FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2808055278> ?p ?o ?g. }

• W2808055278 abstract "Formate dehydrogenase H (FDH-H) and [NiFe]-hydrogenase 3 (Hyd-3) form the catalytic components of the hydrogen-producing formate hydrogenlyase (FHL) complex, which disproportionates formate to H2 and CO2 during mixed acid fermentation in enterobacteria. FHL comprises minimally seven proteins and little is understood about how this complex is assembled. Early studies identified a ferredoxin-like protein, HydN, as being involved in FDH-H assembly into the FHL complex. In order to understand how FDH-H and its small subunit HycB, which is also a ferredoxin-like protein, attach to the FHL complex, the possible roles of HydN and its paralogue, YsaA, in FHL complex stability and assembly were investigated. Deletion of the hycB gene reduced redox dye-mediated FDH-H activity to approximately 10%, abolished FHL-dependent H2-production, and reduced Hyd-3 activity. These data are consistent with HycB being an essential electron transfer component of the FHL complex. The FDH-H activity of the hydN and the ysaA deletion strains was reduced to 59% and 57% of the parental, while the double deletion reduced activity of FDH-H to 28% and the triple deletion with hycB to 1%. Remarkably, and in contrast to the hycB deletion, the absence of HydN and YsaA was without significant effect on FHL-dependent H2-production or total Hyd-3 activity; FDH-H protein levels were also unaltered. This is the first description of a phenotype for the E. coli ysaA deletion strain and identifies it as a novel factor required for optimal redox dye-linked FDH-H activity. A ysaA deletion strain could be complemented for FDH-H activity by hydN and ysaA, but the hydN deletion strain could not be complemented. Introduction of these plasmids did not affect H2 production. Bacterial two-hybrid interactions showed that YsaA, HydN and HycB interact with each other and with the FDH-H protein. Further novel anaerobic cross-interactions of 10 ferredoxin-like proteins in E. coli were also discovered and described. Together, these data indicate that FDH-H activity measured with the redox dye benzyl viologen is the sum of the FDH-H protein interacting with three independent small subunits and suggest that FDH-H can associate with different redox-protein complexes in the anaerobic cell to supply electrons from formate oxidation." @default.
• W2808055278 created "2018-06-21" @default.
• W2808055278 creator A5055325510 @default.
• W2808055278 date "2018-06-11" @default.
• W2808055278 modified "2023-09-26" @default.
• W2808055278 title "The Ferredoxin-Like Proteins HydN and YsaA Enhance Redox Dye-Linked Activity of the Formate Dehydrogenase H Component of the Formate Hydrogenlyase Complex" @default.
• W2808055278 cites W1481775159 @default.
• W2808055278 cites W1496569297 @default.
• W2808055278 cites W1503496924 @default.
• W2808055278 cites W1537502919 @default.
• W2808055278 cites W1910590028 @default.
• W2808055278 cites W1917131476 @default.
• W2808055278 cites W1924589087 @default.
• W2808055278 cites W1925458372 @default.
• W2808055278 cites W1930985780 @default.
• W2808055278 cites W1968535457 @default.
• W2808055278 cites W1976814390 @default.
• W2808055278 cites W1997266605 @default.
• W2808055278 cites W1999749765 @default.
• W2808055278 cites W2006444440 @default.
• W2808055278 cites W2007400695 @default.
• W2808055278 cites W2009135994 @default.
• W2808055278 cites W2011447018 @default.
• W2808055278 cites W2014361215 @default.
• W2808055278 cites W2026937184 @default.
• W2808055278 cites W2032237557 @default.
• W2808055278 cites W2038157034 @default.
• W2808055278 cites W2041973695 @default.
• W2808055278 cites W2042814467 @default.
• W2808055278 cites W2044437130 @default.
• W2808055278 cites W2045183479 @default.
• W2808055278 cites W2047670590 @default.
• W2808055278 cites W2058878931 @default.
• W2808055278 cites W2068658290 @default.
• W2808055278 cites W2090079874 @default.
• W2808055278 cites W2096173332 @default.
• W2808055278 cites W2100132717 @default.
• W2808055278 cites W2101639848 @default.
• W2808055278 cites W2111967267 @default.
• W2808055278 cites W2113785477 @default.
• W2808055278 cites W2116137883 @default.
• W2808055278 cites W2129393436 @default.
• W2808055278 cites W2137012036 @default.
• W2808055278 cites W2143453049 @default.
• W2808055278 cites W2149866996 @default.
• W2808055278 cites W2150618302 @default.
• W2808055278 cites W2155168552 @default.
• W2808055278 cites W2163813592 @default.
• W2808055278 cites W2170899233 @default.
• W2808055278 cites W2189955651 @default.
• W2808055278 cites W2312988331 @default.
• W2808055278 cites W2336330109 @default.
• W2808055278 cites W2417795995 @default.
• W2808055278 cites W2737194925 @default.
• W2808055278 cites W4211068972 @default.
• W2808055278 cites W2613693416 @default.
• W2808055278 doi "https://doi.org/10.3389/fmicb.2018.01238" @default.
• W2808055278 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6004506" @default.
• W2808055278 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/29942290" @default.
• W2808055278 hasPublicationYear "2018" @default.
• W2808055278 type Work @default.
• W2808055278 sameAs 2808055278 @default.
• W2808055278 citedByCount "12" @default.
• W2808055278 countsByYear W28080552782018 @default.
• W2808055278 countsByYear W28080552782019 @default.
• W2808055278 countsByYear W28080552782020 @default.
• W2808055278 countsByYear W28080552782022 @default.
• W2808055278 countsByYear W28080552782023 @default.
• W2808055278 crossrefType "journal-article" @default.
• W2808055278 hasAuthorship W2808055278A5055325510 @default.
• W2808055278 hasBestOaLocation W28080552781 @default.
• W2808055278 hasConcept C104292427 @default.
• W2808055278 hasConcept C104317684 @default.
• W2808055278 hasConcept C116569031 @default.
• W2808055278 hasConcept C134621786 @default.
• W2808055278 hasConcept C161790260 @default.
• W2808055278 hasConcept C170493617 @default.
• W2808055278 hasConcept C178790620 @default.
• W2808055278 hasConcept C181199279 @default.
• W2808055278 hasConcept C185592680 @default.
• W2808055278 hasConcept C2778428456 @default.
• W2808055278 hasConcept C2780178953 @default.
• W2808055278 hasConcept C55493867 @default.
• W2808055278 hasConcept C55904794 @default.
• W2808055278 hasConcept C71240020 @default.
• W2808055278 hasConcept C79115784 @default.
• W2808055278 hasConceptScore W2808055278C104292427 @default.
• W2808055278 hasConceptScore W2808055278C104317684 @default.
• W2808055278 hasConceptScore W2808055278C116569031 @default.
• W2808055278 hasConceptScore W2808055278C134621786 @default.
• W2808055278 hasConceptScore W2808055278C161790260 @default.
• W2808055278 hasConceptScore W2808055278C170493617 @default.
• W2808055278 hasConceptScore W2808055278C178790620 @default.
• W2808055278 hasConceptScore W2808055278C181199279 @default.
• W2808055278 hasConceptScore W2808055278C185592680 @default.
• W2808055278 hasConceptScore W2808055278C2778428456 @default.
• W2808055278 hasConceptScore W2808055278C2780178953 @default.
• W2808055278 hasConceptScore W2808055278C55493867 @default.
• W2808055278 hasConceptScore W2808055278C55904794 @default.
• W2808055278 hasConceptScore W2808055278C71240020 @default.

• next