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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Autores principales: Molinas, M.F., De Candia, A., Szajnman, S.H., Rodríguez, J.B., Martí, M., Pereira, M., Teixeira, M., Todorovic, S., Murgida, D.H.
Formato: JOUR
Materias:
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
Spectrum Analysis, Raman
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_14639076_v13_n40_p18088_Molinas
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
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spelling todo:paper_14639076_v13_n40_p18088_Molinas2023-10-03T16:16:45Z Electron transfer dynamics of Rhodothermus marinus caa 3 cytochrome c domains on biomimetic films Molinas, M.F. De Candia, A. Szajnman, S.H. Rodríguez, J.B. Martí, M. Pereira, M. Teixeira, M. Todorovic, S. Murgida, D.H. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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, M.F.
De Candia, A.
Szajnman, S.H.
Rodríguez, J.B.
Martí, M.
Pereira, M.
Teixeira, M.
Todorovic, S.
Murgida, D.H.
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.
format JOUR
author Molinas, M.F.
De Candia, A.
Szajnman, S.H.
Rodríguez, J.B.
Martí, M.
Pereira, M.
Teixeira, M.
Todorovic, S.
Murgida, D.H.
author_facet Molinas, M.F.
De Candia, A.
Szajnman, S.H.
Rodríguez, J.B.
Martí, M.
Pereira, M.
Teixeira, M.
Todorovic, S.
Murgida, D.H.
author_sort Molinas, M.F.
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
url http://hdl.handle.net/20.500.12110/paper_14639076_v13_n40_p18088_Molinas
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