Proton Transfer Ionization

Proton transfer ionization is a chemical process in which an acid-base reaction creates charged molecules by moving a proton between a reagent and an analyte, enabling their detection and analysis. In mass spectrometry, reagent ions with high proton affinity transfer a proton to suitable analyte molecules, producing ions such as [M+H]+; the reaction’s efficiency depends on proton affinity, gas-phase chemistry, and experimental conditions. This soft ionization approach often preserves molecular ions while limiting fragmentation, supporting molecular-weight determination and structural characterization. It is especially useful for analyzing volatile and semi-volatile compounds, monitoring trace chemicals, and coupling chemical separation with sensitive mass-based detection.

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Education

JoVE Core - Chemistry

Ionization Energy

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2020

The amount of energy required to remove the most loosely bound electron from a gaseous atom in its ground state is called its first ionization energy (IE1). The first ionization energy for an element, X, is the energy required to form a cation with 1+ charge: The energy required to remove the second most loosely bound electron is called the second ionization energy (IE2). The energy required to remove the third electron is the third ionization energy, and so on. Energy is always required...

Proton Exchange Membrane Fuel Cells

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2023

Source: Laboratories of Margaret Workman and Kimberly Frye - Depaul University The United States consumes a large amount of energy – the current rate is around 97.5 quadrillion BTUs annually. The vast majority (90%) of this energy comes from non-renewable fuel sources. This energy is used for electricity (39%), transportation (28%), industry (22%), and residential/commercial use (11%). As the world has a limited supply of these non-renewable sources, the United States (among others) is...

Research

JoVE Journal - Engineering
Free Sample

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy

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Cited by 21 •

2014

Key steps of protein function, in particular backbone conformational changes and proton transfer reactions, often take place in the microsecond to millisecond time scale. These dynamical processes can be studied by time-resolved step-scan Fourier-transform infrared spectroscopy, in particular for proteins whose function is triggered by light.

Isotopic Effect in Double Proton Transfer Process of Porphycene Investigated by Enhanced QM/MM Method

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2019

A protocol that uses enhanced QM/MM method to investigate the isotopic effect on the double proton transfer process in porphycene is presented here.

A Study of the Complexation of Mercury(II) with Dicysteinyl Tetrapeptides by Electrospray Ionization Mass Spectrometry

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2016

The characterization of complexes formed in different relative ratios of mercury(II) to dicysteinyl tetrapeptides by electrospray ionization orbitrap mass spectrometry is presented.

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