Electron transfer dynamics of Rhodothermus marinus caa 3 cytochrome c domains on biomimetic films
The subunit II of the caa 3 oxygen reductase from Rhodothermus marinus contains, in addition to the Cu A center, a c-type heme group in the cytochrome c domain (Cyt-D) that is the putative primary electron acceptor of the enzyme. In this work we have combined surface-enhanced resonance Raman (SERR)...
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2011
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Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_14639076_v13_n40_p18088_Molinas http://hdl.handle.net/20.500.12110/paper_14639076_v13_n40_p18088_Molinas |
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paper:paper_14639076_v13_n40_p18088_Molinas2023-06-08T16:16:23Z Electron transfer dynamics of Rhodothermus marinus caa 3 cytochrome c domains on biomimetic films Molinas, Maria Florencia De Candia, Ariel Gustavo Szajnman, Sergio Hernán Rodríguez, Juan Bautista Martí, Marcelo Adrián Murgida, Daniel Horacio cytochrome a cytochrome c cytochrome c oxidase cytochrome caa(3) article chemistry electron transport enzymology metabolism molecular dynamics protein subunit protein tertiary structure Raman spectrometry Rhodothermus Cytochrome c Group Cytochromes a Cytochromes a3 Electron Transport Molecular Dynamics Simulation Protein Structure, Tertiary Protein Subunits Rhodothermus Spectrum Analysis, Raman The subunit II of the caa 3 oxygen reductase from Rhodothermus marinus contains, in addition to the Cu A center, a c-type heme group in the cytochrome c domain (Cyt-D) that is the putative primary electron acceptor of the enzyme. In this work we have combined surface-enhanced resonance Raman (SERR) spectroelectrochemistry, molecular dynamics (MD) simulations and electron pathway calculations to assess the most likely interaction domains and electron entry/exit points of the truncated Cyt-D of subunit II in the reactions with its electron donor, HiPIP and electron acceptor, Cu A. The results indicate that the transient interaction between Cyt-D and HiPIP relies upon a delicate balance of hydrophobic and polar contacts for establishing an optimized electron transfer pathway that involves the exposed edge of the heme group and guaranties efficient inter-protein electron transfer on the nanosecond time scale. The reorganization energy of ca. 0.7 eV was determined by time-resolved SERR spectroelectrochemistry. The intramolecular electron transfer pathway in integral subunit II from Cyt-D to the Cu A redox center most likely involves the iron ligand histidine 20 as an electron exit point in Cyt-D. © the Owner Societies 2011. Fil:Molinas, M.F. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:De Candia, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Szajnman, S.H. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Rodríguez, J.B. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Martí, M. 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. 2011 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_14639076_v13_n40_p18088_Molinas http://hdl.handle.net/20.500.12110/paper_14639076_v13_n40_p18088_Molinas |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
cytochrome a cytochrome c cytochrome c oxidase cytochrome caa(3) article chemistry electron transport enzymology metabolism molecular dynamics protein subunit protein tertiary structure Raman spectrometry Rhodothermus Cytochrome c Group Cytochromes a Cytochromes a3 Electron Transport Molecular Dynamics Simulation Protein Structure, Tertiary Protein Subunits Rhodothermus Spectrum Analysis, Raman |
spellingShingle |
cytochrome a cytochrome c cytochrome c oxidase cytochrome caa(3) article chemistry electron transport enzymology metabolism molecular dynamics protein subunit protein tertiary structure Raman spectrometry Rhodothermus Cytochrome c Group Cytochromes a Cytochromes a3 Electron Transport Molecular Dynamics Simulation Protein Structure, Tertiary Protein Subunits Rhodothermus Spectrum Analysis, Raman Molinas, Maria Florencia De Candia, Ariel Gustavo Szajnman, Sergio Hernán Rodríguez, Juan Bautista Martí, Marcelo Adrián Murgida, Daniel Horacio Electron transfer dynamics of Rhodothermus marinus caa 3 cytochrome c domains on biomimetic films |
topic_facet |
cytochrome a cytochrome c cytochrome c oxidase cytochrome caa(3) article chemistry electron transport enzymology metabolism molecular dynamics protein subunit protein tertiary structure Raman spectrometry Rhodothermus Cytochrome c Group Cytochromes a Cytochromes a3 Electron Transport Molecular Dynamics Simulation Protein Structure, Tertiary Protein Subunits Rhodothermus Spectrum Analysis, Raman |
description |
The subunit II of the caa 3 oxygen reductase from Rhodothermus marinus contains, in addition to the Cu A center, a c-type heme group in the cytochrome c domain (Cyt-D) that is the putative primary electron acceptor of the enzyme. In this work we have combined surface-enhanced resonance Raman (SERR) spectroelectrochemistry, molecular dynamics (MD) simulations and electron pathway calculations to assess the most likely interaction domains and electron entry/exit points of the truncated Cyt-D of subunit II in the reactions with its electron donor, HiPIP and electron acceptor, Cu A. The results indicate that the transient interaction between Cyt-D and HiPIP relies upon a delicate balance of hydrophobic and polar contacts for establishing an optimized electron transfer pathway that involves the exposed edge of the heme group and guaranties efficient inter-protein electron transfer on the nanosecond time scale. The reorganization energy of ca. 0.7 eV was determined by time-resolved SERR spectroelectrochemistry. The intramolecular electron transfer pathway in integral subunit II from Cyt-D to the Cu A redox center most likely involves the iron ligand histidine 20 as an electron exit point in Cyt-D. © the Owner Societies 2011. |
author |
Molinas, Maria Florencia De Candia, Ariel Gustavo Szajnman, Sergio Hernán Rodríguez, Juan Bautista Martí, Marcelo Adrián Murgida, Daniel Horacio |
author_facet |
Molinas, Maria Florencia De Candia, Ariel Gustavo Szajnman, Sergio Hernán Rodríguez, Juan Bautista Martí, Marcelo Adrián Murgida, Daniel Horacio |
author_sort |
Molinas, Maria Florencia |
title |
Electron transfer dynamics of Rhodothermus marinus caa 3 cytochrome c domains on biomimetic films |
title_short |
Electron transfer dynamics of Rhodothermus marinus caa 3 cytochrome c domains on biomimetic films |
title_full |
Electron transfer dynamics of Rhodothermus marinus caa 3 cytochrome c domains on biomimetic films |
title_fullStr |
Electron transfer dynamics of Rhodothermus marinus caa 3 cytochrome c domains on biomimetic films |
title_full_unstemmed |
Electron transfer dynamics of Rhodothermus marinus caa 3 cytochrome c domains on biomimetic films |
title_sort |
electron transfer dynamics of rhodothermus marinus caa 3 cytochrome c domains on biomimetic films |
publishDate |
2011 |
url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_14639076_v13_n40_p18088_Molinas http://hdl.handle.net/20.500.12110/paper_14639076_v13_n40_p18088_Molinas |
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