Unusual semiquinone as an electron buffer in enzymatic quinone oxidation
Identifieur interne : 000003 ( Main/Exploration ); précédent : 000002; suivant : 000004Unusual semiquinone as an electron buffer in enzymatic quinone oxidation
Auteurs : Łukasz Bujnowicz [Pologne] ; Marcin Sarewicz [Pologne] ; Artur Osyczka [Pologne]Source :
- Postepy biochemii [ 0032-5422 ] ; 2020.
Descripteurs français
- KwdFr :
- MESH :
- composition chimique : Benzoquinones.
- métabolisme : Benzoquinones, Cytochromes, Superoxydes.
- Oxydoréduction, Transport d'électrons, Électrons.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Benzoquinones.
- chemical , metabolism : Benzoquinones, Cytochromes, Superoxides.
- Electron Transport, Electrons, Oxidation-Reduction.
Abstract
Cytochromes bc1 and c b6f are part of respiratory or photosynthetic machinery. The main role of these enzymes is to build proton motive force across the bioenergetic membranes by coupling the proton translocations with electron transfer from the pool of membrane-soluble quinones to water-soluble redox proteins. Despite many years of research, the mechanism of quinol oxidation is not fully understood. It is assumed that unstable form of a partially oxidized quinol – semiquinone is an intermediate state of this process and that it is also a potential electron donor in the side reaction of superoxide generation. This semiquinone has remained experimentally elusive over years but recently a semiquinone interacting with the reduced iron-sulfur cluster was identified as a new state of the enzyme. The results indicate that semiquinone coupled to the iron-sulfur cluster is most probably an additional state that can prevent side reactions, including superoxide generation.
DOI: 10.18388/pb.2020_326
PubMed: 32700506
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Unusual semiquinone as an electron buffer in enzymatic quinone oxidation</title><author><name sortKey="Bujnowicz, Lukasz" sort="Bujnowicz, Lukasz" uniqKey="Bujnowicz L" first="Łukasz" last="Bujnowicz">Łukasz Bujnowicz</name><affiliation wicri:level="1"><nlm:affiliation>Zakład Biofizyki Molekularnej; Wydział Biochemii, Biofizyki i Biotechnologii Uniwersytetu Jagiellońskiego w Krakowie. lukasz.bujnowicz@uj.edu.pl.</nlm:affiliation><country wicri:rule="url">Pologne</country></affiliation></author><author><name sortKey="Sarewicz, Marcin" sort="Sarewicz, Marcin" uniqKey="Sarewicz M" first="Marcin" last="Sarewicz">Marcin Sarewicz</name><affiliation wicri:level="1"><nlm:affiliation>Zakład Biofizyki Molekularnej; Wydział Biochemii, Biofizyki i Biotechnologii; Uniwersytet Jagielloński, Kraków. artur.osyczka@uj.edu.pl.</nlm:affiliation><country wicri:rule="url">Pologne</country></affiliation></author><author><name sortKey="Osyczka, Artur" sort="Osyczka, Artur" uniqKey="Osyczka A" first="Artur" last="Osyczka">Artur Osyczka</name><affiliation wicri:level="1"><nlm:affiliation>Zakład Biofizyki Molekularnej; Wydział Biochemii, Biofizyki i Biotechnologii; Uniwersytet Jagielloński, Kraków. artur.osyczka@uj.edu.pl.</nlm:affiliation><country wicri:rule="url">Pologne</country></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2020">2020</date><idno type="RBID">pubmed:32700506</idno><idno type="pmid">32700506</idno><idno type="doi">10.18388/pb.2020_326</idno><idno type="wicri:Area/Main/Corpus">000057</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000057</idno><idno type="wicri:Area/Main/Curation">000057</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000057</idno><idno type="wicri:Area/Main/Exploration">000057</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Unusual semiquinone as an electron buffer in enzymatic quinone oxidation</title><author><name sortKey="Bujnowicz, Lukasz" sort="Bujnowicz, Lukasz" uniqKey="Bujnowicz L" first="Łukasz" last="Bujnowicz">Łukasz Bujnowicz</name><affiliation wicri:level="1"><nlm:affiliation>Zakład Biofizyki Molekularnej; Wydział Biochemii, Biofizyki i Biotechnologii Uniwersytetu Jagiellońskiego w Krakowie. lukasz.bujnowicz@uj.edu.pl.</nlm:affiliation><country wicri:rule="url">Pologne</country></affiliation></author><author><name sortKey="Sarewicz, Marcin" sort="Sarewicz, Marcin" uniqKey="Sarewicz M" first="Marcin" last="Sarewicz">Marcin Sarewicz</name><affiliation wicri:level="1"><nlm:affiliation>Zakład Biofizyki Molekularnej; Wydział Biochemii, Biofizyki i Biotechnologii; Uniwersytet Jagielloński, Kraków. artur.osyczka@uj.edu.pl.</nlm:affiliation><country wicri:rule="url">Pologne</country></affiliation></author><author><name sortKey="Osyczka, Artur" sort="Osyczka, Artur" uniqKey="Osyczka A" first="Artur" last="Osyczka">Artur Osyczka</name><affiliation wicri:level="1"><nlm:affiliation>Zakład Biofizyki Molekularnej; Wydział Biochemii, Biofizyki i Biotechnologii; Uniwersytet Jagielloński, Kraków. artur.osyczka@uj.edu.pl.