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Metal Binding (metal + binding)
Terms modified by Metal Binding Selected AbstractsA Novel Macromolecular Complex: Fabrication of Monodisperse Colloidal Microspheres by Precipitation Polymerization of Imine Chains and Concomitant Transition Metal BindingADVANCED MATERIALS, Issue 17 2003H. Houjou A series of monodisperse colloidal microspheres has been fabricated by precipitation polymerization of imine chains and concomitant transition metal binding. The resulting metal-bound polyimine microspheres (M-PIMSs, M = Co, Ni, Cu, or Zn, see Figure, which shows Zn-PIMSs) have characteristic diameters in the range from 0.5 to 1.4 ,m, depending on the metal used, and are of interest for applications in photonic devices. [source] Metal-free MIRAS phasing: structure of apo-S100A3ACTA CRYSTALLOGRAPHICA SECTION D, Issue 8 2002Peer R. E. Mittl S100 proteins are involved in metal-dependent intracellular signalling. Metal-free S100A3, a cysteine-rich Ca2+ - and Zn2+ -binding protein, has been crystallized by vapour diffusion under the strict exclusion of oxygen and in the absence of divalent metal ions. Metal binding induces large conformational changes, rendering the apo-S100A3 crystals very sensitive to various metal compounds. Therefore, the structure was solved by MIRAS phasing using potassium iodide and xenon derivatives. Iodide replaces a water molecule at the surface of the S100A3 protein, whereas xenon binds in a hydrophobic cavity at the dimer interface. Despite significant non-isomorphism, the combination of both derivatives was sufficient for structure determination. The overall apo-S100A3 structure resembles the structures of metal-free S100B and S100A6 solution structures. In contrast to the NMR structures, the EF-hand loops are well ordered in the apo-S100A3 crystal structure. In the N-terminal pseudo-EF-hand loop a water molecule occupies the position of the Ca2+ ion. The C-terminal canonical EF-hand loop shows an extended conformation and a different helix arrangement to other S100/metal complex crystal structures. [source] Partial oxidation and oxidative polymerization of metallothioneinELECTROPHORESIS, Issue 20 2008Hajo Haase Abstract One mechanism for regulation of metal binding to metallothionein (MT) involves the non-enzymatic or enzymatic oxidation of its thiols to disulfides. Formation and speciation of oxidized MT have not been investigated in detail despite the biological significance of this redox biochemistry. While metal ion-bound thiols in MT are rather resistant towards oxidation, free thiols are readily oxidized. MT can be partially oxidized to a state in which some of its thiols remain reduced and bound to metal ions. Analysis of the oxidation products with SDS-PAGE and a thiol-specific labeling technique, employing eosin-5-iodoacetamide, demonstrates higher-order aggregates of MT with intermolecular disulfide linkages. The polymerization follows either non-enzymatic or enzymatic oxidation, indicating that it is a general property of oxidized MT. Supramolecular assemblies of MT add new perspectives to the complex redox and metal equilibria of this protein. [source] Creating metal-spiked bed sediments: A case study from Orewa estuary, New Zealand,ENVIRONMENTAL TOXICOLOGY & CHEMISTRY, Issue 10 2008Xueqiang Lu Abstract Spiking sediments to achieve target concentrations of heavy metal pollutants is a key step in sediment toxicity tests. It is difficult, however, to ensure that metals in an artificially spiked sediment will behave naturally. A method has been developed in the present study to create Cu-, Pb-, and Zn-spiked sediments in which naturally occurring adsorption onto sediment surfaces is the dominant process binding the metals and in which precipitation of readily redissolved minerals and other metal-bearing phases (artifacts of the spiking procedure) are avoided. Uncontaminated bed sediment from an intertidal mudflat in the Orewa estuary, New Zealand, was characterized in terms of existing metal content, optimal adsorption pH, and adsorption capacity. Competitive adsorption between Cu and Pb as well as complexation by seawater anions only slightly affected metal adsorption from seawater. Surface complexation modeling indicated that iron oxide surfaces in the sediment likely were dominating metal adsorption processes. Spiking experiments were designed using these established adsorption characteristics but with significantly higher (>100-fold) concentrations of sediments and dissolved metals and a liquid to solid (L:S) ratio of approximately 5.5. An equilibration time of at least 36 h was required to achieve a reproducible target metal concentration, which could be reliably predicted from the L:S ratio and the initial metal concentration in the spiking solution. Adsorption equilibrium remained the