Crystal structure based design of functional metal/protein hybrids

Ueno, Takafumi; Yokoi, Norihiko; Abe, Satoshi; Watanabe, Yoshihito

doi:10.1016/j.jinorgbio.2007.06.025

Cited by 18 publications

(15 citation statements)

References 60 publications

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“…Interactions between metal oxide NPs and proteins in vivo or in vitro involve coordination and non-covalent interactions [112]. Protein binding to ZnO NPs can result in major structural changes, unfolding behavior, of the periplasmic domain of the ToxR protein by a substantial decrease in the α-helical content of the free protein [98].…”

Section: Key Factors and Toxicity Mechanismsmentioning

confidence: 99%

The Toxic Effects and Mechanisms of CuO and ZnO Nanoparticles

et al. 2012

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Recent nanotechnological advances suggest that metal oxide nanoparticles (NPs) have been expected to be used in various fields, ranging from catalysis and opto-electronic materials to sensors, environmental remediation, and biomedicine. However, the growing use of NPs has led to their release into environment and the toxicity of metal oxide NPs on organisms has become a concern to both the public and scientists. Unfortunately, there are still widespread controversies and ambiguities with respect to the toxic effects and mechanisms of metal oxide NPs. Comprehensive understanding of their toxic effect is necessary to safely expand their use. In this review, we use CuO and ZnO NPs as examples to discuss how key factors such as size, surface characteristics, dissolution, and exposure routes mediate toxic effects, and we describe corresponding mechanisms, including oxidative stress, coordination effects and non-homeostasis effects.

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Section: Key Factors and Toxicity Mechanismsmentioning

confidence: 99%

The Toxic Effects and Mechanisms of CuO and ZnO Nanoparticles

et al. 2012

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“…22 Knowing all the iron-binding sites in ferritin–protein cages is important not only for understanding biological function but also for designing metal sites in ferritin–protein nanocages for nanodevices and nanocatalysts. 7,8,23 …”

Section: Introductionmentioning

confidence: 99%

Moving Metal Ions through Ferritin−Protein Nanocages from Three-Fold Pores to Catalytic Sites

et al. 2010

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Ferritin nanocages synthesize ferric oxide minerals, containing hundreds to thousands of Fe(III) diferric oxo/hydroxo complexes, by reactions of Fe(II) ions with O2 at multiple di-iron catalytic centers. Ferric–oxy multimers, tetramers, and/or larger mineral nuclei form during postcatalytic transit through the protein cage, and mineral accretion occurs in the central cavity. We determined how Fe(II) substrates can access catalytic sites using frog M ferritins, active and inactivated by ligand substitution, crystallized with 2.0 M Mg(II) ± 0.1 M Co(II) for Co(II)-selective sites. Co(II) inhibited Fe(II) oxidation. High-resolution (<1.5 Å) crystal structures show (1) a line of metal ions, 15 Å long, which penetrates the cage and defines ion channels and internal pores to the nanocavity that link external pores to the cage interior, (2) metal ions near negatively charged residues at the channel exits and along the inner cavity surface that model Fe(II) transit to active sites, and (3) alternate side-chain conformations, absent in ferritins with catalysis eliminated by amino acid substitution, which support current models of protein dynamics and explain changes in Fe–Fe distances observed during catalysis. The new structural data identify a ~27-Å path Fe(II) ions can follow through ferritin entry channels between external pores and the central cavity and along the cavity surface to the active sites where mineral synthesis begins. This “bucket brigade” for Fe(II) ion access to the ferritin catalytic sites not only increases understanding of biological nanomineral synthesis but also reveals unexpected design principles for protein cage-based catalysts and nanomaterials.

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“…Transition-metal complexes attached to biomolecules have, for example, been used as anticancer agents, [3,4] radioactive [4][5][6][7][8][9] or luminescent [10][11][12] labels, paramagnetic NMR probes, [13] or semisynthetic metalloenzymes in catalysis. [14][15][16][17][18][19][20][21][22][23][24][25][26][27][28] The incorporation of transition-metal complexes into proteins can be accomplished by a variety of different methods, Abstract: The first crystal structures of lipases that have been covalently modified through site-selective inhibition by different organometallic phosphonatepincer-metal complexes are described. Two ECE-pincer-type d 8 -metal complexes, that is, platinum (1) E= NMe 2 or SMe) were introduced prior to crystallization and have been shown to bind selectively to the Ser 120 residue in the active site of the lipase cutinase to give cut-1 (platinum) or cut-2 (palladium) hybrids.…”

Section: Introductionmentioning

confidence: 99%

Solid‐State Structural Characterization of Cutinase–ECE‐Pincer–Metal Hybrids

Rutten

Wieczorek

Mannie

et al. 2009

Chemistry A European J

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The first crystal structures of lipases that have been covalently modified through site-selective inhibition by different organometallic phosphonate-pincer-metal complexes are described. Two ECE-pincer-type d(8)-metal complexes, that is, platinum (1) or palladium (2) with phosphonate esters (ECE = [(EtO)-(O=)P(-O-C(6)H(4)-(NO(2))-4)(-C(3)H(6)-4-(C(6)H(2)-(CH(2)E)(2))](-); E = NMe(2) or SMe) were introduced prior to crystallization and have been shown to bind selectively to the Ser(120) residue in the active site of the lipase cutinase to give cut-1 (platinum) or cut-2 (palladium) hybrids. For all five presented crystal structures, the ECE-pincer-platinum or -palladium head group sticks out of the cutinase molecule and is exposed to the solvent. Depending on the nature of the ECE-pincer-metal head group, the ECE-pincer-platinum and -palladium guests occupy different pockets in the active site of cutinase, with concomitant different stereochemistries on the phosphorous atom for the cut-1 (S(P)) and cut-2 (R(P)) structures. When cut-1 was crystallized under halide-poor conditions, a novel metal-induced dimeric structure was formed between two cutinase-bound pincer-platinum head groups, which are interconnected through a single mu-Cl bridge. This halide-bridged metal dimer shows that coordination chemistry is possible with protein-modified pincer-metal complexes. Furthermore, we could use NCN-pincer-platinum complex 1 as site-selective tool for the phasing of raw protein diffraction data, which shows the potential use of pincer-platinum complex 1 as a heavy-atom derivative in protein crystallography.

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Crystal structure based design of functional metal/protein hybrids

Cited by 18 publications

References 60 publications

The Toxic Effects and Mechanisms of CuO and ZnO Nanoparticles

The Toxic Effects and Mechanisms of CuO and ZnO Nanoparticles

Moving Metal Ions through Ferritin−Protein Nanocages from Three-Fold Pores to Catalytic Sites

Solid‐State Structural Characterization of Cutinase–ECE‐Pincer–Metal Hybrids

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