</nlm:affiliation><country wicri:rule="url">Pologne</country></affiliation></author></analytic><series><title level="j">Postepy biochemii</title><idno type="ISSN">0032-5422</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Benzoquinones (chemistry)</term><term>Benzoquinones (metabolism)</term><term>Cytochromes (metabolism)</term><term>Electron Transport (MeSH)</term><term>Electrons (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Superoxides (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Benzoquinones (composition chimique)</term><term>Benzoquinones (métabolisme)</term><term>Cytochromes (métabolisme)</term><term>Oxydoréduction (MeSH)</term><term>Superoxydes (métabolisme)</term><term>Transport d'électrons (MeSH)</term><term>Électrons (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Benzoquinones</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Benzoquinones</term><term>Cytochromes</term><term>Superoxides</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Benzoquinones</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Benzoquinones</term><term>Cytochromes</term><term>Superoxydes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Electron Transport</term><term>Electrons</term><term>Oxidation-Reduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Oxydoréduction</term><term>Transport d'électrons</term><term>Électrons</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Cytochromes bc1 and c b6f are part of respiratory or photosynthetic machinery. The main role of these enzymes is to build proton motive force across the bioenergetic membranes by coupling the proton translocations with electron transfer from the pool of membrane-soluble quinones to water-soluble redox proteins. Despite many years of research, the mechanism of quinol oxidation is not fully understood. It is assumed that unstable form of a partially oxidized quinol – semiquinone is an intermediate state of this process and that it is also a potential electron donor in the side reaction of superoxide generation. This semiquinone has remained experimentally elusive over years but recently a semiquinone interacting with the reduced iron-sulfur cluster was identified as a new state of the enzyme. The results indicate that semiquinone coupled to the iron-sulfur cluster is most probably an additional state that can prevent side reactions, including superoxide generation.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" IndexingMethod="Curated" Owner="NLM"><PMID Version="1">32700506</PMID><DateCompleted><Year>2020</Year><Month>09</Month><Day>18</Day></DateCompleted><DateRevised><Year>2020</Year><Month>09</Month><Day>18</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Print">0032-5422</ISSN><JournalIssue CitedMedium="Print"><Volume>66</Volume><Issue>2</Issue><PubDate><Year>2020</Year><Month>06</Month><Day>27</Day></PubDate></JournalIssue><Title>Postepy biochemii</Title><ISOAbbreviation>Postepy Biochem</ISOAbbreviation></Journal><ArticleTitle>Unusual semiquinone as an electron buffer in enzymatic quinone oxidation</ArticleTitle><Pagination><MedlinePgn>91-99</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.18388/pb.2020_326</ELocationID><Abstract><AbstractText>Cytochromes bc1 and c b6f are part of respiratory or photosynthetic machinery. The main role of these enzymes is to build proton motive force across the bioenergetic membranes by coupling the proton translocations with electron transfer from the pool of membrane-soluble quinones to water-soluble redox proteins. Despite many years of research, the mechanism of quinol oxidation is not fully understood. It is assumed that unstable form of a partially oxidized quinol – semiquinone is an intermediate state of this process and that it is also a potential electron donor in the side reaction of superoxide generation. This semiquinone has remained experimentally elusive over years but recently a semiquinone interacting with the reduced iron-sulfur cluster was identified as a new state of the enzyme. The results indicate that semiquinone coupled to the iron-sulfur cluster is most probably an additional state that can prevent side reactions, including superoxide generation.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Bujnowicz</LastName><ForeName>Łukasz</ForeName><Initials>Ł</Initials><AffiliationInfo><Affiliation>Zakład Biofizyki Molekularnej; Wydział Biochemii, Biofizyki i Biotechnologii Uniwersytetu Jagiellońskiego w Krakowie. lukasz.bujnowicz@uj.edu.pl.