Search results for "Metal binding"

showing 10 items of 11 documents

Adaptative biochemical pathways and regulatory networks in Klebsiella oxytoca BAS-10 producing a biotechnologically relevant exopolysaccharide during…

2012

Abstract Background A bacterial strain previously isolated from pyrite mine drainage and named BAS-10 was tentatively identified as Klebsiella oxytoca. Unlikely other enterobacteria, BAS-10 is able to grow on Fe(III)-citrate as sole carbon and energy source, yielding acetic acid and CO2 coupled with Fe(III) reduction to Fe(II) and showing unusual physiological characteristics. In fact, under this growth condition, BAS-10 produces an exopolysaccharide (EPS) having a high rhamnose content and metal-binding properties, whose biotechnological applications were proven as very relevant. Results Further phylogenetic analysis, based on 16S rDNA sequence, definitively confirmed that BAS-10 belongs t…

Proteomicsmetal binding exopolysaccharideRhamnoseeducationlcsh:QR1-502BioengineeringSettore BIO/19 - Microbiologia GeneraleFerric CompoundsApplied Microbiology and BiotechnologyCitric Acidlcsh:Microbiology03 medical and health scienceschemistry.chemical_compoundAcetic acidRNA Ribosomal 16SGene Regulatory NetworksPhylogeny030304 developmental biology2. Zero hunger0303 health sciencesbiology030306 microbiologyResearchKlebsiella oxytocaKlebsiella oxytocabiology.organism_classificationBacterial strainKlebsiella oxytoca; 2D-DIGE analysis; metal binding exopolysaccharide;Metabolic pathwaychemistryBiochemistryFermentation2D-DIGE analysiFermentationEnergy sourceCitric acidMetabolic Networks and PathwaysBiotechnology
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Plasma Proteins, Yolk Proteins and Metal-Binding Proteins

1994

The extracellular fluid of the metazoans is not only a transport vehicle but also, for the majority of the body’s cells, their growth environment. Proteins play an important role here, providing colloid-osmotic pressure and acting as buffers. The most important parameter in this respect is their concentration which, depending upon the species, the developmental stage and the physiological conditions, can vary from less than 1 to more than 200 mg/ml (Table 5.1). In addition to these general functions, individual plasma proteins have various specific roles, e.g. in the transport of substances, in defence reactions, in blood clotting or in the solution of clots. At least in the case of the mor…

Retinol binding proteinMembrane proteinAntifreeze proteinChemistryExtracellular fluidExtracellularBiophysicsMetal binding proteinsPlant lipid transfer proteinsBlood proteins
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Copper binding capacity of root exudates of cultivated plants and associated weeds

2001

International audience; Cu binding to root exudates of two cultivated plants, wheat (Triticum aestivum) and rape (Brassica napus), and two weeds associated with wheat, dog daisy (Matricaria inodora) and cornflower (Centaurea cyanus), was studied in vitro under hydroponic and sterile conditions. Nutrient solutions were prepared with or without P. A MetPLATE microbiological test was used to assess the metal complexing capacity of root exudates. In the P-deficient solutions, no exudation was observed for any of the four plants; consequently, no Cu binding occurred. When P was present in the nutrient solutions, the plant exudates displayed differing abilities to complex Cu. No difference was de…

[SDV]Life Sciences [q-bio]BrassicaSoil Science010501 environmental sciencesRELATION PLANTE SOL01 natural sciencesMicrobiologyMetalNutrientCopper bindingBotanyMatricaria0105 earth and related environmental sciencesCultivated plant taxonomybiologyfood and beverages04 agricultural and veterinary sciencesbiology.organism_classificationvisual_art[SDE]Environmental Sciences040103 agronomy & agriculturevisual_art.visual_art_medium0401 agriculture forestry and fisheriesHeavy metal bindingCentaurea cyanusAgronomy and Crop Science
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Peptidomimetics – An infinite reservoir of metal binding motifs in metabolically stable and biologically active molecules

