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

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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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Autor principal: Silveira, C.M
Otros Autores: Castro, M.A, Dantas, J.M, Salgueiro, C., Murgida, D.H, Todorovic, S.
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: Royal Society of Chemistry 2017
Acceso en línea:Registro en Scopus
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Biblioteca Central Dr. Luis F. Leloir (FCEN) de Universidad de Buenos Aires
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024 7 |2 cas  |a cytochrome c, 9007-43-6, 9064-84-0; peroxidase, 9003-99-0; Bacterial Proteins; Cytochromes c; microperoxidase; Peroxidases 
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100 1 |a Silveira, C.M. 
245 1 0 |a Structure, electrocatalysis and dynamics of immobilized cytochrome PccH and its microperoxidase 
260 |b Royal Society of Chemistry  |c 2017 
270 1 0 |m Silveira, C.M.; Instituto de Tecnologia Química e Biológica António Xavier, Universidade NOVA de Lisboa, Av. da República, Portugal; email: celiasilveira@itqb.unl.pt 
506 |2 openaire  |e Política editorial 
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520 3 |a 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.  |l eng 
536 |a Detalles de la financiación: Canadian Anesthesiologists' Society, SFRH/BD/89701/2012, UID/Multi/04378/2013 
536 |a Detalles de la financiación: Secretaría de Ciencia y Técnica, Universidad de Buenos Aires, 20020130100206BA 
536 |a Detalles de la financiación: SFRH/BPD/ 79566/2011, CMS, PTDC/ BBB-BQB/3554/2014, IF/00710/2014 
536 |a Detalles de la financiación: Fundação para a Ciência e a Tecnologia 
536 |a Detalles de la financiación: Manitoba Arts Council 
536 |a Detalles de la financiación: POCI, COMPETE2020 
536 |a Detalles de la financiación: Agencia Nacional de Promoción Científica y Tecnológica, PICT2011-1249, PICT2015-133 
536 |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas 
536 |a Detalles de la financiación: MS data were provided by the UniMS - Mass Spectrometry Unit, ITQB/iBET, Oeiras, Portugal. This work was financially supported by: Project LISBOA-01-0145-FEDER-007660 (Microbiologia Molecular, Estrutural e Celular) funded by FEDER funds through COMPETE2020 - Programa Operacional Competitividade e Internacionaliza?a ?o (POCI) and by national funds through FCT - Funda?a?o para a Ci?ncia e a Tecnologia, which ST and CMS acknowledge, together with IF/00710/2014 (ST) and SFRH/BPD/ 79566/2011 (CMS). This work was also supported by grants PTDC/ BBB-BQB/3554/2014 (to CAS), SFRH/BD/89701/2012 (to JMD) and UID/Multi/04378/2013 from Funda?a?o para a Ci?ncia e a Tecnologia. DHM thanks the financial support from ANPCyT (PICT2015-133; PICT2011-1249) and UBACYT (20020130100206BA). MAC and DHM are staff members of CONICET. 
593 |a Instituto de Tecnologia Química e Biológica António Xavier, Universidade NOVA de Lisboa, Av. da República, Oeiras, 2780-157, Portugal 
593 |a UCIBIO, REQUIMTE, Faculdade de Ciências e Tecnologia, Universidade NOVA de Lisboa, Monte de Caparica, 2829-516, Portugal 
593 |a Departamento de Química Inorgánica, Analítica y Química Física, INQUIMAE (CONICET-UBA), Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Argentina 
690 1 0 |a BACTERIAL PROTEIN 
690 1 0 |a CYTOCHROME C 
690 1 0 |a PEROXIDASE 
690 1 0 |a ADSORPTION 
690 1 0 |a ELECTRODE 
690 1 0 |a ELECTRON 
690 1 0 |a GEOBACTER 
690 1 0 |a METABOLISM 
690 1 0 |a RAMAN SPECTROMETRY 
690 1 0 |a THERMODYNAMICS 
690 1 0 |a ADSORPTION 
690 1 0 |a BACTERIAL PROTEINS 
690 1 0 |a CYTOCHROMES C 
690 1 0 |a ELECTRODES 
690 1 0 |a ELECTRONS 
690 1 0 |a GEOBACTER 
690 1 0 |a PEROXIDASES 
690 1 0 |a SPECTRUM ANALYSIS, RAMAN 
690 1 0 |a THERMODYNAMICS 
700 1 |a Castro, M.A. 
700 1 |a Dantas, J.M. 
700 1 |a Salgueiro, C. 
700 1 |a Murgida, D.H. 
700 1 |a Todorovic, S. 
773 0 |d Royal Society of Chemistry, 2017  |g v. 19  |h pp. 8908-8918  |k n. 13  |p Phys. Chem. Chem. Phys.  |x 14639076  |t Physical Chemistry Chemical Physics 
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