A5023182593- Iron Metabolism and Disorders
- Trace Elements in Health
- Hemoglobinopathies and Related Disorders
- Porphyrin Metabolism and Disorders
- Plant Micronutrient Interactions and Effects
- RNA regulation and disease
- Folate and B Vitamins Research
- Lysosomal Storage Disorders Research
- Drug Transport and Resistance Mechanisms
- Retinoids in leukemia and cellular processes
- Mass Spectrometry Techniques and Applications
- Calcium signaling and nucleotide metabolism
- Antioxidant Activity and Oxidative Stress
- Sphingolipid Metabolism and Signaling
- Metal complexes synthesis and properties
- Oral microbiology and periodontitis research
- Phytochemicals and Antioxidant Activities
- Neurological diseases and metabolism
- Microfluidic and Capillary Electrophoresis Applications
- Endoplasmic Reticulum Stress and Disease
- Bacterial Genetics and Biotechnology
- thermodynamics and calorimetric analyses
- Bacteriophages and microbial interactions
- Metal-Catalyzed Oxygenation Mechanisms
- Ion channel regulation and function
State University of New York
2008-2025
State University of New York at Potsdam
2015-2024
Division of Chemistry
2015
University of New Hampshire
2001-2008
University of New Hampshire at Manchester
2002-2008
University of Brescia
2002-2008
Universidad de Zaragoza
2005
University of Reading
2005
Délégation Paris 7
1999-2000
Centre National de la Recherche Scientifique
1999-2000
The health benefits of cranberries have long been recognized. However, the mechanisms behind its function are poorly understood. We investigated iron-binding properties quercetin, major phenolic phytochemical present in cranberries, and other selected compounds (chrysin, 3-hydroxyflavone, 3',4'-dihydroxy flavone, rutin, flavone) aqueous media using UV/vis, NMR EPR spectroscopies ESI-Mass spectrometry. Strong confirmed for containing "iron-binding motifs" identified their structures. apparent...
Abstract The interaction between nuclear receptor coactivator 4 (NCOA4) and the iron storage protein ferritin is a crucial component of cellular homeostasis. binding NCOA4 to FTH1 subunits initiates ferritinophagy—a ferritin-specific autophagic pathway leading release stored inside ferritin. dysregulation associated with several diseases, including neurodegenerative disorders cancer, highlighting NCOA4-ferritin interface as prime target for drug development. Here, we present cryo-EM...
Human ferritins sequester and store iron as a stable FeOOH(s) mineral core within protein shell assembled from 24 subunits of two types, H L. Core mineralization in recombinant H- L-subunit homopolymer heteropolymer several site-directed H-subunit variants was investigated to determine the oxidation/hydrolysis chemistry function flux into protein. Stopped-flow absorption spectrometry, UV electrode oximetry revealed that forms by at least three pathways, not previously thought. They...
Ferritin is a widespread iron mineralizing and detoxification protein that stores as hydrous ferric oxide mineral core within shell-like structure of 4/3/2 octahedral symmetry. Iron mineralization initiated at dinuclear ferroxidase centers inside the where Fe2+ O2 meet react to form μ-1,2-peroxodiferric intermediate subsequently decays μ-oxo dimeric oligomeric iron(III) species ultimately core. Several types channels penetrate shell are possible pathways for diffusion dioxygen centers. In...
Mushrooms are a potent source of dietary antioxidants and often marketed for their capability decreasing oxidative stress preventing diseases. To date, however, little research has been done on the antioxidant activity commercially available mushroom extractions, or stability over time. Herein, capacity six tinctures (hydro-alcoholic extracts chaga, maitake, shiitake, reishi, lion's mane, turkey tail) were evaluated using panel five assays: Oxygen Radical Absorbance Capacity (ORAC),...
