AI Article Synopsis
- The study investigated the basicity of highly protonated cytochrome c and myoglobin ions using mass spectrometry and various reactions, focusing on different charge states.
- Surprisingly, highly charged protein ions (HCPIs) can protonate non-polar molecules and inert gases like argon, oxygen, and nitrogen during reactions.
- The research predicts that protonated cyt c and myoglobin ions lose protons to vacuum at specific charge states, and findings suggest that protein ions with higher charge states can be generated in low-pressure conditions to minimize unwanted reactions with atmospheric gases.
Article Abstract
The basicity of highly protonated cytochrome c (cyt c) and myoglobin (myo) ions were investigated using tandem mass spectrometry, ion-molecule reactions (IMRs), and theoretical calculations as a function of charge state. Surprisingly, highly charged protein ions (HCPI) can readily protonate non-polar molecules and inert gases, including Ar, O , and N in thermal IMRs. The most HCPIs that can be observed are over 130 kJ mol less basic than the least basic neutral organic molecules known (tetrafluoromethane and methane). Based on theoretical calculations, it is predicted that protonated cyt c and myo ions should spontaneously lose a proton to vacuum for charge states in which every third residue is protonated. In this study, HCPIs are formed where every fourth residue on average is protonated. These results indicate that protein ions in higher charge states can be formed using a low-pressure ion source to reduce proton-transfer reactions between protein ions and gases from the atmosphere.
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| http://dx.doi.org/10.1002/anie.201702781 | DOI Listing |
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