Browse
Submit Data
Databases
API
Help

Dataset Information

16 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Stimulation of Redox-Induced Electron Transfer by Interligand Hydrogen Bonding in a Cobalt Complex with Redox-Active Guanidine Ligand.

ABSTRACT: Octahedrally coordinated cobalt(II) complexes with a redox-active bisguanidine ligand and acac co-ligands were synthesized and their redox chemistry analysed in detail. The N-H functions in a bisguanidine ligand with partially alkylated guanidino groups form N-H⋅⋅⋅O hydrogen bonds with the acac co-ligands, thereby massively influencing the redox chemistry. For all complexes, the first one-electron oxidation is metal-centred, leading to Co^III complexes with neutral bisguanidine ligand units. Further one-electron oxidation is ligand-centred in the case of Co-bisguanidine complexes with fully alkylated guanidino groups, giving Co^III complexes with radical monocationic bisguanidine ligands. On the other hand, the hydrogen-bond strengthening upon oxidation of the Co-bisguanidine complex with partially alkylated guanidino groups initiates metal reduction (Co^III →Co^II ) and two-electron oxidation of the guanidine ligand, providing the first example for the stimulation of redox-induced electron transfer by interligand hydrogen bonding.

SUBMITTER: Lohmeyer L

PROVIDER: S-EPMC8252010 | biostudies-literature |

REPOSITORIES: biostudies-literature

ACCESS DATA

Json Xml

Similar Datasets

Cobalt-Catalyzed Hydrogen-Atom Transfer Induces Bicyclizations that Tolerate Electron-Rich and Electron-Deficient Intermediate Alkenes.

Project description:A novel CoII -catalyzed polyene cyclization was developed that is uniquely effective when performed in hexafluoroisopropanol as the solvent. The process is presumably initiated by metal-catalyzed hydrogen-atom transfer (MHAT) to 1,1-disubstituted or monosubstituted alkenes, and the reaction is remarkable for its tolerance of internal alkenes bearing either electron-rich methyl or electron-deficient nitrile substituents. Electron-rich aromatic terminators are required in both cases. Terpenoid scaffolds with different substitution patterns are obtained with excellent diastereoselectivities, and the bioactive C20-oxidized abietane diterpenoid carnosaldehyde was made to showcase the utility of the nitrile-bearing products. Also provided are the results of several mechanistic experiments that suggest the process features an MHAT-induced radical bicyclization with late-stage oxidation to regenerate the aromatic terminator.

| S-EPMC7124983 | biostudies-literature

Modulating the cobalt redox potential through imidazole hydrogen bonding interactions in a supramolecular biomimetic protein-cofactor model.

Project description:A realistic model for the active site of histidine-on cobalamin@protein complexes is reported and studied under homogeneous and immobilized conditions. Analysis of lower ligand modulation and its influence on the properties of the biomimetic compound are presented. The cofactor attachment by a protein's histidine residue was imitated by covalently linking an artificial imidazole-containing linker to cobyric acid. The resulting intramolecular coordination complex is an excellent structural model of its natural archetype, according to 2D 1H-NMR studies and molecular modeling. The effect of deprotonation of the axially coordinating imidazole ligand - as proposed for natural cofactor complexes - tunes significantly the position of the cathodic peak (?V = -203 mV) and stabilizes thereby the CoIII form. Partial deprotonation of the imidazole moiety through hydrogen bonding interactions was then achieved by immobilizing the biomimetic model on hydrophobic C18 silica, which yielded an unprecedented insight on how this class of Cbl-dependent proteins may fine-tune their properties in biological systems.

| S-EPMC6013808 | biostudies-literature

Hydrogen bonding penalty upon ligand binding.

Project description:Ligand binding involves breakage of hydrogen bonds with water molecules and formation of new hydrogen bonds between protein and ligand. In this work, the change of hydrogen bonding energy in the binding process, namely hydrogen bonding penalty, is evaluated with a new method. The hydrogen bonding penalty can not only be used to filter unrealistic poses in docking, but also improve the accuracy of binding energy calculation. A new model integrated with hydrogen bonding penalty for free energy calculation gives a root mean square error of 0.7 kcal/mol on 74 inhibitors in the training set and of 1.1 kcal/mol on 64 inhibitors in the test set. Moreover, an application of hydrogen bonding penalty into a high throughput docking campaign for EphB4 inhibitors is presented, and remarkably, three novel scaffolds are discovered out of seven tested. The binding affinity and ligand efficiency of the most potent compound is about 300 nM and 0.35 kcal/mol per non-hydrogen atom, respectively.

| S-EPMC3117785 | biostudies-literature

Light-induced hydrogen bonding pattern and driving force of electron transfer in AppA BLUF domain photoreceptor.

