FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1967091985> ?p ?o ?g. }

• W1967091985 endingPage "7034" @default.
• W1967091985 startingPage "7024" @default.
• W1967091985 abstract "Sulfur dehydrogenase, Sox(CD)(2), is an essential part of the sulfur-oxidizing enzyme system of the chemotrophic bacterium Paracoccus pantotrophus. Sox(CD)(2) is a alpha(2)beta(2) complex composed of the molybdoprotein SoxC (43 442 Da) and the hybrid diheme c-type cytochrome SoxD (37 637 Da). Sox(CD)(2) catalyzes the oxidation of protein-bound sulfur to sulfate with a unique six-electron transfer. Amino acid sequence analysis identified the heme-1 domain of SoxD proteins to be specific for sulfur dehydrogenases and to contain a novel ProCysMetXaaAspCys motif, while the heme-2 domain is related to various cytochromes c(2). Purification of sulfur dehydrogenase without protease inhibitor yielded a dimeric SoxCD(1) complex consisting of SoxC and SoxD(1) of 30 kDa, which contained only the heme-1 domain. The heme-2 domain was isolated as a new cytochrome SoxD(2) of about 13 kDa. Both hemes of SoxD in Sox(CD)(2) are redox-active with midpoint potentials at E(m)1 = 218 +/- 10 mV and E(m)2 = 268 +/- 10 mV, while SoxCD(1) and SoxD(2) both exhibit a midpoint potential of E(m) = 278 +/- 10 mV. Electrochemically induced FTIR difference spectra of Sox(CD)(2), SoxCD(1), and SoxD(2) were distinct. A carboxy group is protonated upon reduction of the SoxD(1) heme but not for SoxD(2). The specific activity of SoxCD(1) and Sox(CD)(2) was identical as was the yield of electrons with thiosulfate in the reconstituted Sox enzyme system. To examine the physiological significance of the heme-2 domain, a mutant was constructed that was deleted for the heme-2 domain, which produced SoxCD(1) and transferred electrons from thiosulfate to oxygen. These data demonstrated the crucial role of the heme-1 domain of SoxD for catalytic activity, electron yield, and transfer of the electrons to the cytoplasmic membrane, while the heme-2 domain mediated the alpha(2)beta(2) tetrameric structure of sulfur dehydrogenase." @default.
• W1967091985 created "2016-06-24" @default.
• W1967091985 creator A5000422071 @default.
• W1967091985 creator A5009597606 @default.
• W1967091985 creator A5017371558 @default.
• W1967091985 creator A5025424578 @default.
• W1967091985 creator A5061208586 @default.
• W1967091985 creator A5091871975 @default.
• W1967091985 date "2005-04-08" @default.
• W1967091985 modified "2023-10-05" @default.
• W1967091985 title "Sulfur Dehydrogenase of<i>Paracoccus pantotrophus</i>: The Heme-2 Domain of the Molybdoprotein Cytochrome<i>c</i>Complex Is Dispensable for Catalytic Activity" @default.
• W1967091985 cites W1486421713 @default.
• W1967091985 cites W1524781921 @default.
• W1967091985 cites W1534410293 @default.
• W1967091985 cites W1897322573 @default.
• W1967091985 cites W1966802143 @default.
• W1967091985 cites W1980134163 @default.
• W1967091985 cites W1995234983 @default.
• W1967091985 cites W2018396914 @default.
• W1967091985 cites W2043809520 @default.
• W1967091985 cites W2044671364 @default.
• W1967091985 cites W2047766633 @default.
• W1967091985 cites W2067984990 @default.
• W1967091985 cites W2072210452 @default.
• W1967091985 cites W2073333486 @default.
• W1967091985 cites W2075000548 @default.
• W1967091985 cites W2086563608 @default.
• W1967091985 cites W2093560200 @default.
• W1967091985 cites W2161340005 @default.
