Photophysics and photochemistry of horseradish peroxidase A2 upon ultraviolet illumination
Autor(a) principal: | |
---|---|
Data de Publicação: | 2007 |
Outros Autores: | , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10400.1/11670 |
Resumo: | Detailed analysis of the effects of ultraviolet (UV) and blue light illumination of horseradish peroxidase A2, a heme-containing enzyme that reduces H2O2 to oxidize organic and inorganic compounds, is presented. The effects of increasing illumination time on the protein's enzymatic activity, Reinheitzahl value,. fluorescence emission,. fluorescence lifetime distribution,. fluorescence mean lifetime, and heme absorption are reported. UV illumination leads to an exponential decay of the enzyme activity followed by changes in heme group absorption. Longer UV illumination time leads to lower T-m values as well as helical content loss. Prolonged UV illumination and heme irradiation at 403 nm has a pronounced effect on the. fluorescence quantum yield correlated with changes in the prosthetic group pocket, leading to a pronounced decrease in the heme's Soret absorbance band. Analysis of the picosecond-resolved. fluorescence emission of horseradish peroxidase A2 with streak camera shows that UV illumination induces an exponential change in the preexponential factors distribution associated to the protein's. fluorescence lifetimes, leading to an exponential increase of the mean. fluorescence lifetime. Illumination of aromatic residues and of the heme group leads to changes indicative of heme leaving the molecule and/or that photoinduced chemical changes occur in the heme moiety. Our studies bring new insight into light-induced reactions in proteins. We show how streak camera technology can be of outstanding value to follow such ultrafast processes and how streak camera data can be correlated with protein structural changes. |
id |
RCAP_bf41b66f883646febb60e0db841f47ec |
---|---|
oai_identifier_str |
oai:sapientia.ualg.pt:10400.1/11670 |
network_acronym_str |
RCAP |
network_name_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository_id_str |
7160 |
spelling |
Photophysics and photochemistry of horseradish peroxidase A2 upon ultraviolet illuminationAromatic-Amino-AcidsCytochrome-C PeroxidaseExcited-State ChemistryUnusual Fluorescence BehaviorDilute Aqueous-SolutionTryptophan FluorescenceCircular-DichroismHydrated ElectronGlobal AnalysisInactivationDetailed analysis of the effects of ultraviolet (UV) and blue light illumination of horseradish peroxidase A2, a heme-containing enzyme that reduces H2O2 to oxidize organic and inorganic compounds, is presented. The effects of increasing illumination time on the protein's enzymatic activity, Reinheitzahl value,. fluorescence emission,. fluorescence lifetime distribution,. fluorescence mean lifetime, and heme absorption are reported. UV illumination leads to an exponential decay of the enzyme activity followed by changes in heme group absorption. Longer UV illumination time leads to lower T-m values as well as helical content loss. Prolonged UV illumination and heme irradiation at 403 nm has a pronounced effect on the. fluorescence quantum yield correlated with changes in the prosthetic group pocket, leading to a pronounced decrease in the heme's Soret absorbance band. Analysis of the picosecond-resolved. fluorescence emission of horseradish peroxidase A2 with streak camera shows that UV illumination induces an exponential change in the preexponential factors distribution associated to the protein's. fluorescence lifetimes, leading to an exponential increase of the mean. fluorescence lifetime. Illumination of aromatic residues and of the heme group leads to changes indicative of heme leaving the molecule and/or that photoinduced chemical changes occur in the heme moiety. Our studies bring new insight into light-induced reactions in proteins. We show how streak camera technology can be of outstanding value to follow such ultrafast processes and how streak camera data can be correlated with protein structural changes.Biophysical SocietySapientiaNeves-Petersen, Maria TeresaKlitgaard, SorenLeitao Carvalho, Ana SofiaPetersen, Steffen B.de Barros, Maria Raquel AiresMelo, Eduardo2018-12-07T14:53:45Z2007-032007-03-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.1/11670eng0006-349510.1529/biophysj.106.095455info: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:RCAAP2023-07-24T10:23:31Zoai:sapientia.ualg.pt:10400.1/11670Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T20:03:08.715815Repositório 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 |
