An overview of the factors playing a role in cytochrome P450 monooxygenase and ferredoxin interactions.
Identifieur interne : 000174 ( Main/Exploration ); précédent : 000173; suivant : 000175An overview of the factors playing a role in cytochrome P450 monooxygenase and ferredoxin interactions.
Auteurs : Zinhle Edith Chiliza [Afrique du Sud] ; José Martínez-Oyanedel [Chili] ; Khajamohiddin Syed [Afrique du Sud]Source :
- Biophysical reviews [ 1867-2450 ] ; 2020.
Abstract
Cytochrome P450 monooxygenases (CYPs/P450s) are heme-thiolate proteins that are ubiquitously present in organisms, including non-living entities such as viruses. With the exception of self-sufficient P450s, all other P450 enzymes need electrons to perform their enzymatic activity and these electrons are supplied by P450 redox proteins. Different types of P450 redox proteins can be found in organisms and are classified into different classes. Bacterial P450s (class I) receive electrons from ferredoxins which are iron-sulfur cluster proteins. The presence of more than one copy and different types of ferredoxins within a bacterial species poses fundamental questions about the selectivity of P450s and ferredoxins in relation to each other. Apart from transferring electrons, ferredoxins have also been found to modulate P450 functions. Achieving an understanding of the interaction between ferredoxins and P450s is required to harness their biotechnological potential for designing a universal electron transfer protein. A brief overview of factors playing a role in ferredoxin and P450 interactions is presented in this review article.
DOI: 10.1007/s12551-020-00749-7
PubMed: 32885385
PubMed Central: PMC7575658
Affiliations:
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xml:lang="fr">Chili</country><wicri:regionArea>Laboratorio de Biofísica Molecular, Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias Biológicas, Universidad de Concepción, Concepción</wicri:regionArea><wicri:noRegion>Concepción</wicri:noRegion></affiliation></author><author><name sortKey="Syed, Khajamohiddin" sort="Syed, Khajamohiddin" uniqKey="Syed K" first="Khajamohiddin" last="Syed">Khajamohiddin Syed</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and Microbiology, Faculty of Science and Agriculture, University of Zululand, KwaDlangezwa, 3886, South Africa. khajamohiddinsyed@gmail.com.</nlm:affiliation><country xml:lang="fr">Afrique du Sud</country><wicri:regionArea>Department of Biochemistry and Microbiology, Faculty of Science and Agriculture, University of Zululand, KwaDlangezwa, 3886</wicri:regionArea><wicri:noRegion>3886</wicri:noRegion></affiliation></author></analytic><series><title level="j">Biophysical reviews</title><idno type="ISSN">1867-2450</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Cytochrome P450 monooxygenases (CYPs/P450s) are heme-thiolate proteins that are ubiquitously present in organisms, including non-living entities such as viruses. With the exception of self-sufficient P450s, all other P450 enzymes need electrons to perform their enzymatic activity and these electrons are supplied by P450 redox proteins. Different types of P450 redox proteins can be found in organisms and are classified into different classes. Bacterial P450s (class I) receive electrons from ferredoxins which are iron-sulfur cluster proteins. The presence of more than one copy and different types of ferredoxins within a bacterial species poses fundamental questions about the selectivity of P450s and ferredoxins in relation to each other. Apart from transferring electrons, ferredoxins have also been found to modulate P450 functions. Achieving an understanding of the interaction between ferredoxins and P450s is required to harness their biotechnological potential for designing a universal electron transfer protein. A brief overview of factors playing a role in ferredoxin and P450 interactions is presented in this review article.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">32885385</PMID><DateRevised><Year>2020</Year><Month>10</Month><Day>30</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">1867-2450</ISSN><JournalIssue CitedMedium="Print"><Volume>12</Volume><Issue>5</Issue><PubDate><Year>2020</Year><Month>Oct</Month></PubDate></JournalIssue><Title>Biophysical reviews</Title><ISOAbbreviation>Biophys Rev</ISOAbbreviation></Journal><ArticleTitle>An overview of the factors playing a role in cytochrome P450 monooxygenase and ferredoxin interactions.</ArticleTitle><Pagination><MedlinePgn>1217-1222</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s12551-020-00749-7</ELocationID><Abstract><AbstractText>Cytochrome P450 monooxygenases (CYPs/P450s) are heme-thiolate proteins that are ubiquitously present in organisms, including non-living entities such as viruses. With the exception of self-sufficient P450s, all other P450 enzymes need electrons to perform their enzymatic activity and these electrons are supplied by P450 redox proteins. Different types of P450 redox proteins can be found in organisms and are classified into different classes. Bacterial P450s (class I) receive electrons from ferredoxins which are iron-sulfur cluster proteins. The presence of more than one copy and different types of ferredoxins within a bacterial species poses fundamental questions about the selectivity of P450s and ferredoxins in relation to each other. Apart from transferring electrons, ferredoxins have also been found to modulate P450 functions. Achieving an understanding of the interaction between ferredoxins and P450s is required to harness their biotechnological potential for designing a universal electron transfer protein. A brief overview of factors playing a role in ferredoxin and P450 interactions is presented in this review article.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Chiliza</LastName><ForeName>Zinhle Edith</ForeName><Initials>ZE</Initials><Identifier Source="ORCID">https://orcid.org/0000-0001-5244-2984</Identifier><AffiliationInfo><Affiliation>Department of Biochemistry and Microbiology, Faculty of Science and Agriculture, University of Zululand, KwaDlangezwa, 3886, South Africa.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Martínez-Oyanedel</LastName><ForeName>José</ForeName><Initials>J</Initials><Identifier Source="ORCID">https://orcid.org/0000-0001-8616-7474</Identifier><AffiliationInfo><Affiliation>Laboratorio de Biofísica Molecular, Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias Biológicas, Universidad de Concepción, Concepción, Chile.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Syed</LastName><ForeName>Khajamohiddin</ForeName><Initials>K</Initials><Identifier Source="ORCID">https://orcid.org/0000-0002-1497-3570</Identifier><AffiliationInfo><Affiliation>Department of Biochemistry and Microbiology, Faculty of Science and Agriculture, University of Zululand, KwaDlangezwa, 3886, South Africa. khajamohiddinsyed@gmail.com.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>114159</GrantID><Agency>National Research Foundation</Agency><Country></Country></Grant><Grant><GrantID>117182</GrantID><Agency>National Research Foundation (ZA)</Agency><Country></Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>09</Month><Day>03</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Biophys Rev</MedlineTA><NlmUniqueID>101498573</NlmUniqueID><ISSNLinking>1867-2450</ISSNLinking></MedlineJournalInfo><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Cytochrome P450 monooxygenase</Keyword><Keyword MajorTopicYN="N">Evolution</Keyword><Keyword MajorTopicYN="N">Ferredoxins</Keyword><Keyword MajorTopicYN="N">Heme</Keyword><Keyword MajorTopicYN="N">Interactions</Keyword><Keyword MajorTopicYN="N">Iron-sulfur cluster</Keyword><Keyword MajorTopicYN="N">Redox potentials</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2020</Year><Month>06</Month><Day>09</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2020</Year><Month>08</Month><Day>28</Day></PubMedPubDate><PubMedPubDate 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