Project description:The AppA BLUF (blue light sensing using FAD) domain from Rhodobacter sphaeroides serves as a blue light-sensing photoreceptor. The charge separation process between Tyr-21 and flavin plays an important role in the light signaling state by transforming the dark state conformation to the light state one. By solving the linearized Poisson-Boltzmann equation, I calculated E(m) for Tyr-21, flavin, and redox-active Trp-104 and revealed the electron transfer (ET) driving energy. Rotation of the Gln-63 side chain that converts protein conformation from the dark state to the light state is responsible for the decrease of 150 mV in E(m) for Tyr-21, leading to the significantly larger ET driving energy in the light state conformation. The pK(a) values of protonation for flavin anions are essentially the same in both dark and light state crystal structures. In contrast to the ET via Tyr-21, formation of the W state results in generation of only the dark state conformation (even if the initial conformation is in the light state); this could explain why Trp-104-mediated ET deactivates the light-sensing yield and why the activity of W104A mutant is similar to that of the light-adapted native BLUF.

| S-EPMC2662152 | biostudies-literature

Hydrogen bonding networks tune proton-coupled redox steps during the enzymatic six-electron conversion of nitrite to ammonia.

Project description:Multielectron multiproton reactions play an important role in both biological systems and chemical reactions involved in energy storage and manipulation. A key strategy employed by nature in achieving such complex chemistry is the use of proton-coupled redox steps. Cytochrome c nitrite reductase (ccNiR) catalyzes the six-electron seven-proton reduction of nitrite to ammonia. While a catalytic mechanism for ccNiR has been proposed on the basis of studies combining computation and crystallography, there have been few studies directly addressing the nature of the proton-coupled events that are predicted to occur along the nitrite reduction pathway. Here we use protein film voltammetry to directly interrogate the proton-coupled steps that occur during nitrite reduction by ccNiR. We find that conversion of nitrite to ammonia by ccNiR adsorbed to graphite electrodes is defined by two distinct phases; one is proton-coupled, and the other is not. Mutation of key active site residues (H257, R103, and Y206) modulates these phases and specifically alters the properties of the detected proton-dependent step but does not inhibit the ability of ccNiR to conduct the full reduction of nitrite to ammonia. We conclude that the active site residues examined are responsible for tuning the protonation steps that occur during catalysis, likely through an extensive hydrogen bonding network, but are not necessarily required for the reaction to proceed. These results provide important insight into how enzymes can specifically tune proton- and electron transfer steps to achieve high turnover numbers in a physiological pH range.

| S-EPMC4159211 | biostudies-literature

Virus and chlorine adsorption onto guanidine modified cellulose nanofibers using covalent and hydrogen bonding.

Project description:Unsafe drinking water leads to millions of human deaths each year, while contaminated wastewater discharges are a significant threat to aquatic life. To relieve the burden of unsafe water, we are in search of an inexpensive material that can adsorb pathogenic viruses from drinking water and adsorb toxic residual chlorine from wastewater. To impart virus and chlorine removal abilities to cellulosic materials, we modified the primary hydroxyl group with a positively charged guanidine group, to yield guanidine modified cellulose derivatives. Microcrystalline cellulose (MC) bearing covalently bonded guanidine hydrochloride (MC-GC) and hydrogen-bonded guanidine hydrochloride (MC-GH) were synthesized, and electrospun into nanofibers after blending with the non-ionogenic polyvinyl alcohol (PVA), to produce large pore sized, high surface area membranes. The MC-GC/PVA and MC-GH/PVA nanofibers were stabilized against water dissolution by crosslinking with glutaraldehyde vapor. The water-stable MC-GC/PVA mats were able to remove more than 4 logs of non-enveloped porcine parvovirus (PPV) and enveloped Sindbis virus and reached 58% of chlorine removal. The MC-GC/PVA nanofibers demonstrated better performance for pathogen removal and dechlorination than MC-GH/PVA nanofibers. This first study of MC-GC/PVA electrospun mats for virus removal shows they are highly effective and merit additional research for virus removal.

| S-EPMC7500341 | biostudies-literature

Intramolecular Hydrogen Bonding Restricts Gd-Aqua-Ligand Dynamics.

