spectrometry
thermodynamics
Adsorption
Bacterial Proteins
Cytochromes c
Electrodes
Electrons
Geobacter
Peroxidases
Spectrum Analysis, Raman
Thermodynamics
Murgida, Daniel Horacio
Structure, electrocatalysis and dynamics of immobilized cytochrome PccH and its microperoxidase
topic_facet bacterial protein
cytochrome c
peroxidase
adsorption
electrode
electron
Geobacter
metabolism
Raman spectrometry
thermodynamics
Adsorption
Bacterial Proteins
Cytochromes c
Electrodes
Electrons
Geobacter
Peroxidases
Spectrum Analysis, Raman
Thermodynamics
description Geobacter sulfurreducens cells have the ability to exchange electrons with conductive materials, and the periplasmic cytochrome PccH plays an essential role in the direct electrode-to-cell electron transfer in this bacterium. It has atypically low redox potential and unique structural features that differ from those observed in other c-type cytochromes. We report surface enhanced resonance Raman spectroscopic and electrochemical characterization of the immobilized PccH, together with molecular dynamics simulations that allow for the rationalization of experimental observations. Upon attachment to electrodes functionalized with partially or fully hydrophobic self-assembled monolayers, PccH displays a distribution of native and non-native heme spin configurations, similar to those observed in horse heart cytochrome c. The native structural and thermodynamic features of PccH are preserved upon attachment mixed hydrophobic (-CH 3 /-NH 2 ) surfaces, while pure -OH, -NH 2 and -COOH surfaces do not provide suitable platforms for its adsorption, indicating that its still unknown physiological redox partner might be membrane integrated. Neither of the employed immobilization strategies results in electrocatalytically active PccH capable of the reduction of hydrogen peroxide. Pseudoperoxidase activity is observed in immobilized microperoxidase, which is enzymatically produced from PccH and spectroscopically characterized. Further improvement of PccH microperoxidase stability is required for its application in electrochemical biosensing of hydrogen peroxide. © the Owner Societies.
author Murgida, Daniel Horacio
author_facet Murgida, Daniel Horacio
author_sort Murgida, Daniel Horacio
title Structure, electrocatalysis and dynamics of immobilized cytochrome PccH and its microperoxidase
title_short Structure, electrocatalysis and dynamics of immobilized cytochrome PccH and its microperoxidase
title_full Structure, electrocatalysis and dynamics of immobilized cytochrome PccH and its microperoxidase
title_fullStr Structure, electrocatalysis and dynamics of immobilized cytochrome PccH and its microperoxidase
title_full_unstemmed Structure, electrocatalysis and dynamics of immobilized cytochrome PccH and its microperoxidase
title_sort structure, electrocatalysis and dynamics of immobilized cytochrome pcch and its microperoxidase
publishDate 2017
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_14639076_v19_n13_p8908_Silveira
http://hdl.handle.net/20.500.12110/paper_14639076_v19_n13_p8908_Silveira
work_keys_str_mv AT murgidadanielhoracio structureelectrocatalysisanddynamicsofimmobilizedcytochromepcchanditsmicroperoxidase
_version_ 1768545803446517760

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