Matches in SemOpenAlex for { <https://semopenalex.org/work/W1573670961> ?p ?o ?g. }
Showing items 1 to 82 of
82
with 100 items per page.
- W1573670961 abstract "Abstract A heat-labile iron-cytochrome c reductase was isolated from Ferrobacillus ferrooxidans by sonic oscillation of the cells at pH 5.5 in the presence of protamine sulfate and purified 20-fold with 10% recovery by successive fractionation of the high speed (144,000 x g) supernatant solution with ammonium sulfate and Sephadex G-200. The enzyme displayed a pH optimum of 5.7 to 6.2 and typical substrate saturation curves with a Km of 2.75 x 10-5 m for cytochrome c and 1.6 x 10-3 m for FeSO4·7H2O. The protein nature of the catalyst was established by its protein content and susceptibility to the proteolytic action of Pronase and to heat. Exposure for 1 min at 100° was sufficient to destroy the activity completely. The most highly purified fraction of iron-cytochrome c reductase contained cytochrome c and apparently nonfunctional cytochrome b. Enzymatic activity, proportional to protein concentration and linear with time, was inhibited by reduced glutathione, p-hydroxymercuribenzoate, and cysteine, but not by atebrin, Amytal, or antimycin A. The inhibition by p-hydroxymercuribenzoate could be entirely reversed by equivalent concentrations of reduced glutathione or cysteine. Reduced cytochrome c, ferric ions, and several other metal ions also inhibited the reductase activity. The close association of the enzyme with the iron oxidase activity of F. ferrooxidans was partially shown by the generally parallel distribution of the two activities in the various fractions resulting from Sephadex treatment and from differential centrifugation. Various attempts to separate the iron oxidase and cytochrome c reductase activities from one another in the less purified fractions were unsuccessful leading to destruction of either both activities or the iron oxidase activity. The most highly purified iron-cytochrome c reductase fraction (F5) possessed no iron oxidase activity and contained a factor that stimulated less purified fractions several-fold in both their cytochrome c oxidase and iron oxidase activities but not in their iron-cytochrome c reductase activity." @default.
- W1573670961 created "2016-06-24" @default.
- W1573670961 creator A5050639027 @default.
- W1573670961 creator A5088190259 @default.
- W1573670961 date "1966-11-01" @default.
- W1573670961 modified "2023-09-30" @default.
- W1573670961 title "Electron Transport Systems of the Chemoautotroph Ferrobacillus ferrooxidans" @default.
- W1573670961 cites W1498911307 @default.
- W1573670961 cites W1541445884 @default.
- W1573670961 cites W1570190665 @default.
- W1573670961 cites W1775749144 @default.
- W1573670961 cites W2061952463 @default.
- W1573670961 cites W2068371198 @default.
- W1573670961 cites W2279913030 @default.
- W1573670961 cites W2283926690 @default.
- W1573670961 cites W3119802893 @default.
- W1573670961 cites W69209863 @default.
- W1573670961 cites W70706850 @default.
- W1573670961 cites W91637582 @default.
- W1573670961 doi "https://doi.org/10.1016/s0021-9258(18)99646-8" @default.
- W1573670961 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/4288725" @default.
- W1573670961 hasPublicationYear "1966" @default.
- W1573670961 type Work @default.
- W1573670961 sameAs 1573670961 @default.
- W1573670961 citedByCount "19" @default.
- W1573670961 crossrefType "journal-article" @default.
- W1573670961 hasAuthorship W1573670961A5050639027 @default.
- W1573670961 hasAuthorship W1573670961A5088190259 @default.
- W1573670961 hasBestOaLocation W15736709611 @default.
- W1573670961 hasConcept C123249941 @default.
- W1573670961 hasConcept C133166286 @default.
- W1573670961 hasConcept C134651460 @default.
- W1573670961 hasConcept C163994747 @default.
- W1573670961 hasConcept C181199279 @default.
- W1573670961 hasConcept C185592680 @default.
- W1573670961 hasConcept C2779201268 @default.
- W1573670961 hasConcept C2780768313 @default.
- W1573670961 hasConcept C28859421 @default.
- W1573670961 hasConcept C29311851 @default.
- W1573670961 hasConcept C43617362 @default.
- W1573670961 hasConcept C538909803 @default.
- W1573670961 hasConcept C55493867 @default.
- W1573670961 hasConceptScore W1573670961C123249941 @default.
- W1573670961 hasConceptScore W1573670961C133166286 @default.
- W1573670961 hasConceptScore W1573670961C134651460 @default.
- W1573670961 hasConceptScore W1573670961C163994747 @default.
- W1573670961 hasConceptScore W1573670961C181199279 @default.
- W1573670961 hasConceptScore W1573670961C185592680 @default.
- W1573670961 hasConceptScore W1573670961C2779201268 @default.
- W1573670961 hasConceptScore W1573670961C2780768313 @default.
- W1573670961 hasConceptScore W1573670961C28859421 @default.
- W1573670961 hasConceptScore W1573670961C29311851 @default.
- W1573670961 hasConceptScore W1573670961C43617362 @default.
- W1573670961 hasConceptScore W1573670961C538909803 @default.
- W1573670961 hasConceptScore W1573670961C55493867 @default.
- W1573670961 hasLocation W15736709611 @default.
- W1573670961 hasOpenAccess W1573670961 @default.
- W1573670961 hasPrimaryLocation W15736709611 @default.
- W1573670961 hasRelatedWork W137790106 @default.
- W1573670961 hasRelatedWork W1505201936 @default.
- W1573670961 hasRelatedWork W1524803322 @default.
- W1573670961 hasRelatedWork W1530879923 @default.
- W1573670961 hasRelatedWork W1577918814 @default.
- W1573670961 hasRelatedWork W1588269551 @default.
- W1573670961 hasRelatedWork W1825592043 @default.
- W1573670961 hasRelatedWork W2005366936 @default.
- W1573670961 hasRelatedWork W2030335983 @default.
- W1573670961 hasRelatedWork W2031107830 @default.
- W1573670961 hasRelatedWork W2036723226 @default.
- W1573670961 hasRelatedWork W2046896485 @default.
- W1573670961 hasRelatedWork W2047487059 @default.
- W1573670961 hasRelatedWork W2051697962 @default.
- W1573670961 hasRelatedWork W2061600722 @default.
- W1573670961 hasRelatedWork W2085161404 @default.
- W1573670961 hasRelatedWork W2140253599 @default.
- W1573670961 hasRelatedWork W2164351560 @default.
- W1573670961 hasRelatedWork W2166143241 @default.
- W1573670961 hasRelatedWork W91637582 @default.
- W1573670961 isParatext "false" @default.
- W1573670961 isRetracted "false" @default.
- W1573670961 magId "1573670961" @default.
- W1573670961 workType "article" @default.