Photophysics and photochemistry of horseradish peroxidase A2 upon ultraviolet illumination |
title |
Photophysics and photochemistry of horseradish peroxidase A2 upon ultraviolet illumination |
spellingShingle |
Photophysics and photochemistry of horseradish peroxidase A2 upon ultraviolet illumination Neves-Petersen, Maria Teresa Aromatic-Amino-Acids Cytochrome-C Peroxidase Excited-State Chemistry Unusual Fluorescence Behavior Dilute Aqueous-Solution Tryptophan Fluorescence Circular-Dichroism Hydrated Electron Global Analysis Inactivation |
title_short |
Photophysics and photochemistry of horseradish peroxidase A2 upon ultraviolet illumination |
title_full |
Photophysics and photochemistry of horseradish peroxidase A2 upon ultraviolet illumination |
title_fullStr |
Photophysics and photochemistry of horseradish peroxidase A2 upon ultraviolet illumination |
title_full_unstemmed |
Photophysics and photochemistry of horseradish peroxidase A2 upon ultraviolet illumination |
title_sort |
Photophysics and photochemistry of horseradish peroxidase A2 upon ultraviolet illumination |
author |
Neves-Petersen, Maria Teresa |
author_facet |
Neves-Petersen, Maria Teresa Klitgaard, Soren Leitao Carvalho, Ana Sofia Petersen, Steffen B. de Barros, Maria Raquel Aires Melo, Eduardo |
author_role |
author |
author2 |
Klitgaard, Soren Leitao Carvalho, Ana Sofia Petersen, Steffen B. de Barros, Maria Raquel Aires Melo, Eduardo |
author2_role |
author author author author author |
dc.contributor.none.fl_str_mv |
Sapientia |
dc.contributor.author.fl_str_mv |
Neves-Petersen, Maria Teresa Klitgaard, Soren Leitao Carvalho, Ana Sofia Petersen, Steffen B. de Barros, Maria Raquel Aires Melo, Eduardo |
dc.subject.por.fl_str_mv |
Aromatic-Amino-Acids Cytochrome-C Peroxidase Excited-State Chemistry Unusual Fluorescence Behavior Dilute Aqueous-Solution Tryptophan Fluorescence Circular-Dichroism Hydrated Electron Global Analysis Inactivation |
topic |
Aromatic-Amino-Acids Cytochrome-C Peroxidase Excited-State Chemistry Unusual Fluorescence Behavior Dilute Aqueous-Solution Tryptophan Fluorescence Circular-Dichroism Hydrated Electron Global Analysis Inactivation |
description |
Detailed analysis of the effects of ultraviolet (UV) and blue light illumination of horseradish peroxidase A2, a heme-containing enzyme that reduces H2O2 to oxidize organic and inorganic compounds, is presented. The effects of increasing illumination time on the protein's enzymatic activity, Reinheitzahl value,. fluorescence emission,. fluorescence lifetime distribution,. fluorescence mean lifetime, and heme absorption are reported. UV illumination leads to an exponential decay of the enzyme activity followed by changes in heme group absorption. Longer UV illumination time leads to lower T-m values as well as helical content loss. Prolonged UV illumination and heme irradiation at 403 nm has a pronounced effect on the. fluorescence quantum yield correlated with changes in the prosthetic group pocket, leading to a pronounced decrease in the heme's Soret absorbance band. Analysis of the picosecond-resolved. fluorescence emission of horseradish peroxidase A2 with streak camera shows that UV illumination induces an exponential change in the preexponential factors distribution associated to the protein's. fluorescence lifetimes, leading to an exponential increase of the mean. fluorescence lifetime. Illumination of aromatic residues and of the heme group leads to changes indicative of heme leaving the molecule and/or that photoinduced chemical changes occur in the heme moiety. Our studies bring new insight into light-induced reactions in proteins. We show how streak camera technology can be of outstanding value to follow such ultrafast processes and how streak camera data can be correlated with protein structural changes. |
publishDate |
2007 |
dc.date.none.fl_str_mv |
2007-03 2007-03-01T00:00:00Z 2018-12-07T14:53:45Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10400.1/11670 |
url |
http://hdl.handle.net/10400.1/11670 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
0006-3495 10.1529/biophysj.106.095455 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
Biophysical Society |
publisher.none.fl_str_mv |
Biophysical Society |
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 |
instname_str |
Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
instacron_str |
RCAAP |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository.name.fl_str_mv |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
repository.mail.fl_str_mv |
|
_version_ |
1799133265354817536 |