Matches in SemOpenAlex for { <https://semopenalex.org/work/W2014960917> ?p ?o ?g. }
- W2014960917 endingPage "4153" @default.
- W2014960917 startingPage "4149" @default.
- W2014960917 abstract "The proton-translocating NADH-quinone oxidoreductase (EC 1.6.99.3) is the largest and least understood enzyme complex of the respiratory chain. The mammalian mitochondrial enzyme (also called complex I) contains more than 40 subunits, whereas its structurally simpler bacterial counterpart (NDH-1) in Paracoccus denitrificans and Thermus thermophilus HB-8 consists of 14 subunits. A major unsolved question is the location and mechanism of the terminal electron transfer step from iron-sulfur cluster N2 to quinone. Potent inhibitors acting at this key region are candidate photoaffinity probes to dissect NADH-quinone oxidoreductases. Complex I and NDH-1 are very sensitive to inhibition by a variety of structurally diverse toxicants, including rotenone, piericidin A, bullatacin, and pyridaben. We designed (trifluoromethyl)diazirinyl[3H]pyridaben ([3H]TDP) as our photoaffinity ligand because it combines outstanding inhibitor potency, a suitable photoreactive group, and tritium at high specific activity. Photoaffinity labeling of mitochondrial electron transport particles was specific and saturable. Isolation, protein sequencing, and immunoprecipitation identified the high-affinity specifically labeled 23-kDa subunit as PSST of complex I. Immunoprecipitation of labeled membranes of P. denitrificans and T. thermophilus established photoaffinity labeling of the equivalent bacterial NQO6. Competitive binding and enzyme inhibition studies showed that photoaffinity labeling of the specific high-affinity binding site of PSST is exceptionally sensitive to each of the high-potency inhibitors mentioned above. These findings establish that the homologous PSST of mitochondria and NQO6 of bacteria have a conserved inhibitor-binding site and that this subunit plays a key role in electron transfer by functionally coupling iron-sulfur cluster N2 to quinone." @default.
- W2014960917 created "2016-06-24" @default.
- W2014960917 creator A5019777938 @default.
- W2014960917 creator A5026936772 @default.
- W2014960917 creator A5040037974 @default.
- W2014960917 creator A5043739803 @default.
- W2014960917 creator A5080582789 @default.
- W2014960917 creator A5084365151 @default.
- W2014960917 creator A5084885647 @default.
- W2014960917 date "1999-03-30" @default.
- W2014960917 modified "2023-10-16" @default.
- W2014960917 title "NADH-quinone oxidoreductase: PSST subunit couples electron transfer from iron–sulfur cluster N2 to quinone" @default.
- W2014960917 cites W1422610633 @default.
- W2014960917 cites W1479672172 @default.
- W2014960917 cites W1482317169 @default.
- W2014960917 cites W1507356284 @default.
- W2014960917 cites W1544861790 @default.
- W2014960917 cites W1556704697 @default.
- W2014960917 cites W1562613004 @default.
- W2014960917 cites W1587218958 @default.
- W2014960917 cites W1975421048 @default.
- W2014960917 cites W1979368553 @default.
- W2014960917 cites W1986003680 @default.
- W2014960917 cites W1987761987 @default.
- W2014960917 cites W2001563231 @default.
- W2014960917 cites W2002806282 @default.
- W2014960917 cites W2012003686 @default.
- W2014960917 cites W2018289835 @default.
- W2014960917 cites W2019356464 @default.
- W2014960917 cites W2026551489 @default.
- W2014960917 cites W2035446976 @default.
- W2014960917 cites W2041867957 @default.
- W2014960917 cites W2048367257 @default.
- W2014960917 cites W2051023475 @default.
- W2014960917 cites W205203631 @default.
- W2014960917 cites W2053313807 @default.
- W2014960917 cites W2062282234 @default.
- W2014960917 cites W2067124266 @default.
- W2014960917 cites W2071493241 @default.
- W2014960917 cites W2076088762 @default.
- W2014960917 cites W2085101416 @default.
- W2014960917 cites W2100837269 @default.
- W2014960917 cites W2126557788 @default.
- W2014960917 cites W2154660868 @default.
- W2014960917 cites W2160088789 @default.
- W2014960917 cites W2419303900 @default.
- W2014960917 cites W315113715 @default.
- W2014960917 cites W4211133612 @default.
- W2014960917 cites W4298103304 @default.
- W2014960917 cites W1907199996 @default.
- W2014960917 doi "https://doi.org/10.1073/pnas.96.7.4149" @default.
- W2014960917 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/22435" @default.
- W2014960917 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10097178" @default.
- W2014960917 hasPublicationYear "1999" @default.
- W2014960917 type Work @default.
- W2014960917 sameAs 2014960917 @default.
- W2014960917 citedByCount "153" @default.
- W2014960917 countsByYear W20149609172012 @default.
- W2014960917 countsByYear W20149609172013 @default.
- W2014960917 countsByYear W20149609172014 @default.
- W2014960917 countsByYear W20149609172015 @default.
- W2014960917 countsByYear W20149609172016 @default.
- W2014960917 countsByYear W20149609172017 @default.
- W2014960917 countsByYear W20149609172018 @default.
- W2014960917 countsByYear W20149609172019 @default.
- W2014960917 countsByYear W20149609172020 @default.
- W2014960917 countsByYear W20149609172021 @default.
- W2014960917 countsByYear W20149609172022 @default.
- W2014960917 crossrefType "journal-article" @default.
- W2014960917 hasAuthorship W2014960917A5019777938 @default.
- W2014960917 hasAuthorship W2014960917A5026936772 @default.
- W2014960917 hasAuthorship W2014960917A5040037974 @default.
- W2014960917 hasAuthorship W2014960917A5043739803 @default.
- W2014960917 hasAuthorship W2014960917A5080582789 @default.
- W2014960917 hasAuthorship W2014960917A5084365151 @default.
- W2014960917 hasAuthorship W2014960917A5084885647 @default.
- W2014960917 hasBestOaLocation W20149609171 @default.
- W2014960917 hasConcept C104292427 @default.
- W2014960917 hasConcept C104317684 @default.
- W2014960917 hasConcept C107824862 @default.
- W2014960917 hasConcept C181199279 @default.
- W2014960917 hasConcept C185592680 @default.
- W2014960917 hasConcept C2778581200 @default.
- W2014960917 hasConcept C2779268744 @default.
- W2014960917 hasConcept C2780643102 @default.
- W2014960917 hasConcept C2780679169 @default.
- W2014960917 hasConcept C2780883830 @default.
- W2014960917 hasConcept C2908540775 @default.
- W2014960917 hasConcept C3020377403 @default.
- W2014960917 hasConcept C547475151 @default.
- W2014960917 hasConcept C55493867 @default.
- W2014960917 hasConcept C60538801 @default.
- W2014960917 hasConcept C71240020 @default.
- W2014960917 hasConceptScore W2014960917C104292427 @default.
- W2014960917 hasConceptScore W2014960917C104317684 @default.
- W2014960917 hasConceptScore W2014960917C107824862 @default.
- W2014960917 hasConceptScore W2014960917C181199279 @default.
- W2014960917 hasConceptScore W2014960917C185592680 @default.