process governing metal binding to the sediment, and no indication was observed that the adsorption capacity of the sediment had been exceeded or that additional metal-bearing phases had been formed. [source] Comparison of Cd, Cu, and Zn toxic effects on four marine phytoplankton by pulse-amplitude-modulated fluorometryENVIRONMENTAL TOXICOLOGY & CHEMISTRY, Issue 10 2005Ai-Jun Miao Abstract The toxic effects of Cd, Cu, and Zn on four different marine phytoplankton, Dunaliella tertiolecta, Prorocentrum minimum, Synechococcus sp., and Thalassiosira weissflogii, were examined by comparing the cell-specific growth rate, pulse-amplitude-modulated (PAM) parameters (maximum photosystem II quantum yield ,M and operational quantum yield ,'M), chlorophyll a content, and cellular metal concentration, over a 96-h period. The calculated no-observed-effect concentration (NOEC) based on both cell-specific growth rate and two PAM parameters (,M and ,'M) were mostly identical. Thus, these PAM parameters and cell-specific growth rate were comparable in their sensitivities as the biomarkers for trace metal toxicity to marine phytoplankton. The cyanobacteria Synechococcus sp. was the most sensitive species among the four algal species tested because of its higher cell surface to volume ratio. The toxicity of the three tested metals followed the order of Cd > Cu > Zn based on the cellular metal concentration of the four algae at the NOEC. The cellular metal bioaccumulation followed the same Freundlich isotherm for each metal regardless of the algal species, indicating that the metal accumulation was a nonmetabolic process under high ambient metal concentrations and that the cell surface metal binding was comparable among the different species. For all the algae examined in our study, the bioaccumulation potentials of Cu and Zn were similar to each other, while the Cd bioaccumulation was much lower under environmentally realistic metal concentration. [source] Comparative metal binding and genomic analysis of the avian (chicken) and mammalian metallothioneinFEBS JOURNAL, Issue 3 2006Laura Villarreal Chicken metallothionein (ckMT) is the paradigm for the study of metallothioneins (MTs) in the Aves class of vertebrates. Available literature data depict ckMT as a one-copy gene, encoding an MT protein highly similar to mammalian MT1. In contrast, the MT system in mammals consists of a four-member family exhibiting functional differentiation. This scenario prompted us to analyse the apparently distinct evolutionary patterns followed by MTs in birds and mammals, at both the functional and structural levels. Thus, in this work, the ckMT metal binding abilities towards Zn(II), Cd(II) and Cu(I) have been thoroughly revisited and then compared with those of the mammalian MT1 and MT4 isoforms, identified as zinc- and copper-thioneins, respectively. Interestingly, a new mechanism of MT dimerization is reported, on the basis of the coordinating capacity of the ckMT C-terminal histidine. Furthermore, an evolutionary study has been performed by means of in silico analyses of avian MT genes and proteins. The joint consideration of the functional and genomic data obtained questions the two features until now defining the avian MT system. Overall, in vivo and in vitro metal-binding results reveal that the Zn(II), Cd(II) and Cu(I) binding abilities of ckMT lay between those of mammalian MT1 and MT4, being closer to those of MT1 for the divalent metal ions but more similar to those of MT4 for Cu(I). This is consistent with a strong functional constraint operating on low-copy number genes that must cope with differentiating functional limitation. Finally, a second MT gene has been identified in silico in the chicken genome, ckMT2, exhibiting all the features to be considered an active coding region. The results presented here allow a new insight into the metal binding abilities of warm blooded vertebrate MTs and their evolutionary relationships. [source] A Novel Macromolecular Complex: Fabrication of Monodisperse Colloidal Microspheres by Precipitation Polymerization of Imine Chains and Concomitant Transition Metal BindingADVANCED MATERIALS, Issue 17 2003H. Houjou A series of monodisperse colloidal microspheres has been fabricated by precipitation polymerization of imine chains and concomitant transition metal binding. The resulting metal-bound polyimine microspheres (M-PIMSs, M = Co, Ni, Cu, or Zn, see Figure, which shows Zn-PIMSs) have characteristic diameters in the range from 0.5 to 1.4 ,m, depending on the metal used, and are of interest for applications in photonic devices. [source] Mitochondrial copper metabolism and delivery to cytochrome c oxidaseIUBMB LIFE, Issue 7 2008Darryl Horn Abstract Metals are essential elements of all living organisms. Among them, copper is required for a multiplicity of functions