Dataset Information

Zinc Binding to Fulvic acids: Assessing the Impact of pH, Metal Concentrations and Chemical Properties of Fulvic Acids on the Mechanism and Stability of Formed Soluble Complexes.

ABSTRACT: The aim of the study was defined as a complementary analysis of molecular interactions between zinc (Zn) and fulvic acids (FAs) at a broad pH range (3-7), different metal concentrations (0-50 mg dm-3) and chemical properties of FAs and their impact on the Zn binding mechanism, stability, and efficiency. The results showed that the complexation reaction prevailed at pH 6 and 7, whereas protons exchange dominated interactions at pH 3. Stability constant of the complexes increased along with pH (logK increased from ~3.8 to 4.2). Complexation was preferred by less-humidified structures of lower molecular mass containing more oxygen groups. The number of fluorophores available for Zn(II) increased from pH 3 to 7 by ~44%. Depending on the pH, complexation involved a bidentate chelate, monodentate and bidentate bridging mode. Zn(II) binding was insufficiently modeled by the classic Stern-Volmer equation and well described by the double logarithmic equation (R > 0.94) as well as by a modified Stern-Volmer formula assuming the existence of available and unavailable fluorophore populations (R > 0.98). The fluorescence ratio of different fluorophores was proposed as an indicator of the binding affinity of various structures. A positive relationship was found between the fraction of accessible fluorophores and Zn(II) binding at pH 7 determined based on proton release (R = 0.91-0.97). The obtained results can find application in controlling the mobility and bioavailability of Zn in different conditions.

SUBMITTER: Boguta P

PROVIDER: S-EPMC7144464 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature

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Publications

Zinc Binding to Fulvic acids: Assessing the Impact of pH, Metal Concentrations and Chemical Properties of Fulvic Acids on the Mechanism and Stability of Formed Soluble Complexes.

Boguta Patrycja P Sokołowska Zofia Z

Molecules (Basel, Switzerland) 20200312 6

The aim of the study was defined as a complementary analysis of molecular interactions between zinc (Zn) and fulvic acids (FAs) at a broad pH range (3-7), different metal concentrations (0-50 mg dm<sup>-3</sup>) and chemical properties of FAs and their impact on the Zn binding mechanism, stability, and efficiency. The results showed that the complexation reaction prevailed at pH 6 and 7, whereas protons exchange dominated interactions at pH 3. Stability constant of the complexes increased along ...[more]

PMID: 32178414

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Project description:Helicobacter pylori , a pathogen that colonizes the human stomach, requires the nickel-containing metalloenzymes urease and NiFe-hydrogenase to survive this low pH environment. The maturation of both enzymes depends on the metallochaperone, HypA. HypA contains two metal sites, an intrinsic zinc site and a low-affinity nickel binding site. X-ray absorption spectroscopy (XAS) shows that the structure of the intrinsic zinc site of HypA is dynamic and able to sense both nickel loading and pH changes. At pH 6.3, an internal pH that occurs during acid shock, the zinc site undergoes unprecedented ligand substitutions to convert from a Zn(Cys)(4) site to a Zn(His)(2)(Cys)(2) site. NMR spectroscopy shows that binding of Ni(II) to HypA results in paramagnetic broadening of resonances near the N-terminus. NOEs between the beta-CH(2) protons of Zn cysteinyl ligands are consistent with a strand-swapped HypA dimer. Addition of nickel causes resonances from the zinc binding motif and other regions to double, indicating more than one conformation can exist in solution. Although the structure of the high-spin, 5-6 coordinate Ni(II) site is relatively unaffected by pH, the nickel binding stoichiometry is decreased from one per monomer to one per dimer at pH = 6.3. Mutation of any cysteine residue in the zinc binding motif results in a zinc site structure similar to that found for holo-WT-HypA at low pH and is unperturbed by the addition of nickel. Mutation of the histidines that flank the CXXC motifs results in a zinc site structure that is similar to holo-WT-HypA at neutral pH (Zn(Cys)(4)) and is no longer responsive to nickel binding or pH changes. Using an in vitro urease activity assay, it is shown that the recombinant protein is sufficient for recovery of urease activity in cell lysate from a HypA deletion mutant, and that mutations in the zinc-binding motif result in a decrease in recovered urease activity. The results are interpreted in terms of a model wherein HypA controls the flow of nickel traffic in the cell in response to nickel availability and pH.

Dataset Information

Zinc Binding to Fulvic acids: Assessing the Impact of pH, Metal Concentrations and Chemical Properties of Fulvic Acids on the Mechanism and Stability of Formed Soluble Complexes.

Publications

Zinc Binding to Fulvic acids: Assessing the Impact of pH, Metal Concentrations and Chemical Properties of Fulvic Acids on the Mechanism and Stability of Formed Soluble Complexes.

Similar Datasets

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