The effect of non-coordinating side chains on the metal binding affinities of peptides of histidine

Polyhedron ◽  
2013 ◽  
Vol 62 ◽  
pp. 7-17 ◽  
Author(s):  
Ildikó Turi ◽  
Daniele Sanna ◽  
Eugenio Garribba ◽  
Giuseppe Pappalardo ◽  
Imre Sóvágó
Keyword(s):  
Metal Binding ◽  
Side Chains ◽  
Binding Affinities

scholarly journals Synthesis of New Derivatives of BEDT-TTF: Installation of Alkyl, Ethynyl, and Metal-Binding Side Chains and Formation of Tris(BEDT-TTF) Systems

2021 ◽  
Vol 7 (8) ◽  
pp. 110
Author(s):  
Songjie Yang ◽  
Matteo Zecchini ◽  
Andrew Brooks ◽  
Sara Krivickas ◽  
Desiree Dalligos ◽  
...  
Keyword(s):  
Metal Binding ◽  
Tricarboxylic Acid ◽  
Metal Salts ◽  
Side Chain ◽  
Side Chains ◽  
Ethynyl Group ◽  
X Ray ◽  
Transition Metal Salts ◽  
Alkyl Side Chains ◽  
Derivatives Of

The syntheses of new BEDT-TTF derivatives are described. These comprise BEDT-TTF with one ethynyl group (HC≡C-), with two (n-heptyl) or four (n-butyl) alkyl side chains, with two trans acetal (-CH(OMe)2) groups, with two trans aminomethyl (-CH2NH2) groups, and with an iminodiacetate (-CH2N(CH2CO2−)2 side chain. Three transition metal salts have been prepared from the latter donor, and their magnetic properties are reported. Three tris-donor systems are reported bearing three BEDT-TTF derivatives with ester links to a core derived from benzene-1,3,5-tricarboxylic acid. The stereochemistry and molecular structure of the donors are discussed. X-ray crystal structures of two BEDT-TTF donors are reported: one with two CH(OMe)2 groups and with one a -CH2N(CH2CO2Me)2 side chain.

A micro-scale method for determining relative metal-binding affinities of proteins

1997 ◽  
Vol 8 (3) ◽  
pp. 215-218 ◽  
Author(s):  
Jens Sommer-Knudsen ◽  
Antony Bacic
Keyword(s):  
Metal Binding ◽  
Binding Affinities ◽  
Micro Scale ◽  
Scale Method

Metal Binding Affinities ofArabidopsisZinc and Copper Transporters: Selectivities Match the Relative, but Not the Absolute, Affinities of their Amino-Terminal Domains,

Biochemistry ◽  
2009 ◽  
Vol 48 (49) ◽  
pp. 11640-11654 ◽  
Author(s):  
Matthias Zimmermann ◽  
Oliver Clarke ◽  
Jacqui M. Gulbis ◽  
David W. Keizer ◽  
Renee S. Jarvis ◽  
...  
Keyword(s):  
Metal Binding ◽  
Binding Affinities ◽  
Amino Terminal ◽  
Copper Transporters ◽  
The Absolute ◽  
Terminal Domains

Synthesis and structure of a coordination polymer based on 6-furylpurine

2016 ◽  
Vol 71 (10) ◽  
pp. 1051-1055
Author(s):  
Indranil Sinha ◽  
Jutta Kösters ◽  
Jens Müller
Keyword(s):  
Coordination Polymer ◽  
Metal Binding ◽  
Density Functional ◽  
Density Functional Theory Calculations ◽  
Binding Affinities ◽  
Purine Derivative ◽  
Functional Theory ◽  
Binding Behavior ◽  
Nitrogen Donor ◽  
Aqueous Conditions

AbstractThe synthesis and structure of [Ag(9-methyl-6-furylpurine)(NO3)]n are reported. The title compound represents a rare example of a purine derivative metalated at all three endocyclic nitrogen atoms. It forms a two-dimensional coordination polymer comprising 14-membered trinuclear metallacycles. Density functional theory calculations helped to understand the metal-binding behavior of the 6-furylpurine moiety by showing the silver(I)-binding affinities of all three nitrogen donor atoms to be essentially identical under aqueous conditions.

A comparative study on the nickel binding ability of peptides containing separate cysteinyl residues

2019 ◽  
Vol 48 (44) ◽  
pp. 16800-16811
Author(s):  
Györgyi Szunyog ◽  
Aliz Laskai ◽  
Dóra Szűcs ◽  
Imre Sóvágó ◽  
Katalin Várnagy
Keyword(s):  
Comparative Study ◽  
Metal Binding ◽  
Binding Affinities ◽  
Binding Modes ◽  
Binding Ability ◽  
Nickel Binding ◽  
Major Species

The different metal binding affinities of two cysteine containing oligopeptides are related to the different binding modes of the major species.

Enhancement of enzymatic activity for myoglobins by modification of heme-propionate side chains

2004 ◽  
Vol 08 (03) ◽  
pp. 255-264 ◽  
Author(s):  
Takashi Hayashi ◽  
Hideaki Sato ◽  
Takashi Matsuo ◽  
Takaaki Matsuda ◽  
Yutaka Hitomi ◽  
...  
Keyword(s):  
Binding Site ◽  
Metal Binding ◽  
Protein Function ◽  
Site Directed Mutagenesis ◽  
Side Chain ◽  
Side Chains ◽  
Cytochrome P450 Enzyme ◽  
Prosthetic Group ◽  
Heme Pocket ◽  
P450 Enzyme

The modification of myoglobin is an attractive process not only for understanding its molecular mechanism but also for engineering the protein function. The strategy of myoglobin functionalization can be divided into at least two approaches: site-directed mutagenesis and reconstitution with a non-natural prosthetic group. The former method enables us to mainly modulate the physiological function, while the latter has the advantage of introducing a new function on the protein. Particularly, replacement of the native hemin with an artificially created hemin having hydrophobic moieties at the terminal of the heme-propionate side chains serves as an appropriate substrate-binding site near the heme pocket, and consequently enhances the peroxidase and peroxygenase activities for the reconstituted myoglobin. In addition, the incorporation of the synthetic hemin bearing modified heme-propionates into an appropriate apomyoglobin mutant drastically enhances the peroxidase activity. In contrast, to convert myoglobin into a cytochrome P450 enzyme, a flavin moiety as an electron transfer mediator was introduced at the terminal of the heme-propionate side chain. The flavomyoglobin catalyzes the deformylation of 2-phenylpropanal in the presence of NADH under aerobic conditions through the peroxoanion formation from the oxygenated species. In addition, modification of the heme-propionate side chains has an significant influence on regulating the reactivity of the horseradish peroxidase. Furthermore, the heme-propionate side chain can form a metal binding site with a carboxylate residue in the heme pocket. These studies indicate that modification of the heme-propionate side chains can be a new and effective way to engineer functions for the hemoproteins.

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