including mitochondrial oxidative phosphorylation and protection against oxidative stress. Here we will focus on describing the pathways involved in the delivery of copper to cytochrome c oxidase (COX), a mitochondrial metalloenzyme acting as the terminal enzyme of the mitochondrial respiratory chain. The catalytic core of COX is formed by three mitochondrially-encoded subunits and contains three copper atoms. Two copper atoms bound to subunit 2 constitute the CuA site, the primary acceptor of electrons from ferrocytochrome c. The third copper, CuB, is associated with the high-spin heme a3 group of subunit 1. Recent studies, mostly performed in the yeast Saccharomyces cerevisiae, have provided new clues about 1) the source of the copper used for COX metallation; 2) the roles of Sco1p and Cox11p, the proteins involved in the direct delivery of copper to the CuA and CuB sites, respectively; 3) the action mechanism of Cox17p, a copper chaperone that provides copper to Sco1p and Cox11p; 4) the existence of at least four Cox17p homologues carrying a similar twin CX9C domain suggestive of metal binding, Cox19p, Cox23p, Pet191p and Cmc1p, that could be part of the same pathway; and 5) the presence of a disulfide relay system in the intermembrane space of mitochondria that mediates import of proteins with conserved cysteines motifs such as the CX9C characteristic of Cox17p and its homologues. The different pathways are reviewed and discussed in the context of both mitochondrial COX assembly and copper homeostasis. © 2008 IUBMB IUBMB Life, 60(7): 421,429, 2008 [source] Alpha-synuclein and its role in metal binding: Relevance to Parkinson's diseaseJOURNAL OF NEUROSCIENCE RESEARCH, Issue 3 2008Josephine A. Wright Abstract Parkinson's disease and some other neurodegenerative disorders are associated with a protein that can aggregate and form fibrils called alpha-synuclein. Like many other proteins associated with neurodegenerative disorders, this protein has no known function, and the mechanism by which it could cause diseases is poorly defined. It was recently suggested that it binds copper. This review assesses what is known about alpha-synuclein and its interaction with metals. © 2007 Wiley-Liss, Inc. [source] Structure of laminin-binding adhesin (Lmb) from Streptococcus agalactiaeACTA CRYSTALLOGRAPHICA SECTION D, Issue 12 2009Preethi Ragunathan Adhesion/invasion of pathogenic bacteria is a critical step in infection and is mediated by surface-exposed proteins termed adhesins. The crystal structure of recombinant Lmb, a laminin-binding adhesin from Streptococcus agalactiae, has been determined at 2.5,Å resolution. Based on sequence and structural homology, Lmb was placed into the cluster 9 family of the ABC (ATP-binding cassette) transport system. The structural organization of Lmb closely resembles that of ABC-type solute-binding proteins (SBPs), in which two structurally related globular domains interact with each other to form a metal-binding cavity at the interface. The bound zinc in Lmb is tetrahedrally coordinated by three histidines and a glutamate from both domains. A comparison of Lmb with other metal transporters revealed an interesting feature of the dimerization of molecules in the crystallographic asymmetric unit in all zinc-binding transporters. A closer comparison of Lmb with the zinc-binding ZnuA from Escherichia coli and Synechocystis 6803 suggested that Lmb might undergo a unique structural rearrangement upon metal binding and release. The crystal structure of Lmb provides an impetus for further investigations into the molecular basis of laminin binding by human pathogens. Being ubiquitous in all serotypes of group B streptococcus (GBS), the structure of Lmb may direct the development of an efficient vaccine. [source] Purification, crystallization and preliminary X-ray analysis of an aminoacylhistidine dipeptidase (PepD) from Vibrio alginolyticusACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 3 2009Chin-Yuan Chang The aminoacylhistidine dipeptidase (PepD) protein encoded by Vibrio alginolyticus pepD was successfully overexpressed and characterized and the putative active-site residues responsible for metal binding and catalysis were identified. The purified enzyme contained two zinc ions per monomer. The recombinant dipeptidase enzyme, which was identified as a homodimer in solution, exhibited broad substrate specificity for Xaa-His dipeptides, with highest activity towards the His-His dipeptide. The purified protein was crystallized using the hanging-drop vapour-diffusion method. Preliminary crystallographic analysis showed that the crystal belonged to space group P61 or P65, with unit-cell parameters a = b = 80.42, c = 303.11,Å. The crystal contained two molecules per asymmetric unit and the predicted solvent content was 53.4%. [source] The effect