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- W2188114977 abstract "Thebisulfite reductase was a tetramer andhadtwotypesofsubunits with an a232structure andan individual molecular weight of47,000. Theenzyme exhibited absorption maximaat576,389,and279 nm, with aweakbandat693nm. Upontheaddition ofdithionite, theabsorption maximaat576and693nm were weakened, anda new bandappeared at605nm. Theprotein reacted withCOinthepresenceofdithionite togive a complex with absorption peaksat593,548,and395nm. Theextinction coefficients ofthe purified enzyme at576,389,and279nm were 89,000, 310,000, and663,000 Mcm-,respectively. Siroheme was detected astheprosthetic group.Theprotein contains 20to21nonhemeiron atomsand16to17acid-labile sulfur groupsper molecule. Thedatasuggest thepresenceoffoursirohemes andprobably four (4Fe-4S) centers permolecule bycomparison withdesulfoviridin, thedissimilatorysulfite reductase fromDesulfovibrio species. Theprotein contains 36cysteine residues andishighinacidic andaromatic aminoacids. TheN-terminal amino acids ofthea and,Bsubunits were threonine andserine, respectively. With reduced methyl viologen aselectron donor, themajor product ofsulfite reduction was trithionate, andthepHoptimum foractivity was 6.0. Theenzyme was stable to70°Canddenatured rapidly abovethis temperature. Thedependence ofT. commune bisulfite reductase activity on temperature was linear between 35and 65°C, andtheQiovalues observed were above3.Thepresenceofthis new typeof dissimilatory bisulfite reductase inT.commune isdiscussed intermsoftaxonomic significance." @default.
- W2188114977 created "2016-06-24" @default.
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- W2188114977 date "1983-01-01" @default.
- W2188114977 modified "2023-09-24" @default.
- W2188114977 title "Characterization ofa NewTypeofDissimilatory Sulfite Reductase Present inThermodesulfobacterium" @default.
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- W2188114977 hasPublicationYear "1983" @default.
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