Search results for "Iron-Sulfur Proteins"

showing 5 items of 15 documents

The oxidation of ubiquinol by the isolated rieske iron-sulfur protein in solution

1990

The pre-steady-state redox reactions of the Rieske iron-sulfur protein isolated from beef heart mitochondria have been characterized. The rates of oxidation by c-type cytochromes is much faster than the rate of reduction by ubiquinols. This enables the monitoring of the oxidation of ubiquinols by the Rieske protein through the steady-state electron transfer to cytochrome c in solution. The pH and ionic strength dependence of this reaction indicate that the ubiquinol anion is the direct reductant of the oxidized cluster of the iron-sulfur protein. The second electron from ubiquinol is diverted to oxygen by the isolated Rieske protein, and forms oxygen radicals that contribute to the steady-s…

Iron-Sulfur ProteinsUbiquinolCytochromeUbiquinoneBiophysicsmacromolecular substancesPhotochemistryBiochemistryRedoxMitochondria HeartElectron Transport Complex IIIElectron transferchemistry.chemical_compoundCytochrome C1AnimalsMolecular BiologybiologyChemistryCytochrome cHydrogen-Ion ConcentrationSolutionsKineticsCoenzyme Q – cytochrome c reductaseRieske proteinbiology.proteinCytochromesCattleOxidation-ReductionArchives of Biochemistry and Biophysics
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Response of the oxygen sensor NreB to air in vivo: Fe-S-containing NreB and apo-NreB in aerobically and anaerobically growing Staphylococcus carnosus.

2009

ABSTRACT The sensor kinase NreB from Staphylococcus carnosus contains an O 2 -sensitive [4Fe-4S] 2+ cluster which is converted by O 2 to a [2Fe-2S] 2+ cluster, followed by complete degradation and formation of Fe-S-less apo-NreB. NreB·[2Fe-2S] 2+ and apoNreB are devoid of kinase activity. NreB contains four Cys residues which ligate the Fe-S clusters. The accessibility of the Cys residues to alkylating agents was tested and used to differentiate Fe-S-containing and Fe-S-less NreB. In a two-step labeling procedure, accessible Cys residues in the native protein were first labeled by iodoacetate. In the second step, Cys residues not labeled in the first step were alkylated with the fluorescent…

Iron-Sulfur ProteinsbiologyAerobic bacteriaStaphylococcusGene Expression Regulation BacterialAlkylationbiology.organism_classificationMicrobiologyModels BiologicalAerobiosisOxygenBiochemistryBacterial ProteinsSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationNative stateImmunoprecipitationAnaerobic bacteriaAnaerobiosisCysteineKinase activityMolecular BiologyBacteriaCysteineStaphylococcus carnosusSignal TransductionJournal of bacteriology
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A PAS domain with an oxygen labile [4Fe-4S](2+) cluster in the oxygen sensor kinase NreB of Staphylococcus carnosus.

2008

The cytoplasmic histidine sensor kinase NreB of Staphylococcus carnosus responds to O(2) and controls together with the response regulator NreC the expression of genes of nitrate/nitrite respiration. nreBC homologous genes were found in Staphylococcus strains and Bacillus clausii, and a modified form was found in some Lactobacillus strains. NreB contains a sensory domain with similarity to heme B binding PAS domains. Anaerobically prepared NreB of S. carnosus exhibited a (diamagnetic) [4Fe-4S](2+) cluster when assessed by Mossbauer spectroscopy. Upon reaction with air, the cluster was degraded with a half-life of approximately 2.5 min. No significant amounts of Mossbauer or EPR detectable i…

Iron-Sulfur ProteinsbiologyHistidine KinaseChemistryLigandAirStaphylococcusHistidine kinasebiology.organism_classificationBiochemistrylaw.inventionOxygenHeme Bchemistry.chemical_compoundCrystallographyMagneticsSpectroscopy MossbauerPAS domainlawKinase activityElectron paramagnetic resonanceProtein KinasesHistidineStaphylococcus carnosusHalf-LifeBiochemistry
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The oxygen-responsive transcriptional regulator FNR ofEscherichia coli : the search for signals and reactions

1997

The FNR (fumarate and nitrate reductase regulation) protein of Escherichia coli is an oxygen-responsive transcriptional regulator required for the switch from aerobic to anaerobic metabolism. In the absence of oxygen, FNR changes from the inactive to the active state. The sensory and the regulatory functions reside in separate domains of FNR. The sensory domain contains a Fe-S cluster, which is of the [4Fe-4S]2+ type under anaerobic conditions. It is suggested that oxygen is supplied to the cytoplasmic FNR by diffusion and inactivates FNR by direct interaction. Reactivation under anoxic conditions requires cellular reductants. In vitro, the Fe-S cluster is converted to a [3Fe-4S]+ or a [2Fe…

Iron-Sulfur Proteinsinorganic chemicalsEscherichia coli Proteinschemistry.chemical_elementBiologyNitrate reductasemedicine.disease_causeenvironment and public healthMicrobiologyOxygenMetabolic pathwayBacterial ProteinschemistryBiochemistryCytoplasmRespirationEscherichia coliTranscriptional regulationmedicinebacteriaSignal transductionMolecular BiologyEscherichia coliSignal TransductionTranscription FactorsMolecular Microbiology
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The fnr Gene of Bacillus licheniformis and the Cysteine Ligands of the C-Terminal FeS Cluster

1998

Many of the O2-responsive gene regulators of bacteria are members of the fumarate nitrate reductase-cyclic AMP receptor protein family of transcriptional regulators (12, 13, 15, 17) with predicted structures similar to those of the cyclic AMP receptor protein (11). The Fnr (stands for fumarate nitrate reductase regulator) protein from Escherichia coli (FnrEc) controls the expression of a variety of genes, mainly of anaerobic respiration and metabolism (5, 13). It contains a N-terminal cluster of three essential cysteine residues which are supposed to bind together with Cys122 a [4Fe 4S]2+ cluster which is required for O2 sensing (4, 7, 8, 10, 16). A wide variety of gram-negative bacteria co…

inorganic chemicalsIron-Sulfur ProteinsMolecular Sequence DataRestriction MappingMutantBacillusGenetics and Molecular BiologySequence alignmentmacromolecular substancesBacillus subtilisLigandsNitrate reductaseenvironment and public healthMicrobiologyBacterial ProteinsAmino Acid SequenceCysteineBacillus licheniformisMolecular BiologyPeptide sequenceBacillus megateriumSequence Homology Amino AcidbiologyEscherichia coli ProteinsGene Expression Regulation Bacterialbiology.organism_classificationenzymes and coenzymes (carbohydrates)KineticsBiochemistryBacillus megateriumbacteriaSequence AlignmentBacillus subtilisTranscription FactorsCysteineJournal of Bacteriology
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