ArticleJournal of the American Society for Mass Spectrometry2000
Effects of pH on the kinetic reaction mechanism of myoglobin unfolding studied by time-resolved electrospray ionization mass spectrometry.
Article in Journal of the American Society for Mass Spectrometry, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 99 citations in OpenAlex.
- Mathematical and Computational Models of Biochemical Reactions and Cell Signaling-From Ordinary Differential Equations to Machine Learning.International journal of molecular sciences · 2026Review
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- Understanding the Thermal Denaturation of Myoglobin with IMS-MS: Evidence for Multiple Stable Structures and Trapped Pre-equilibrium States.Journal of the American Society for Mass Spectrometry · 2021Article
- Site-Specific Siderocalin Binding to Ferric and Ferric-Free Enterobactin As Revealed by Mass Spectrometry.ACS chemical biology · 2020Article
- In-capillary microextraction for direct mass spectrometry analysis of biological samples.Talanta · 2018Article
- Microdroplet fusion mass spectrometry for fast reaction kinetics.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Influence of reactive species on the modification of biomolecules generated from the soft plasma.Scientific reports · 2015Article
- Thermally accelerated oxidative degradation of quercetin using continuous flow kinetic electrospray-ion trap-time of flight mass spectrometry.Journal of the American Society for Mass Spectrometry · 2013Article
- Basic vapor exposure for tuning the charge state distribution of proteins in negative electrospray ionization: elucidation of mechanisms by fluorescence spectroscopy.Journal of the American Society for Mass Spectrometry · 2012Article
- Vapor treatment of electrospray droplets: evidence for the folding of initially denatured proteins on the sub-millisecond time-scale.Journal of the American Society for Mass Spectrometry · 2012Article
- Negative electrospray droplet exposure to gaseous bases for the manipulation of protein charge state distributions.Analytical chemistry · 2011Article
- Electrospray droplet exposure to gaseous acids for the manipulation of protein charge state distributions.Analytical chemistry · 2010Article
- A hydrogen peroxide biosensor based on the direct electrochemistry of hemoglobin modified with quantum dots.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2007Article
- Direct correlation of the crystal structure of proteins with the maximum positive and negative charge states of gaseous protein ions produced by electrospray ionization.Journal of the American Society for Mass Spectrometry · 2005Article
- Denaturation of lysozyme and myoglobin in laser spray.Journal of the American Society for Mass Spectrometry · 2005Article
- Secondary structural characterization of oligonucleotide strands using electrospray ionization mass spectrometry.Nucleic acids research · 2005Article
- Diffusion measurements by electrospray mass spectrometry for studying solution-phase noncovalent interactions.Journal of the American Society for Mass Spectrometry · 2003Article
- The influence of electrostatic interactions on the detection of heme-globin complexes in ESI-MS.Journal of the American Society for Mass Spectrometry · 2001Article
- The methanol-induced conformational transitions of beta-lactoglobulin, cytochrome c, and ubiquitin at low pH: a study by electrospray ionization mass spectrometry.Journal of the American Society for Mass Spectrometry · 2001Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In most cases, kinetic unfolding reactions of proteins follow a simple one-step mechanism that does not involve any detectable intermediates. One example for a more complicated unfolding reaction is the acid-induced denaturation of holo-myoglobin (hMb). This reaction proceeds through a transient intermediate and can be described by a sequential two-step mechanism (Konermann et al. Biochemistry 1997, 36, 6448-6454). Time-resolved electrospray ionization mass spectrometry (ESI MS) is a new technique for monitoring the kinetics of protein folding and unfolding in solution. Different protein conformations can be distinguished by the different charge state distributions that they generate during ESI. At the same time this technique allows monitoring the loss or binding of noncovalent protein ligands. In this work, time-resolved ESI MS is used to study the dependence of the kinetic unfolding mechanism of hMb on the specific solvent conditions used in the experiment. It is shown that hMb unfolds through a short-lived intermediate only at acidic pH. Under basic conditions no intermediate is observed. These findings are confirmed by the results of optical stopped-flow absorption experiments. This appears to be the first time that a dependence of the kinetic mechanism for protein unfolding on external conditions such as pH has been observed.
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