of the side chain length of Asp and Glu on coordination structure of Cu2+ in a de novo designed proteinBIOPOLYMERS, Issue 11 2009Daigo Shiga Abstract Metal ions in proteins are important not only for the formation of the proper structures but also for various biological activities. For biological functions such as hydrolysis and oxidation, metal ions often adopt unusual coordination structures. We constructed a stable scaffold for metal binding to create distorted metal coordination structures. A stable four stranded ,-helical coiled-coil structure was used as the scaffold, and the metal binding site was in the cavity created at the center of the structure. Two His residues and one Asp or Glu residue were used to coordinate the metal ions, AM2D and AM2E, respectively. Cu2+ bound to AM2D with an equatorial planar coordination structure with two His, one Asp, and H2O as detected by electron spin resonance and UV spectral analyzes. On the other hand, Cu2+ had a slightly distorted square planar structure when it bound two His and Glu in AM2E, due to the longer side-chain of the Glu residue as compared to the Asp residue. Computational analysis also supported the distorted coordination structure of Cu2+ in AM2E. This construct should be useful to create various coordinations of metal ions for catalytic functions. © 2009 Wiley Periodicals, Inc. Biopolymers 91: 907,916, 2009. This article was originally published online as an accepted preprint. The "Published Online" date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com [source] Adsorption of Cadmium Ion and Gallium Ion to Immobilized Metallothionein Fusion ProteinBIOTECHNOLOGY PROGRESS, Issue 6 2002Masaaki Terashima A fusion protein made from maltose binding protein (pmal) and human metallothionein (MT) was expressed using E. coli. The purified recombinant protein (pmal-MT) was immobilized on Chitopearl resin, and characteristics of pmal-MT for metal binding were evaluated. As expected from the tertiary structure of metallothionein, the pmal-MT ligand adsorbed 12.1 cadmium molecules per one molecule of the ligand at pH 5.2. The pmal-MT ligand also bound 26.6 gallium molecules per one molecule of the ligand at pH 6.5. Neither cadmium ion nor gallium ion bound to a control protein bovine serum albumin (BSA). Adsorption isotherms for both ions were correlated by Langmuir-type equations. Two types of binding sites have been elucidated on the basis of HSAB (hard and soft acid and base) theory. It was suggested that gallium ion specifically binds to amino acid residues containing oxygen and nitrogen atoms, while cadmium ion binds to specific binding sites formed by multiple cysteine residues. The pmal-MT ligand bound these metals in the concentration range of 0.2,1.0 mM, and the bound metal ions could be eluted under relatively mild conditions (pH 2.0). The pmal-MT Chitopearl resin was stable and could be used repeatedly without loss of binding activity. Thus, this new ligand would be useful for recovery of toxic heavy metals and/or valuable metal ions from various aqueous solutions. [source] Self-assembly of multinuclear complexes with enantiomerically pure chiral binaphthoxy imine ligands: Effect of the alkyl spacer connecting two binaphthyl units on the metal bindingCHIRALITY, Issue 9 2006Takeshi Maeda Abstract Metal complexing behavior of enantiomerically pure ,,,-diiminoalkanes possessing the two terminal binaphthyl units (L1 and L2) was studied. The ligands L1 and L2 were prepared by the reaction of optically pure 2,-butoxy-3-formyl-2-hydroxy-1,1,-binaphthyl with propane and pentane diamines. Reactions of L1 and L2 with equimolar amount of Cu(OAc)2 afforded quantitatively multinuclear complexes 1. The structure of 1 was confirmed by MALDI,TOF MS spectroscopy, X-ray single-crystal-structure analysis, and UV/vis and CD spectroscopic analyses. The reaction of L1 having a 1,3-propanediyl spacer resulted in the formation of a self-assembled product, which was assigned as enantiopure trinuclear circular helicate 1a, while the ligand having a 1,5-pentanediyl spacer L2 gave a different self-assembled product, dinuclear side-by-side complex 1b. The circular dichroism (CD) spectrum of 1a in solution showed intense Cotton effects in both the ,,,* transition of the naphthalene units and the LMCT region of the N,O -chelate moieties. The CD spectrum of 1b was completely different from that of 1a; in particular the Cotton effects in the LMCT region were very weak, contrary to those of 1a. These results suggest that 1a retains some chirality induced on the N,O -chelating moieties even in solution, while the induced chirality on the N,O -chelating moieties in 1b is not very significant, being consistent with the consequences of the X-ray single-crystal-structure studies. Chirality, 2006. © 2006 Wiley-Liss, Inc. [source] | |||||||||||||