Matches in SemOpenAlex for { <https://semopenalex.org/work/W2892098931> ?p ?o ?g. }
Showing items 1 to 71 of
71
with 100 items per page.
- W2892098931 abstract "Aerobic respiration is linked to oxidative phosphorylation and involves a redox-linked proton translocation across the mitochondrial inner membrane. Deeper understanding of the mechanism of mitochondrial electron transport requires detailed characterization of the redox centers present in respiratory enzyme complexes. A combination of low temperature MCD spectra and magnetization data, with parallel EPR, CD, and UV-visible experiments, has been used to characterize the structural, electronic, and magnetic properties of the iron sulfur centers in respiratory enzymes. The enzymes studied were those associated with electron transport in mammalian mitochondria, with comparative studies of similar enzymes and proteins in heterotropic bacteria. The results from studies of soluble high molecular weight NADH dehydrogenase are consistent with the presence of one 2Fe-2S and three 4Fe-4S centers, each approximately stoichiometric with FMN. Comparison of EPT spectra of Complex I and soluble enzyme indicates that the same clusters are present in the more intact particulate preparation. Spectroscopic experiments demonstrate that both yeast and mammalian succinate dehydrogenase, and the analogous fumarate reductase from E. coli, contain a 2Fe-2S , a 3Fe-xS , and a 4Fe-4S cluster in amounts stoichiometric with FAD. The trinuclear cluster was shown to be a necessary requirement for reconstitutive activity. In addition, evidence is presented to show that the 3Fe-xS and 4Fe-4S centers are distinct entities rather than interconversion products of the same cluster. Spectroscopic studies of the iron sulfur center in mammalian electron transfer flavoprotein (ETF) dehydrogenase were consistent with the presence of one 3Fe-4S cluster. In addition, dithionite reduction of ETF dehydrogenase was shown to involve addition of two electrons to FAD and one electron to the iron sulfur cluster, whereas the enzymatic process involves one electron reduction of both redox centers. Comparison of spectra from T. thermophilus Rieske protein with that from spinach ferredoxin indicated substantial differences in the electronic structure of their 2Fe-2S clusters. The differences most likely relate to variations in the ligand amino acid groups." @default.
- W2892098931 created "2018-09-27" @default.
- W2892098931 creator A5069392422 @default.
- W2892098931 date "2022-06-14" @default.
- W2892098931 modified "2023-09-28" @default.
- W2892098931 title "Spectroscopic Studies of Mitochondrial Iron Sulfur Proteins (Succinate Dehydrogenase, Electron Paramagnetic Resonance, Fumarate Reductase)." @default.
- W2892098931 cites W1570796718 @default.
- W2892098931 cites W2080733474 @default.
- W2892098931 doi "https://doi.org/10.31390/gradschool_disstheses.4252" @default.
- W2892098931 hasPublicationYear "2022" @default.
- W2892098931 type Work @default.
- W2892098931 sameAs 2892098931 @default.
- W2892098931 citedByCount "0" @default.
- W2892098931 crossrefType "dissertation" @default.
- W2892098931 hasAuthorship W2892098931A5069392422 @default.
- W2892098931 hasBestOaLocation W28920989311 @default.
- W2892098931 hasConcept C104292427 @default.
- W2892098931 hasConcept C104317684 @default.
- W2892098931 hasConcept C121612415 @default.
- W2892098931 hasConcept C123669783 @default.
- W2892098931 hasConcept C134621786 @default.
- W2892098931 hasConcept C134651460 @default.
- W2892098931 hasConcept C179104552 @default.
- W2892098931 hasConcept C181199279 @default.
- W2892098931 hasConcept C185592680 @default.
- W2892098931 hasConcept C24840226 @default.
- W2892098931 hasConcept C2776317432 @default.
- W2892098931 hasConcept C2776319529 @default.
- W2892098931 hasConcept C2777852564 @default.
- W2892098931 hasConcept C2781330172 @default.
- W2892098931 hasConcept C3020377403 @default.
- W2892098931 hasConcept C55493867 @default.
- W2892098931 hasConcept C55904794 @default.
- W2892098931 hasConcept C71995715 @default.
- W2892098931 hasConcept C75473681 @default.
- W2892098931 hasConceptScore W2892098931C104292427 @default.
- W2892098931 hasConceptScore W2892098931C104317684 @default.
- W2892098931 hasConceptScore W2892098931C121612415 @default.
- W2892098931 hasConceptScore W2892098931C123669783 @default.
- W2892098931 hasConceptScore W2892098931C134621786 @default.
- W2892098931 hasConceptScore W2892098931C134651460 @default.
- W2892098931 hasConceptScore W2892098931C179104552 @default.
- W2892098931 hasConceptScore W2892098931C181199279 @default.
- W2892098931 hasConceptScore W2892098931C185592680 @default.
- W2892098931 hasConceptScore W2892098931C24840226 @default.
- W2892098931 hasConceptScore W2892098931C2776317432 @default.
- W2892098931 hasConceptScore W2892098931C2776319529 @default.
- W2892098931 hasConceptScore W2892098931C2777852564 @default.
- W2892098931 hasConceptScore W2892098931C2781330172 @default.
- W2892098931 hasConceptScore W2892098931C3020377403 @default.
- W2892098931 hasConceptScore W2892098931C55493867 @default.
- W2892098931 hasConceptScore W2892098931C55904794 @default.
- W2892098931 hasConceptScore W2892098931C71995715 @default.
- W2892098931 hasConceptScore W2892098931C75473681 @default.
- W2892098931 hasLocation W28920989311 @default.
- W2892098931 hasOpenAccess W2892098931 @default.
- W2892098931 hasPrimaryLocation W28920989311 @default.
- W2892098931 hasRelatedWork W1840703237 @default.
- W2892098931 hasRelatedWork W1956476910 @default.
- W2892098931 hasRelatedWork W2017037513 @default.
- W2892098931 hasRelatedWork W2017112326 @default.
- W2892098931 hasRelatedWork W2020627214 @default.
- W2892098931 hasRelatedWork W2096859010 @default.
- W2892098931 hasRelatedWork W2892098931 @default.
- W2892098931 hasRelatedWork W4211141604 @default.
- W2892098931 hasRelatedWork W985524815 @default.
- W2892098931 hasRelatedWork W2027015907 @default.
- W2892098931 isParatext "false" @default.
- W2892098931 isRetracted "false" @default.
- W2892098931 magId "2892098931" @default.
- W2892098931 workType "dissertation" @default.