Carrier-Based Ion-Selective Electrodes and Bulk Optodes. 1. General Characteristics.

Biochar is a pyrogenous, organic material synthesized through pyrolysis of different biomass (plant or animal waste). The potential biochar applications include: (1) pollution remediation due to high CEC and specific surface area; (2) soil fertility improvement on the way of liming effect, enrichment in volatile matter and increase of pore volume, (3) carbon sequestration due to carbon and ash content, etc. Biochar properties are affected by several technological parameters, mainly pyrolysis temperature and feedstock kind, which differentiation can lead to products with a wide range of values of pH, specific surface area, pore volume, CEC, volatile matter, ash and carbon content. High pyrolysis temperature promotes the production of biochar with a strongly developed specific surface area, high porosity, pH as well as content of ash and carbon, but with low values of CEC and content of volatile matter. This is most likely due to significant degree of organic matter decomposition. Biochars produced from animal litter and solid waste feedstocks exhibit lower surface areas, carbon content, volatile matter and high CEC compared to biochars produced from crop residue and wood biomass, even at higher pyrolysis temperatures. The reason for this difference is considerable variation in lignin and cellulose content as well as in moisture content of biomass. The physicochemical properties of biochar determine application of this biomaterial as an additive to improve soil quality. This review succinctly presents the impact of pyrolysis temperature and the type of biomass on the physicochemical characteristics of biochar and its impact on soil fertility.

https://link.springer.com/content/pdf/10.1007/s11157-020-09523-3.pdf

Biochar physicochemical properties: pyrolysis temperature and feedstock kind effects

Changes in surface chemistry of activated carbons by wet oxidation

Understanding the thermal reduction of graphene oxide (GO) is important for graphene exfoliation, and chemical and morphological modifications. In this process, the role of trapped water and the evolution of oxygen during annealing are still not well-understood. To unravel the complex mechanisms leading to the removal of oxygen in reduced GO, we have performed in situ transmission infrared absorption spectroscopy measurements of GO films upon thermal annealing at 60–850 °C in vacuum (10–3–10–4 Torr). Using cluster-based first-principles calculations, epoxides, ethers (pyrans and furans), hydroxyls, carboxyls, lactols, and various types of ketones and their possible derivatives have been identified from the spectroscopic data. Furthermore, the interactions between randomly arranged nearby oxygen species are found to affect the spectral response (red and blue shifts) and the overall chemistry during annealing. For instance, the initial composition of oxygen species (relative amounts and types of species, su...

The Role of Oxygen during Thermal Reduction of Graphene Oxide Studied by Infrared Absorption Spectroscopy

Characterization of a major refractory component of marine dissolved organic matter

Summary Tables.- Combination Tables.- C NMR Spectroscopy.- H NMR Spectroscopy.- Heteronuclear NMR Spectroscopy.- IR Spectroscopy.- Mass Spectrometry.- UV/Vis Spectroscopy.

Structure Determination of Organic Compounds

We describe an approach for the determination of binding constants for protein-ligand complexes with electrospray ionization mass spectrometry, based on the observation of unbound ligands competing for binding to a protein target. For the first time, dissociation constants lower than picomolar could be determined with good accuracy by electrospray ionization mass spectrometry. The presented methodology relies only on the determination of signal intensity ratios for free ligands in the low mass region. Therefore, all the advantages of measuring low masses with mass spectrometry, such as high resolution are preserved. By using a reference ligand with known binding affinity, the affinity of a second ligand can be determined. Since no noncovalently bound species are observed, assumptions about response factors are not necessary. The method is validated with ligands binding to avidin and applied to ligands binding to p38 mitogen-activated protein kinase.

Binding constant determination of high-affinity protein-ligand complexes by electrospray ionization mass spectrometry and ligand competition.

Electronegative substituents cause a decrease in |J|gem while a double or triple bond next to the CH2 group causes an increase.

1H NMR Spectroscopy

We present a comprehensive study for determining the binding affinity of a protein-ligand complex, using mass spectrometric methods. Mass spectrometry has been used to study noncovalent interactions for a number of years. However, the use of soft ionization mass spectrometry for quantitative analysis of noncovalently bound complexes is not widely accepted. This paper reports a comparison of MS methods against established methods such as surface plasmon resonance (SPR) and circular dichroism (CD) whose suitability for the quantitative assessment of noncovalent interactions is well known. ESI titration and MALDI-SUPREX were used as representative mass spectrometric methods for this work. We chose to study the calmodulin-melittin complex that presents three challenges: (i) it exhibits a high affinity (low nanomolar KD); (ii) complexes are formed only in the presence of a coactivator, calcium ions in this case; and (iii) the protein and the complex show a different ionization efficiency. Dissociation constants were obtained from each method for the selected system and compared thoroughly to elucidate pros and cons of the selected methodologies in terms of their ability for the determination of binding constants of protein-ligand complexes. ESI titration, SPR, CD and MALDI-SUPREX yielded KD values in the low nanomolar range that are in general agreement with an older value reported in the literature. We also critically evaluated the limitations in particular of the MS methods and the associated data evaluation procedures. We present an improved evaluation of SUPREX data, as well as a detailed error analysis for all methods used.

Critical evaluation of mass spectrometric measurement of dissociation constants: accuracy and cross-validation against surface plasmon resonance and circular dichroism for the calmodulin–melittin system

This study highlights the benefits of nano electrospray ionization mass spectrometry (nanoESI-MS) as a fast and label-free method not only for determination of dissociation constants (KD) of a cooperatively regulated enzyme but also to better understand the mechanism of enzymatic cooperativity of multimeric proteins. We present an approach to investigate the allosteric mechanism in the binding of inhibitors to the homotetrameric enzyme fructose 1,6-bisphosphatase (FBPase), a potential therapeutic target for glucose control in type 2 diabetes. A series of inhibitors binding at an allosteric site of FBPase were investigated to determine their KDs by nanoESI-MS. The KDs determined by ESI-MS correlate very well with IC50 values in solution. The Hill coefficients derived from nanoESI-MS suggest positive cooperativity. From single-point measurements we could obtain information on relative potency, stoichiometry, conformational changes, and mechanism of cooperativity. A new X-ray crystal structure of FBPase tetr...

Martin Badertscher

Papers

Structure Determination of Organic Compounds

Binding constant determination of high-affinity protein-ligand complexes by electrospray ionization mass spectrometry and ligand competition.

1H NMR Spectroscopy

Critical evaluation of mass spectrometric measurement of dissociation constants: accuracy and cross-validation against surface plasmon resonance and circular dichroism for the calmodulin–melittin system

Determination of protein-ligand binding constants of a cooperatively regulated tetrameric enzyme using electrospray mass spectrometry.