Project description:Aqua ligands can undergo rapid internal rotation about the M-O bond. For magnetic resonance contrast agents, this rotation results in diminished relaxivity. Herein, we show that an intramolecular hydrogen bond to the aqua ligand can reduce this internal rotation and increase relaxivity. Molecular modeling was used to design a series of four Gd complexes capable of forming an intramolecular H-bond to the coordinated water ligand, and these complexes had anomalously high relaxivities compared to similar complexes lacking a H-bond acceptor. Molecular dynamics simulations supported the formation of a stable intramolecular H-bond, while alternative hypotheses that could explain the higher relaxivity were systematically ruled out. Intramolecular H-bonding represents a useful strategy to limit internal water rotational motion and increase relaxivity of Gd complexes.

| S-EPMC5558827 | biostudies-literature

Copper(I) Complex Mediated Nitric Oxide Reductive Coupling: Ligand Hydrogen Bonding Derived Proton Transfer Promotes N2O(g) Release.

Project description:A cuprous chelate bearing a secondary sphere hydrogen bonding functionality, [(PV-tmpa)CuI]+, transforms •NO(g) to N2O(g) in high-yields in methanol. Ligand derived proton transfer facilitates N-O bond cleavage of a putative hyponitrite intermediate releasing N2O(g), underscoring the crucial balance between H-bonding capabilities and acidities in (bio)chemical •NO(g) coupling systems.

| S-EPMC6896986 | biostudies-literature

Controlled Interconversion of a Dinuclear Au Species Supported by a Redox-Active Bridging PNP Ligand Facilitates Ligand-to-Gold Electron Transfer.

Project description:Redox non-innocent ligands have recently emerged as interesting tools to obtain new reactivity with a wide variety of metals. However, gold has almost been neglected in this respect. Here, we report mechanistic investigations related to a rare example of ligand-based redox chemistry in the coordination sphere of gold. The dinuclear metal-centered mixed-valent AuI -AuIII complex 1, supported by monoanionic diarylamido-diphosphine ligand PNPPr and with three chlorido ligands overall, undergoes a complex series of reactions upon halide abstraction by silver salt or Lewis acids such as gallium trichloride. Formation of the ultimate AuI -AuI complex 2 requires the intermediacy of AuI -AuI dimers 5 and 7 as well as the unique AuIII -AuIII complex 6, both of which are interconverted in a feedback loop. Finally, unprecedented ortho-selective C-H activation of the redox-active PNP ligand results in the carbazolyldiphosphine derivative PN*PPr via ligand-to-metal two-electron transfer. This work demonstrates that the redox-chemistry of gold may be significantly expanded and modified when using a reactive ligand scaffold.

| S-EPMC5413818 | biostudies-literature

Intramolecular hydrogen-bonding in a cobalt aqua complex and electrochemical water oxidation activity.

Project description:Water oxidation is catalysed in Nature by a redox cofactor embedded in a hydrogen-bonded network designed to orchestrate proton transfer throughout the challenging 4 electron reaction. In order to mimic aspects of this microenvironment, [CoLDMA(CH3CN)2][BF4]2 (2) was synthesized, where LDMA is a dipyridyldiamine ligand with two dimethylamine bases in the secondary coordination sphere. Structural characterization of the corresponding aqua complexes establish hydrogen bonding between the bound water and pendant base(s). Cyclic voltammetry of [CoLDMA(CH3CN)2][BF4]2 (2) reveals enhanced oxidative current upon titration with water and controlled potential electrolysis confirms evolution of O2. The related complex [CoLH(CH3CN)2][BF4]2 (1), which has the same primary coordination environment as 2 but lacks pendant bases, is inactive. The structural and electrochemical studies illustrate the role positioned proton relays can play in promoting redox reactivity.

| S-EPMC5912104 | biostudies-literature

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data