Thermodynamic and kinetic characterization of trihaem cytochrome c3 from Desulfuromonas acetoxidans
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Publication Date: | 2002 |
Other Authors: | , , , , |
Format: | Article |
Language: | eng |
Source: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Download full: | http://hdl.handle.net/10400.6/4617 |
Summary: | Trihaem cytochrome c3 (also known as cytochrome c551.5 and cytochrome c7) is isolated from the periplasmic space of Desulfuromonas acetoxidans, a sulfur-reducing bacterium. Thermodynamic and kinetic data for the trihaem cytochrome c3 are presented and discussed in the context of the possible physiological implications of its functional properties with respect to the natural habitat of D. acetoxidans, namely as a symbiont with green sulfur bacteria working as a mini-sulfuretum. The thermodynamic properties were determined through the fit of redox titration data, followed by NMR and visible spectroscopy, to a model of four functional centres that describes the network of cooperativities between the three haems and one protolytic centre. The kinetics of trihaem cytochrome c3 reduction by sodium dithionite were studied using the stopped-flow technique and the data were fitted to a kinetic model that makes use of the thermodynamic properties to obtain the rate constants of the individual haems. This analysis indicates that the electrons enter the cytochrome mainly via haem I. The reduction potentials of the haems in this cytochrome show little variation with pH within the physiological range, and the kinetic studies show that the rates of reduction are also independent of pH in the range studied. Thus, although the trihaem cytochrome c3 is readily reduced by hydrogenases from Desulfovibrio sp. and its haem core is similar to that of the homologous tetrahaem cytochromes c3, its physico-chemical properties are quite different, which suggests that these multihaem cytochromes with similar structures perform different functions. |
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Thermodynamic and kinetic characterization of trihaem cytochrome c3 from Desulfuromonas acetoxidansCytochrome c7Multihaem cytochromesRedox proteinsThermodynamic and kinetic propertiesTrihaem cytochrome c3Trihaem cytochrome c3 (also known as cytochrome c551.5 and cytochrome c7) is isolated from the periplasmic space of Desulfuromonas acetoxidans, a sulfur-reducing bacterium. Thermodynamic and kinetic data for the trihaem cytochrome c3 are presented and discussed in the context of the possible physiological implications of its functional properties with respect to the natural habitat of D. acetoxidans, namely as a symbiont with green sulfur bacteria working as a mini-sulfuretum. The thermodynamic properties were determined through the fit of redox titration data, followed by NMR and visible spectroscopy, to a model of four functional centres that describes the network of cooperativities between the three haems and one protolytic centre. The kinetics of trihaem cytochrome c3 reduction by sodium dithionite were studied using the stopped-flow technique and the data were fitted to a kinetic model that makes use of the thermodynamic properties to obtain the rate constants of the individual haems. This analysis indicates that the electrons enter the cytochrome mainly via haem I. The reduction potentials of the haems in this cytochrome show little variation with pH within the physiological range, and the kinetic studies show that the rates of reduction are also independent of pH in the range studied. Thus, although the trihaem cytochrome c3 is readily reduced by hydrogenases from Desulfovibrio sp. and its haem core is similar to that of the homologous tetrahaem cytochromes c3, its physico-chemical properties are quite different, which suggests that these multihaem cytochromes with similar structures perform different functions.WILEYuBibliorumCorreia, Ilídio Joaquim SobreiraPaquete, CatarinaLouro, RicardoCatarino, TeresaTurner, DavidXavier, António2018-03-15T09:14:04Z2002-10-282002-10-28T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.6/4617engCorreia, I.J., Paquete, C.M., Louro, R.O., Catarino, T., Turner, D.L. e Xavier, A.V. (2002) “Thermodynamic and kinetic characterisation of trihaem cytochrome c3 from Desulfuromonas acetoxidans”, European Journal of Biochemistry (FEBS Journal), Vol. 269(22), pp. 5722-573010.1046/j.1432-1033.2002.03286.xmetadata only accessinfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-12-15T09:41:41Zoai:ubibliorum.ubi.pt:10400.6/4617Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T00:45:40.858417Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
