29 research outputs found
The Pneumococcal Iron Uptake Protein a (PiuA) Specifically Recognizes Tetradentate FeIIIbis- and Mono-Catechol Complexes
Streptococcus pneumoniae (Spn) is an important Gram-positive human pathogen that causes millions of infections worldwide with an increasing occurrence of antibiotic resistance. Fe acquisition is a crucial virulence determinant in Spn; further, Spn relies on exogenous FeIII-siderophore scavenging to meet nutritional Fe needs. Recent studies suggest that the human catecholamine stress hormone, norepinephrine (NE), facilitates Fe acquisition in Spn under conditions of transferrin-mediated Fe starvation. Here we show that the solute binding lipoprotein PiuA from the piu Fe acquisition ABC transporter PiuBCDA, previously described as an Fe-hemin binding protein, binds tetradentate catechol FeIII complexes, including NE and the hydrolysis products of enterobactin. Two protein-derived ligands (H238, Y300) create a coordinately-saturated FeIII complex, which parallel recent studies in the Gram-negative intestinal pathogen Campylobacter jejuni. Our in vitro studies using NMR spectroscopy and 54Fe LC-ICP-MS confirm the FeIII can move from transferrin to apo-PiuA in a NE-dependent manner. Structural analysis of PiuA FeIII-bis-catechol and GaIII-bis-catechol and GaIII-(NE)2 complexes by NMR spectroscopy reveals only localized structural perturbations in PiuA upon ligand binding, largely consistent with recent descriptions of other solute binding proteins of type II ABC transporters. We speculate that tetradentate FeIII complexes formed by mono- and bis-catechol species are important Fe sources in Gram-positive human pathogens, since PiuA functions in the same way as SstD from Staphylococcus aureus
The Use Of Glassy Matrices To Identify Intermediates In The Nitric Oxide Dioxygenase Reaction Of Hemoglobins And Myoglobins
Rayleigh-Taylor Instability of a Plasma in Presence of a Variable Magnetic Field and Suspended Particles in Porous Medium
Imprisoned Lightning: Charge Transport in Trehalose-Derived Sugar Glasses
Trehalose is a naturally occurring disaccharide noted for its ability to preserve the biological function of proteins and cell membranes during periods of stress—such as water deprivation or extreme temperature—by stabilizing the conformations of the macromolecules within a glassy matrix. This phenomenon makes use of the propensity for trehalose to interact strongly with protein functional groups and solvent water molecules via hydrogen bonding. Previously, it has been shown that trehalose sugar glasses also support long-range charge transport in oxidation-reduction reactions occurring between spatially separated donors and acceptors. Here, through the use of bulk Arrhenius DC-conductivity measurements, we infer that this anomalously high carrier mobility is due to proton hopping along a hydrogen bonding network formed by sorbed “water wires,” a process known as the Grotthuss mechanism. Additionally, we find that the apparent activation energy of the conductivity depends non-monotonically on the bias voltage. The possibility is raised for novel photovoltaic devices based on the entrapment of photosynthetic proteins within these glasses
Trehalose-Based Glassy Matrices as an Effective Tool to Trap Short-Lived Intermediates in the Nitric Oxide Dioxygenation (NOD) Reaction of Hemoglobin
Abstract: T33.00008 : Charge Transport in Trehalose-Derived Sugar Glasses
Trehalose is a naturally occurring disaccharide with a well-known ability to preserve the biological function of proteins and cell membranes during periods of stress, including dehydration, by stabilizing the conformations of the macromolecules within a glassy matrix. This phenomenon makes use of the propensity of trehalose to interact strongly with protein functional groups and solvating water molecules via hydrogen bonding. Recently, it has been shown that trehalose sugar glasses also support long range charge transport in the form of oxidation-reduction reactions occurring between spatially separated donors and acceptors. Based on an Arrhenius conductivity analysis, along with IR-absorption and dielectric spectroscopy data, we propose that a Grotthuss-like proton hopping mechanism is responsible for the high charge carrier mobility and observed bias-dependent apparent activation energy. The possibility is raised for novel redox reactions to be performed on proteins constrained to specific 3D conformations. This could lead to a deeper understanding of biological processes, such as anhydrobiosis, as well as the development of new biomimetic photovoltaic devices