2020

The involvement of metal ions in interactions with therapeutic peptides is inevitable. They are one of the factors able to fine-tune the biological properties of antimicrobial peptides, a promising group of drugs with one large drawback - a problematic metabolic stability. Appropriately chosen, proteolytically stable peptidomimetics seem to be a reasonable solution of the problem, and the use of D-, β-, γ-amino acids, unnatural amino acids, azapeptides, peptoids, cyclopeptides and dehydropeptides is an infinite reservoir of metal binding motifs in metabolically stable, well-designed, biologically active molecules. Below, their specific structural features, metal-chelating abilities and anti…

PeptidomimeticMetal ions in aqueous solutionAntimicrobial peptidesMetal binding sites010402 general chemistryPeptides Cyclic01 natural sciencesBiochemistryInorganic ChemistryPeptoidsHumansMoleculeAmino AcidsChelating Agentschemistry.chemical_classificationBinding SitesBacteria010405 organic chemistryMetal bindingStereoisomerismBiological activityAntimicrobialCombinatorial chemistryAnti-Bacterial Agents0104 chemical sciencesAmino acidchemistryAntimicrobial peptidesPeptidomimeticsJournal of Inorganic Biochemistry
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Computing Metal-Binding Proteins for Therapeutic Benefit

2021

Over one third of biomolecules rely on metal ions to exert their cellular functions. Metal ions can play a structural role by stabilizing the structure of biomolecules, a functional role by promoting a wide variety of biochemical reactions, and a regulatory role by acting as messengers upon binding to proteins regulating cellular metal-homeostasis. These diverse roles in biology ascribe critical implications to metal-binding proteins in the onset of many diseases. Hence, it is of utmost importance to exhaustively unlock the different mechanistic facets of metal-binding proteins and to harness this knowledge to rationally devise novel therapeutic strategies to prevent or cure pathological st…

Functional roleModels MolecularMetalloenzymesCellular functionsMetallo enzymeMolecular ConformationComputational biologyMolecular Dynamics01 natural sciencesBiochemistryQM/MMDockingMetals HeavyDrug DiscoveryBiochemical reactionsMetal transportersGeneral Pharmacology Toxicology and PharmaceuticsPharmacology010405 organic chemistryOrganic ChemistryComputational BiologyMetal binding proteins0104 chemical sciences010404 medicinal & biomolecular chemistryDocking (molecular)Settore CHIM/03 - Chimica Generale E InorganicaMolecular MedicineCarrier Proteins
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Native Electrospray-based Metabolomics Enables the Detection of Metal-binding Compounds

2019

AbstractMetals are essential for the molecular machineries of life, and microbes have evolved a variety of small molecules to acquire, compete for, and utilize metals. Systematic methods for the discovery of metal-small molecule complexes from biological samples are limited. Here we describe a two-step native electrospray ionization mass spectrometry method, in which double-barrel post-column metal-infusion and pH adjustment is combined with ion identity molecular networking, a rule-based informatics workflow. This method can be used to identify metal-binding compounds in complex samples based on defined mass (m/z) offsets of ion features with the same chromatographic profiles. As this nati…

0303 health sciencesElectrosprayMetal bindingElectrospray ionization010402 general chemistryMass spectrometry01 natural sciencesCombinatorial chemistrySmall molecule0104 chemical sciencesIon03 medical and health sciencesMetabolomicsMolecule030304 developmental biology
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Metal Complexes of Two Specific Regions of ZnuA, a Periplasmic Zinc(II) Transporter from Escherichia coli