Abstract Despite ferritin's critical role in regulating cellular and systemic iron levels, our understanding of the structure assembly mechanism isoferritins, discovered over eight decades ago, remains limited. Unveiling how composition molecular architecture hetero‐oligomeric ferritins confer distinct functionality to isoferritins is essential structural intricacies H L subunits influence their interactions with machinery. In this study, ferritin heteropolymers specific subunit ratios were...
In animals, the iron storage and detoxification protein, ferritin, is composed of two functionally genetically distinct subunit types, H (heavy) L (light), which co-assemble in various ratios with tissue specific distributions to form shell-like protein structures 24 subunits within a mineralized core stored. The H-subunit possesses ferroxidase center (FC) that catalyzes Fe(II) oxidation, whereas L-subunit does not. To assess role oxidation formation, human recombinant heteropolymeric...
Ferritin degradation pathways, particularly NCOA4-mediated ferritinophagy, are crucial for maintaining iron homeostasis. Here, we demonstrate the coexistence of two NCOA4 isoforms, one iron-sulfur cluster-free and cluster-bound, in oxygenated cell cultures. Using a combination spectroscopic analytical techniques, vitro characterization fragment (383-522), denoted NCOA4-D, revealed predominance monomeric species with relatively stable [2Fe-2S] cluster under normoxic conditions. The results...
From microorganisms to humans, ferritin plays a central role in the biological management of iron. The ferritins function as iron storage and detoxification proteins by oxidatively depositing hydrous ferric hydroxide mineral core within their shell-like structures. mechanism which is formed has been subject intense investigation for many years. A diiron ferroxidase site located on H-chain subunit vertebrate catalyzes oxidation Fe(II) Fe(III) molecular oxygen. previous stopped-flow kinetics...
Biomineralization of the ferritin iron core involves a complex series events in which H2O2 is produced during oxidation by O2 at dinuclear centre, ‘ferroxidase site’, located on H-subunit mammalian proteins. Rapid-freeze quench Mössbauer spectroscopy was used to probe early and mineralization recombinant human containing 24 H-subunits. The spectra reveal that μ-1,2-peroxodiFe(III) intermediate (species P) with parameters δ (isomer shift) = 0.58mm/s ΔEQ (quadrupole splitting) 1.07mm/s 4.2K...
Bacterioferritin (EcBFR) of Escherichia coli is an iron-mineralizing hemoprotein composed 24 identical subunits, each containing a dinuclear metal-binding site known as the "ferroxidase center." The chemistry Fe(II) binding and oxidation Fe(III) hydrolysis using H(2)O(2) oxidant was studied by electrode oximetry, pH-stat, UV-visible spectrophotometry, electron paramagnetic resonance spin trapping experiments. Absorption spectroscopy data demonstrate two per at ferroxidase center, thus...
Iron deposition within the iron storage protein ferritin involves a complex series of events consisting Fe2+ binding, transport, and oxidation at ferroxidase sites mineralization hydrous ferric oxide core, form iron. In present study, we have examined thermodynamic properties binding to recombinant human H-chain apoferritin (HuHF) by isothermal titration calorimetry (ITC) in order determine location primary ferrous ion on principal pathways which travels dinuclear center prior its Fe3+....
In host-pathogen interactions, the struggle for iron may have major consequences on outcome of disease. To overcome low solubility and bio-availability iron, bacteria evolved multiple systems to acquire from various sources such as heme, hemoglobin ferritin. The molecular basis acquisition heme been extensively studied; however, very little is known about host ferritin, a 24-mer nanocage protein able store thousands atoms within its cavity. human opportunistic pathogen Bacillus cereus,...
At least three ferritins are found in the bacterium Escherichia coli: heme-containing bacterioferritin (EcBFR) and two nonheme bacterial (EcFtnA EcFtnB). In addition to conserved A B sites of diiron ferroxidase center, EcFtnA has a third iron-binding site (the C site) unknown function that is nearby site. present work, complex chemistry iron oxidation deposition was further defined through combination oximetry, pH stat, stopped-flow conventional kinetics, UV–vis, fluorescence, EPR...