scholarly journals The protonation state and binding mode in a metal coordination complex from the charge measured in solution by electrophoretic NMR

2013 ◽  
Vol 5 (7) ◽  
pp. 1648 ◽  
Author(s):  
Marianne Giesecke ◽  
Zoltán Szabó ◽  
István Furó
Keyword(s):  
Binding Mode ◽  
Coordination Complex ◽  
Metal Coordination ◽  
Protonation State

A Photoluminescent Metal Coordination Complex Constructed from Hydrothermal in situ Generated Quinoline-monoacyl­hydrazidate Ligand

2015 ◽  
Vol 642 (1) ◽  
pp. 20-24 ◽  
Author(s):  
Qing-Feng Yang ◽  
Hong-Cun Bai ◽  
Bing Li ◽  
Min Luo ◽  
Juan Jin ◽  
...  
Keyword(s):  
Coordination Complex ◽  
Metal Coordination

Chromogenic detection of Sarin by discolouring decomplexation of a metal coordination complex

2013 ◽  
Vol 49 (79) ◽  
pp. 8946 ◽  
Author(s):  
Lucie Ordronneau ◽  
Alexandre Carella ◽  
Miroslav Pohanka ◽  
Jean-Pierre Simonato
Keyword(s):  
Coordination Complex ◽  
Metal Coordination

scholarly journals Structure and two-metal mechanism of a eukaryal nick-sealing RNA ligase

2015 ◽  
Vol 112 (45) ◽  
pp. 13868-13873 ◽  
Author(s):  
Mihaela-Carmen Unciuleac ◽  
Yehuda Goldgur ◽  
Stewart Shuman
Keyword(s):  
Reaction Pathway ◽  
Domain Architecture ◽  
Coordination Complex ◽  
Metal Coordination ◽  
Rna Repair ◽  
Rna Ligase ◽  
Dna Ligases ◽  
Catalytic Metal ◽  
Rna Capping ◽  
Unique Domain

ATP-dependent RNA ligases are agents of RNA repair that join 3′-OH and 5′-PO4 RNA ends. Naegleria gruberi RNA ligase (NgrRnl) exemplifies a family of RNA nick-sealing enzymes found in bacteria, viruses, and eukarya. Crystal structures of NgrRnl at three discrete steps along the reaction pathway—covalent ligase-(lysyl-Nζ)–AMP•Mn2+ intermediate; ligase•ATP•(Mn2+)2 Michaelis complex; and ligase•Mn2+ complex—highlight a two-metal mechanism of nucleotidyl transfer, whereby (i) an enzyme-bound “catalytic” metal coordination complex lowers the pKa of the lysine nucleophile and stabilizes the transition state of the ATP α phosphate; and (ii) a second metal coordination complex bridges the β- and γ-phosphates. The NgrRnl N domain is a distinctively embellished oligonucleotide-binding (OB) fold that engages the γ-phosphate and associated metal complex and orients the pyrophosphate leaving group for in-line catalysis with stereochemical inversion at the AMP phosphate. The unique domain architecture of NgrRnl fortifies the theme that RNA ligases have evolved many times, and independently, by fusions of a shared nucleotidyltransferase domain to structurally diverse flanking modules. The mechanistic insights to lysine adenylylation gained from the NgrRnl structures are likely to apply broadly to the covalent nucleotidyltransferase superfamily of RNA ligases, DNA ligases, and RNA capping enzymes.

In situ creation of multi-metallic species inside porous silicate materials with tunable catalytic properties

2021 ◽  
Author(s):  
Yang-Yang Liu ◽  
Guo-Peng Zhan ◽  
Chuan-De Wu
Keyword(s):  
Catalytic Properties ◽  
Porous Metal ◽  
Coordination Complex ◽  
Metal Coordination ◽  
Metal Silicate ◽  
Porous Silicate ◽  
Metallic Species ◽  
Silicate Materials

Porous metal silicate (PMS) material PMS-11, consisting of uniformly distributed multi-metallic species inside the pores, is synthesized by using a discrete multi-metal coordination complex as the template, demonstrating high catalytic...

scholarly journals Converting histidine-induced 3D protein arrays in crystals into their 3D analogues in solution by metal coordination cross-linking

2020 ◽  
Vol 3 (1) ◽  
Author(s):  
Xiaoyi Tan ◽  
Hai Chen ◽  
Chunkai Gu ◽  
Jiachen Zang ◽  
Tuo Zhang ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Structural Information ◽  
Building Blocks ◽  
Metal Coordination ◽  
Protein Protein Interactions ◽  
Protonation State ◽  
Physiological Conditions ◽  
Simple Cubic ◽  
Stacking Pattern ◽  
Crystal Structural

Abstract Histidine (His) residues represent versatile motifs for designing protein-protein interactions because the protonation state of the imidazole group of His is the only moiety in protein to be significantly pH dependent under physiological conditions. Here we show that, by the designed His motifs nearby the C4 axes, ferritin nanocages arrange in crystals with a simple cubic stacking pattern. The X-ray crystal structures obtained at pH 4.0, 7.0, and 9.0 in conjunction with thermostability analyses reveal the strength of the π–π interactions between two adjacent protein nanocages can be fine-tuned by pH. By using the crystal structural information as a guide, we constructed 3D protein frameworks in solution by a combination of the relatively weak His–His interaction and Ni2+-participated metal coordination with Glu residues from two adjacent protein nanocages. These findings open up a new way of organizing protein building blocks into 3D protein crystalline frameworks.

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