2020

The crystal structure of ZnZnuA from Escherichia coli reveals two metal binding sites. (i) The primary binding site, His143, is located close the His-rich loop (residues 116-138) and plays a significant role in Zn(II) acquisition. (ii) The secondary binding site involves His224. In this work, we focus on understanding the interactions of two metal ions, Zn(II) and Cu(II), with two regions of ZnuA, which are possible anchoring sites for Zn(II): Ac-115MKSIHGDDDDHDHAEKSDEDHHHGDFNMHLW145-NH2 (primary metal binding site) and Ac-223GHFTVNPEIQPGAQRLHE240-NH2 (secondary metal binding site). The histidine-rich loop (residues 116-138) has a role in the capture of zinc(II), which is then further deliv…

010405 organic chemistryStereochemistryChemistrychemistry.chemical_elementMetal Binding SitePeriplasmic spaceZinc010402 general chemistryLigand (biochemistry)01 natural sciences0104 chemical sciencesInorganic ChemistryMetalchemistry.chemical_compoundvisual_artvisual_art.visual_art_mediumImidazolePhysical and Theoretical ChemistryBinding siteHistidine
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Frontispiece: Positive Allosteric Control of Guests Encapsulation by Metal Binding to Covalent Porphyrin Cages

2019

chemistry.chemical_compoundchemistryCovalent bondMetal bindingOrganic ChemistryAllosteric regulationSupramolecular chemistryGeneral ChemistryCombinatorial chemistryPorphyrinCatalysisEncapsulation (networking)Chemistry - A European Journal
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Poly-Xaa Sequences in Proteins - Biological Role and Interactions with Metal Ions: Chemical and Medical Aspects

2016

Background: The understanding of the bioinorganic and coordination chemistry of metalloproteins containing unusual poly-Xaa sequences, in which a single amino acid is repeated consecutively, is crucial for describing their metal binding-structure-function relationship, and therefore also crucial for understanding their medicinal potential. To the best of our knowledge, this is the first systematic review on metal complexes with polyXaa sequences. Methods: We performed a thorough search of high quality peer reviewed literature on poly-Xaa type of sequences in proteins, focusing on their biological importance and on their interactions with metal ions. Results: 228 papers were included in the…

Metal ions in aqueous solutionComputational biology010402 general chemistry01 natural sciencesBiochemistryCoordination complexTurn (biochemistry)metal chaperonesCoordination ComplexesDrug DiscoveryMetalloproteinHumansAmino Acid SequenceSingle amino acidAmino AcidsBinding siteantimicrobial therapeuticsIonsPharmacologychemistry.chemical_classification010405 organic chemistryMetal bindingOrganic Chemistrymetal ionsProteinsBioinorganic chemistry0104 chemical scienceschemistryChemical physicsMetal-protein complexespoly-Xaa peptide sequencesMolecular MedicineCurrent Medicinal Chemistry
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N-Glycosylamines of 4,6-O-ethylidene-alpha-D-glucopyranose: synthesis, characterisation and structure of CO2H, Cl and F ortho-substituted phenyl deri…

2000

A saccharide based ligand suitable for metal binding (HLCOOH) has been synthesized using 4,6-O-ethylidene-alpha-D-glucopyranose (4,6-O-EGP) and anthranilic acid. A few analogous glycosylamines with chloro and fluoro ortho substitutions have also been synthesized and characterised. Complexes of HLCOOH with Na+, K+, Mg2+, Ca2+, Ba2+, Cd2+ and Hg2+ have been isolated and characterised fully. The crystal structures of 4,6-O-EGP, the chloro analogue of HLCOOH and the K+ complex of L-COOH are established. The anomeric nature, orientation of the binding core and the co-ordination aspects of K+ have been derived from these structures.

chemistry.chemical_classificationAnomerPlatinum(Iv)Metal bindingLigandStereochemistryDiacetoneglucoseGeneral ChemistryCrystal structureNickel(Ii) ComplexesD-GlucopyranoseEnantioselective SynthesesMetalCrown-Etherchemistry.chemical_compoundChemistrychemistryvisual_artCoordinationAnthranilic acidvisual_art.visual_art_mediumTitanium-Carbohydrate ComplexesGlycoside LigandsSugarsCrown etherIndraStra Global
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