Human nitrobindin: the first example of an all-β-barrel ferric heme-protein that catalyzes peroxynitrite detoxification
Nitrobindins (Nbs), constituting a heme-protein family spanning from bacteria to Homo sapiens, display an all-β-barrel structural organization. Human Nb has been described as a domain of the nuclear protein named THAP4, whose physiological function is still unknown. We report the first evidence of t...
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ftunivroma3iris:oai:iris.uniroma3.it:11590/345568 2024-09-15T18:37:34+00:00 Human nitrobindin: the first example of an all-β-barrel ferric heme-protein that catalyzes peroxynitrite detoxification De Simone, Giovanna di Masi, Alessandra Polticelli, Fabio Ascenzi, Paolo De Simone, Giovanna di Masi, Alessandra Polticelli, Fabio Ascenzi, Paolo 2018 http://hdl.handle.net/11590/345568 https://doi.org/10.1002/2211-5463.12534 http://www.elsevier.com/wps/find/journaldescription.cws_home/726807/description#description eng eng info:eu-repo/semantics/altIdentifier/wos/WOS:000451855500011 volume:8 issue:12 firstpage:2002 lastpage:2010 numberofpages:9 journal:FEBS OPENBIO http://hdl.handle.net/11590/345568 doi:10.1002/2211-5463.12534 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-85056326576 http://www.elsevier.com/wps/find/journaldescription.cws_home/726807/description#description human nitrobindin kinetic peroxynitrite scavenging protection of l-tyrosine nitration Biochemistry Genetics and Molecular Biology (all) info:eu-repo/semantics/article 2018 ftunivroma3iris https://doi.org/10.1002/2211-5463.12534 2024-06-26T23:32:06Z Nitrobindins (Nbs), constituting a heme-protein family spanning from bacteria to Homo sapiens, display an all-β-barrel structural organization. Human Nb has been described as a domain of the nuclear protein named THAP4, whose physiological function is still unknown. We report the first evidence of the heme-Fe(III)-based detoxification of peroxynitrite by the all-β-barrel C-terminal Nb-like domain of THAP4. Ferric human Nb (Nb(III)) catalyzes the conversion of peroxynitrite to (Formula presented.) and impairs the nitration of free l-tyrosine. The rate of human Nb(III)-mediated scavenging of peroxynitrite is similar to those of all-α-helical horse heart and sperm whale myoglobin and human hemoglobin, generally taken as the prototypes of all-α-helical heme-proteins. The heme-Fe(III) reactivity of all-β-barrel human Nb(III) and all-α-helical prototypical heme-proteins possibly reflects the out-to-in-plane transition of the heme-Fe(III)-atom preceding peroxynitrite binding. Human Nb(III) not only catalyzes the detoxification of peroxynitrite but also binds NO, possibly representing a target of reactive nitrogen species. Article in Journal/Newspaper Sperm whale Anagrafe della Ricerca d'Ateneo (Universitá degli studi Roma Tre) FEBS Open Bio 8 12 2002 2010 |
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Open Polar |
collection |
Anagrafe della Ricerca d'Ateneo (Universitá degli studi Roma Tre) |
op_collection_id |
ftunivroma3iris |
language |
English |
topic |
human nitrobindin kinetic peroxynitrite scavenging protection of l-tyrosine nitration Biochemistry Genetics and Molecular Biology (all) |
spellingShingle |
human nitrobindin kinetic peroxynitrite scavenging protection of l-tyrosine nitration Biochemistry Genetics and Molecular Biology (all) De Simone, Giovanna di Masi, Alessandra Polticelli, Fabio Ascenzi, Paolo Human nitrobindin: the first example of an all-β-barrel ferric heme-protein that catalyzes peroxynitrite detoxification |
topic_facet |
human nitrobindin kinetic peroxynitrite scavenging protection of l-tyrosine nitration Biochemistry Genetics and Molecular Biology (all) |
description |
Nitrobindins (Nbs), constituting a heme-protein family spanning from bacteria to Homo sapiens, display an all-β-barrel structural organization. Human Nb has been described as a domain of the nuclear protein named THAP4, whose physiological function is still unknown. We report the first evidence of the heme-Fe(III)-based detoxification of peroxynitrite by the all-β-barrel C-terminal Nb-like domain of THAP4. Ferric human Nb (Nb(III)) catalyzes the conversion of peroxynitrite to (Formula presented.) and impairs the nitration of free l-tyrosine. The rate of human Nb(III)-mediated scavenging of peroxynitrite is similar to those of all-α-helical horse heart and sperm whale myoglobin and human hemoglobin, generally taken as the prototypes of all-α-helical heme-proteins. The heme-Fe(III) reactivity of all-β-barrel human Nb(III) and all-α-helical prototypical heme-proteins possibly reflects the out-to-in-plane transition of the heme-Fe(III)-atom preceding peroxynitrite binding. Human Nb(III) not only catalyzes the detoxification of peroxynitrite but also binds NO, possibly representing a target of reactive nitrogen species. |
author2 |
De Simone, Giovanna di Masi, Alessandra Polticelli, Fabio Ascenzi, Paolo |
format |
Article in Journal/Newspaper |
author |
De Simone, Giovanna di Masi, Alessandra Polticelli, Fabio Ascenzi, Paolo |
author_facet |
De Simone, Giovanna di Masi, Alessandra Polticelli, Fabio Ascenzi, Paolo |
author_sort |
De Simone, Giovanna |
title |
Human nitrobindin: the first example of an all-β-barrel ferric heme-protein that catalyzes peroxynitrite detoxification |
title_short |
Human nitrobindin: the first example of an all-β-barrel ferric heme-protein that catalyzes peroxynitrite detoxification |
title_full |
Human nitrobindin: the first example of an all-β-barrel ferric heme-protein that catalyzes peroxynitrite detoxification |
title_fullStr |
Human nitrobindin: the first example of an all-β-barrel ferric heme-protein that catalyzes peroxynitrite detoxification |
title_full_unstemmed |
Human nitrobindin: the first example of an all-β-barrel ferric heme-protein that catalyzes peroxynitrite detoxification |
title_sort |
human nitrobindin: the first example of an all-β-barrel ferric heme-protein that catalyzes peroxynitrite detoxification |
publishDate |
2018 |
url |
http://hdl.handle.net/11590/345568 https://doi.org/10.1002/2211-5463.12534 http://www.elsevier.com/wps/find/journaldescription.cws_home/726807/description#description |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_relation |
info:eu-repo/semantics/altIdentifier/wos/WOS:000451855500011 volume:8 issue:12 firstpage:2002 lastpage:2010 numberofpages:9 journal:FEBS OPENBIO http://hdl.handle.net/11590/345568 doi:10.1002/2211-5463.12534 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-85056326576 http://www.elsevier.com/wps/find/journaldescription.cws_home/726807/description#description |
op_doi |
https://doi.org/10.1002/2211-5463.12534 |
container_title |
FEBS Open Bio |
container_volume |
8 |
container_issue |
12 |
container_start_page |
2002 |
op_container_end_page |
2010 |
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1810481945570705408 |