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Related Concept Videos

Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Adsorption of Gases on Solids01:28

Adsorption of Gases on Solids

Adsorption is a process where molecules, known as the adsorbates, accumulate on a surface, which is referred to as the adsorbent or substrate. Occurring at the solid-gas interface, this phenomenon is crucial in various scientific and industrial contexts. The reverse of adsorption is desorption.Two types of adsorptions exist: physical (physisorption) and chemical (chemisorption). Physisorption involves gas molecules held to the solid's surface by relatively weak intermolecular van der Waals...
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
ATP Driven Pumps I: An Overview01:27

ATP Driven Pumps I: An Overview

ATP-driven pumps, also known as transport ATPases, are integral membrane proteins. They have binding sites for ATP located on the membrane's cytosolic side and the ion-conducting domain in the transmembrane region. These pumps use the free energy released from ATP hydrolysis to move the solutes across cell membranes against an electrochemical gradient.
There are four main types of ATP-driven pumps - P-type, V-type, F-type, and ABC transporter. All these pumps are of varying complexities and are...
ATP Energy Storage and Release01:31

ATP Energy Storage and Release

ATP is a highly unstable molecule. Unless quickly used to perform work, ATP spontaneously dissociates into ADP and inorganic phosphate (Pi), and the free energy released during this process is lost as heat. The energy released by ATP hydrolysis is used to perform work inside the cell and depends on a strategy called energy coupling. Cells couple the exergonic reaction of ATP hydrolysis with endergonic reactions, allowing them to proceed.
One example of energy coupling using ATP involves a...

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Optimized Procedure for Determining the Adsorption of Phosphonates onto Granular Ferric Hydroxide using a Miniaturized Phosphorus Determination Method
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Proton interaction in phosphate adsorption onto goethite.

Bin Zhong1, Robert Stanforth, Shunnian Wu

  • 1Division of Environmental Science & Engineering, National University of Singapore, 9 Engineering Drive 1, Singapore 117576.

Journal of Colloid and Interface Science
|January 27, 2007
PubMed
Summary

Phosphate adsorption on goethite involves complex surface interactions. This study reveals that phosphate binding transitions from monodentate to bidentate complexation as coverage increases, impacting hydroxyl release.

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Optimized Procedure for Determining the Adsorption of Phosphonates onto Granular Ferric Hydroxide using a Miniaturized Phosphorus Determination Method
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Published on: July 14, 2015

Area of Science:

  • Environmental Science
  • Geochemistry
  • Surface Chemistry

Background:

  • Phosphate adsorption on iron oxides like goethite is crucial for nutrient cycling and contaminant sequestration.
  • Current models often simplify phosphate binding as a basic ligand exchange with surface hydroxyl groups.

Purpose of the Study:

  • To investigate the detailed binding mechanisms of phosphate on goethite.
  • To evaluate the role of proton interactions and surface charge changes during phosphate adsorption.
  • To understand how binding forms evolve with increasing phosphate coverage.

Main Methods:

  • Analysis of proton interaction during adsorption.
  • Monitoring of surface charge variations.
  • Evaluation of hydroxyl release stoichiometry at different phosphate loadings.

Main Results:

  • Hydroxyl release stoichiometry increases with phosphate coverage, indicating evolving adsorption mechanisms.
  • Phosphate surface binding shifts from monodentate to bidentate complexation as surface coverage increases.
  • The observed net hydroxyl release is consistent with a 2pK(a) multisite binding model.

Conclusions:

  • Phosphate adsorption on goethite is a dynamic process, not a single ligand exchange mechanism.
  • The transition from monodentate to bidentate binding is a key factor influencing surface charge and proton exchange.
  • A 2pK(a) multisite model provides a more accurate interpretation of phosphate-goethite interactions across varying coverages.