Generation of reactive oxygen species by hydroxypyridone compound/iron complexes.
Identifieur interne : 000116 ( Main/Exploration ); précédent : 000115; suivant : 000117Generation of reactive oxygen species by hydroxypyridone compound/iron complexes.
Auteurs : Keiko Murakami [Japon] ; Masataka Yoshino [Japon]Source :
- Redox report : communications in free radical research [ 1743-2928 ] ; 2020.
Abstract
Objectives: Prooxidant properties of iron-binding hydroxypyridone compounds including deferiprone and mimosine were analyzed. Methods: Hydroxypyridone/iron-dependent production of reactive oxygen species was evidenced by the inactivation of aconitase, the most sensitive enzyme to oxidative stress in permeabilized yeast cells. Results and Discussion: Deferiprone and mimosine produced reactive oxygen species in the presence of ferrous sulfate. The inactivation required sodium azide the inhibitor of catalase, and addition of TEMPOL, a scavenger of superoxide radical, protected aconitase from the inactivation, suggesting that the superoxide radical produced from the hydroxypyridone/iron complex is responsible for the inactivation of aconitase. A principal role of superoxide radical was further supported by the finding that the hydroxypyridone/iron complex can inactivate aconitase in the presence of cyanide the inhibitor of superoxide dismutase. Deferiprone and mimosine stimulated the Fe2+ oxidation, resulting in the one-electron reduction of oxygen to form superoxide anion, which can inactivate aconitase by oxidizing the prosthetic iron-sulfur cluster. Mimosine further stimulated the ascorbate/iron-dependent formation of 8-hydroxy-2'-deoxyguanosine in DNA. Conclusion: Biological toxicity of mimosine and deferiprone reported previously can be accounted for by the prooxidant properties of hydroxypyridone compounds: coordination complex with iron generates reactive oxygen species resulting in the disturbance of mitochondrial energy metabolism and DNA damage.
DOI: 10.1080/13510002.2020.1787662
PubMed: 32615878
PubMed Central: PMC7480593
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The inactivation required sodium azide the inhibitor of catalase, and addition of TEMPOL, a scavenger of superoxide radical, protected aconitase from the inactivation, suggesting that the superoxide radical produced from the hydroxypyridone/iron complex is responsible for the inactivation of aconitase. A principal role of superoxide radical was further supported by the finding that the hydroxypyridone/iron complex can inactivate aconitase in the presence of cyanide the inhibitor of superoxide dismutase. Deferiprone and mimosine stimulated the Fe<sup>2+</sup> oxidation, resulting in the one-electron reduction of oxygen to form superoxide anion, which can inactivate aconitase by oxidizing the prosthetic iron-sulfur cluster. Mimosine further stimulated the ascorbate/iron-dependent formation of 8-hydroxy-2'-deoxyguanosine in DNA. <b>Conclusion:</b> Biological toxicity of mimosine and deferiprone reported previously can be accounted for by the prooxidant properties of hydroxypyridone compounds: coordination complex with iron generates reactive oxygen species resulting in the disturbance of mitochondrial energy metabolism and DNA damage.</div></front></TEI><pubmed><MedlineCitation Status="In-Process" Owner="NLM"><PMID Version="1">32615878</PMID><DateRevised><Year>2020</Year><Month>09</Month><Day>17</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1743-2928</ISSN><JournalIssue CitedMedium="Internet"><Volume>25</Volume><Issue>1</Issue><PubDate><Year>2020</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Redox report : communications in free radical research</Title><ISOAbbreviation>Redox Rep</ISOAbbreviation></Journal><ArticleTitle>Generation of reactive oxygen species by hydroxypyridone compound/iron complexes.</ArticleTitle><Pagination><MedlinePgn>59-63</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1080/13510002.2020.1787662</ELocationID><Abstract><AbstractText><b>Objectives:</b> Prooxidant properties of iron-binding hydroxypyridone compounds including deferiprone and mimosine were analyzed. <b>Methods:</b> Hydroxypyridone/iron-dependent production of reactive oxygen species was evidenced by the inactivation of aconitase, the most sensitive enzyme to oxidative stress in permeabilized yeast cells. <b>Results and Discussion:</b> Deferiprone and mimosine produced reactive oxygen species in the presence of ferrous sulfate. The inactivation required sodium azide the inhibitor of catalase, and addition of TEMPOL, a scavenger of superoxide radical, protected aconitase from the inactivation, suggesting that the superoxide radical produced from the hydroxypyridone/iron complex is responsible for the inactivation of aconitase. A principal role of superoxide radical was further supported by the finding that the hydroxypyridone/iron complex can inactivate aconitase in the presence of cyanide the inhibitor of superoxide dismutase. Deferiprone and mimosine stimulated the Fe<sup>2+</sup> oxidation, resulting in the one-electron reduction of oxygen to form superoxide anion, which can inactivate aconitase by oxidizing the prosthetic iron-sulfur cluster. Mimosine further stimulated the ascorbate/iron-dependent formation of 8-hydroxy-2'-deoxyguanosine in DNA. <b>Conclusion:</b> Biological toxicity of mimosine and deferiprone reported previously can be accounted for by the prooxidant properties of hydroxypyridone compounds: coordination complex with iron generates reactive oxygen species resulting in the disturbance of mitochondrial energy metabolism and DNA damage.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Murakami</LastName><ForeName>Keiko</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, Aichi Medical University School of Medicine, Nagakute, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yoshino</LastName><ForeName>Masataka</ForeName><Initials>M</Initials><Identifier Source="ORCID">https://orcid.org/0000-0001-6497-8698</Identifier><AffiliationInfo><Affiliation>Department of Biochemistry, Aichi Medical University School of Medicine, Nagakute, Japan.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Redox Rep</MedlineTA><NlmUniqueID>9511366</NlmUniqueID><ISSNLinking>1351-0002</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">DNA damage</Keyword><Keyword MajorTopicYN="N">Hydroxypyridone</Keyword><Keyword MajorTopicYN="N">deferiprone</Keyword><Keyword MajorTopicYN="N">hydrogen peroxide</Keyword><Keyword MajorTopicYN="N">iron</Keyword><Keyword MajorTopicYN="N">mimosine</Keyword><Keyword MajorTopicYN="N">reactive oxygen species</Keyword><Keyword MajorTopicYN="N">superoxide</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate 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