• W1967091985 cites W2164363486 @default.
• W1967091985 doi "https://doi.org/10.1021/bi047334b" @default.
• W1967091985 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15865447" @default.
• W1967091985 hasPublicationYear "2005" @default.
• W1967091985 type Work @default.
• W1967091985 sameAs 1967091985 @default.
• W1967091985 citedByCount "25" @default.
• W1967091985 countsByYear W19670919852012 @default.
• W1967091985 countsByYear W19670919852013 @default.
• W1967091985 countsByYear W19670919852015 @default.
• W1967091985 countsByYear W19670919852017 @default.
• W1967091985 countsByYear W19670919852018 @default.
• W1967091985 countsByYear W19670919852021 @default.
• W1967091985 countsByYear W19670919852023 @default.
• W1967091985 crossrefType "journal-article" @default.
• W1967091985 hasAuthorship W1967091985A5000422071 @default.
• W1967091985 hasAuthorship W1967091985A5009597606 @default.
• W1967091985 hasAuthorship W1967091985A5017371558 @default.
• W1967091985 hasAuthorship W1967091985A5025424578 @default.
• W1967091985 hasAuthorship W1967091985A5061208586 @default.
• W1967091985 hasAuthorship W1967091985A5091871975 @default.
• W1967091985 hasConcept C145148216 @default.
• W1967091985 hasConcept C178790620 @default.
• W1967091985 hasConcept C181199279 @default.
• W1967091985 hasConcept C185592680 @default.
• W1967091985 hasConcept C20705724 @default.
• W1967091985 hasConcept C2776217839 @default.
• W1967091985 hasConcept C2780768313 @default.
• W1967091985 hasConcept C28859421 @default.
• W1967091985 hasConcept C29311851 @default.
• W1967091985 hasConcept C30095370 @default.
• W1967091985 hasConcept C55493867 @default.
• W1967091985 hasConcept C71240020 @default.
• W1967091985 hasConceptScore W1967091985C145148216 @default.
• W1967091985 hasConceptScore W1967091985C178790620 @default.
• W1967091985 hasConceptScore W1967091985C181199279 @default.
• W1967091985 hasConceptScore W1967091985C185592680 @default.
• W1967091985 hasConceptScore W1967091985C20705724 @default.
• W1967091985 hasConceptScore W1967091985C2776217839 @default.
• W1967091985 hasConceptScore W1967091985C2780768313 @default.
• W1967091985 hasConceptScore W1967091985C28859421 @default.
• W1967091985 hasConceptScore W1967091985C29311851 @default.
• W1967091985 hasConceptScore W1967091985C30095370 @default.
• W1967091985 hasConceptScore W1967091985C55493867 @default.
• W1967091985 hasConceptScore W1967091985C71240020 @default.
• W1967091985 hasIssue "18" @default.
• W1967091985 hasLocation W19670919851 @default.
• W1967091985 hasLocation W19670919852 @default.
• W1967091985 hasOpenAccess W1967091985 @default.
• W1967091985 hasPrimaryLocation W19670919851 @default.
• W1967091985 hasRelatedWork W1501456700 @default.
• W1967091985 hasRelatedWork W1999879475 @default.
• W1967091985 hasRelatedWork W2003132251 @default.
• W1967091985 hasRelatedWork W2033748091 @default.
• W1967091985 hasRelatedWork W2041542205 @default.
• W1967091985 hasRelatedWork W2071904928 @default.
• W1967091985 hasRelatedWork W2077724203 @default.
• W1967091985 hasRelatedWork W2084078405 @default.
• W1967091985 hasRelatedWork W2090461908 @default.
• W1967091985 hasRelatedWork W4324311635 @default.
• W1967091985 hasVolume "44" @default.
• W1967091985 isParatext "false" @default.
• W1967091985 isRetracted "false" @default.
• W1967091985 magId "1967091985" @default.
• W1967091985 workType "article" @default.