Thermodynamic and kinetic characterization of trihaem cytochrome c3 from Desulfuromonas acetoxidans |
title |
Thermodynamic and kinetic characterization of trihaem cytochrome c3 from Desulfuromonas acetoxidans |
spellingShingle |
Thermodynamic and kinetic characterization of trihaem cytochrome c3 from Desulfuromonas acetoxidans Correia, Ilídio Joaquim Sobreira Cytochrome c7 Multihaem cytochromes Redox proteins Thermodynamic and kinetic properties Trihaem cytochrome c3 |
title_short |
Thermodynamic and kinetic characterization of trihaem cytochrome c3 from Desulfuromonas acetoxidans |
title_full |
Thermodynamic and kinetic characterization of trihaem cytochrome c3 from Desulfuromonas acetoxidans |
title_fullStr |
Thermodynamic and kinetic characterization of trihaem cytochrome c3 from Desulfuromonas acetoxidans |
title_full_unstemmed |
Thermodynamic and kinetic characterization of trihaem cytochrome c3 from Desulfuromonas acetoxidans |
title_sort |
Thermodynamic and kinetic characterization of trihaem cytochrome c3 from Desulfuromonas acetoxidans |
author |
Correia, Ilídio Joaquim Sobreira |
author_facet |
Correia, Ilídio Joaquim Sobreira Paquete, Catarina Louro, Ricardo Catarino, Teresa Turner, David Xavier, António |
author_role |
author |
author2 |
Paquete, Catarina Louro, Ricardo Catarino, Teresa Turner, David Xavier, António |
author2_role |
author author author author author |
dc.contributor.none.fl_str_mv |
uBibliorum |
dc.contributor.author.fl_str_mv |
Correia, Ilídio Joaquim Sobreira Paquete, Catarina Louro, Ricardo Catarino, Teresa Turner, David Xavier, António |
dc.subject.por.fl_str_mv |
Cytochrome c7 Multihaem cytochromes Redox proteins Thermodynamic and kinetic properties Trihaem cytochrome c3 |
topic |
Cytochrome c7 Multihaem cytochromes Redox proteins Thermodynamic and kinetic properties Trihaem cytochrome c3 |
description |
Trihaem cytochrome c3 (also known as cytochrome c551.5 and cytochrome c7) is isolated from the periplasmic space of Desulfuromonas acetoxidans, a sulfur-reducing bacterium. Thermodynamic and kinetic data for the trihaem cytochrome c3 are presented and discussed in the context of the possible physiological implications of its functional properties with respect to the natural habitat of D. acetoxidans, namely as a symbiont with green sulfur bacteria working as a mini-sulfuretum. The thermodynamic properties were determined through the fit of redox titration data, followed by NMR and visible spectroscopy, to a model of four functional centres that describes the network of cooperativities between the three haems and one protolytic centre. The kinetics of trihaem cytochrome c3 reduction by sodium dithionite were studied using the stopped-flow technique and the data were fitted to a kinetic model that makes use of the thermodynamic properties to obtain the rate constants of the individual haems. This analysis indicates that the electrons enter the cytochrome mainly via haem I. The reduction potentials of the haems in this cytochrome show little variation with pH within the physiological range, and the kinetic studies show that the rates of reduction are also independent of pH in the range studied. Thus, although the trihaem cytochrome c3 is readily reduced by hydrogenases from Desulfovibrio sp. and its haem core is similar to that of the homologous tetrahaem cytochromes c3, its physico-chemical properties are quite different, which suggests that these multihaem cytochromes with similar structures perform different functions. |
publishDate |
2002 |
dc.date.none.fl_str_mv |
2002-10-28 2002-10-28T00:00:00Z 2018-03-15T09:14:04Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
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publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10400.6/4617 |
url |
http://hdl.handle.net/10400.6/4617 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Correia, I.J., Paquete, C.M., Louro, R.O., Catarino, T., Turner, D.L. e Xavier, A.V. (2002) “Thermodynamic and kinetic characterisation of trihaem cytochrome c3 from Desulfuromonas acetoxidans”, European Journal of Biochemistry (FEBS Journal), Vol. 269(22), pp. 5722-5730 10.1046/j.1432-1033.2002.03286.x |
dc.rights.driver.fl_str_mv |
metadata only access info:eu-repo/semantics/openAccess |
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metadata only access |
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openAccess |
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application/pdf |
dc.publisher.none.fl_str_mv |
WILEY |
publisher.none.fl_str_mv |
WILEY |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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