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sarewicz</LastName><ForeName>Marcin</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Zakład Biofizyki Molekularnej; Wydział Biochemii, Biofizyki i Biotechnologii; Uniwersytet Jagielloński, Kraków. artur.osyczka@uj.edu.pl.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Osyczka</LastName><ForeName>Artur</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Zakład Biofizyki Molekularnej; Wydział Biochemii, Biofizyki i Biotechnologii; Uniwersytet Jagielloński, Kraków. artur.osyczka@uj.edu.pl.</Affiliation></AffiliationInfo></Author></AuthorList><Language>pol</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><VernacularTitle>Nietypowy semichinon jako element buforujący przepływ elektronów przez cytochromy z rodziny bc.</VernacularTitle><ArticleDate DateType="Electronic"><Year>2020</Year><Month>06</Month><Day>27</Day></ArticleDate></Article><MedlineJournalInfo><Country>Poland</Country><MedlineTA>Postepy Biochem</MedlineTA><NlmUniqueID>0023525</NlmUniqueID><ISSNLinking>0032-5422</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D016227">Benzoquinones</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D003580">Cytochromes</NameOfSubstance></Chemical><Chemical><RegistryNumber>11062-77-4</RegistryNumber><NameOfSubstance UI="D013481">Superoxides</NameOfSubstance></Chemical><Chemical><RegistryNumber>3T006GV98U</RegistryNumber><NameOfSubstance UI="C004532">quinone</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D016227" MajorTopicYN="N">Benzoquinones</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003580" MajorTopicYN="N">Cytochromes</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004579" MajorTopicYN="N">Electron Transport</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004583" MajorTopicYN="Y">Electrons</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013481" MajorTopicYN="N">Superoxides</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList><OtherAbstract Type="Publisher" Language="pol"><AbstractText>Cytochrom bc1, obecny w układach oddechowych, wraz z cytochromem b6f obecnym w roślinnych układach fotosyntetycznych, tworzą rodzinę kompleksów bc. Główną rolą tych enzymów jest budowanie siły protonomotorycznej w poprzek błon bioenergetycznych dzięki sprzęgnięciu translokacji protonów z transferem elektronów z puli rozpuszczalnych w błonie pochodnych chinonów na pulę białkowych przenośników elektronów. Mimo wielu lat badań nie jest w pełni znany mechanizm utlenienia pochodnych chinolu w miejscu QO. Zakłada się, że proces ten przebiega przez niestabilną formę częściowo utlenionego chinolu - semichinon, który może być substratem w ubocznej reakcji powstawania anionorodnika ponadtlenkowego. Semichinon ten pozostaje wciąż nieuchwytny eksperymentalnie. Zaobserwowano natomiast w miejscu QO metastabilną formę semichinonu sprzężoną magnetycznie ze zredukowanym klastrem żelazowo-siarkowym. Klaster ten jest jednym z kofaktorów redoks w enzymach z rodziny bc. Wyniki eksperymentalne wskazują, że sprzężony z klastrem semichion jest dodatkowym stanem w katalizie enzymu i może częściowo zapobiegać niepożądanym reakcjom ubocznym w miejscu QO, w tym produkcji anionorodnika ponadtlenkowego.</AbstractText></OtherAbstract></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2020</Year><Month>04</Month><Day>16</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2020</Year><Month>04</Month><Day>23</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>7</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>7</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>9</Month><Day>20</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">32700506</ArticleId><ArticleId IdType="doi">10.18388/pb.2020_326</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Pologne</li></country></list><tree><country name="Pologne"><noRegion><name sortKey="Bujnowicz, Lukasz" sort="Bujnowicz, Lukasz" uniqKey="Bujnowicz L" first="Łukasz" last="Bujnowicz">Łukasz Bujnowicz</name></noRegion><name sortKey="Osyczka, Artur" sort="Osyczka, Artur" uniqKey="Osyczka A" first="Artur" last="Osyczka">Artur Osyczka</name><name sortKey="Sarewicz, Marcin" sort="Sarewicz, Marcin" uniqKey="Sarewicz M" first="Marcin" last="Sarewicz">Marcin Sarewicz</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/IronSulferCluV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000003 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000003 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Bois
|area= IronSulferCluV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:32700506
|texte= Unusual semiquinone as an electron buffer in enzymatic quinone oxidation
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:32700506" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a IronSulferCluV1
| This area was generated with Dilib version V0.6.38. |  |