ArticleJournal of the American Society for Mass Spectrometry2011
Heme binding in gas-phase holo-myoglobin cations: distal becomes proximal?
Article in Journal of the American Society for Mass Spectrometry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Mass Spectrometric Analysis of Antibody-Epitope Peptide Complex Dissociation: Theoretical Concept and Practical Procedure of Binding Strength Characterization.Molecules (Basel, Switzerland) · 2020Article
- Multistage Ultraviolet Photodissociation Mass Spectrometry To Characterize Single Amino Acid Variants of Human Mitochondrial BCAT2.Analytical chemistry · 2018Article
- Enhancing Sensitivity of Liquid Chromatography-Mass Spectrometry of Peptides and Proteins Using Supercharging Agents.International journal of mass spectrometry · 2018Article
- Real-time HD Exchange Kinetics of Proteins from Buffered Aqueous Solution with Electrothermal Supercharging and Top-Down Tandem Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2016Article
- Salt Bridge Rearrangement (SaBRe) Explains the Dissociation Behavior of Noncovalent Complexes.Journal of the American Society for Mass Spectrometry · 2016Article
- Probing Protein Structure and Folding in the Gas Phase by Electron Capture Dissociation.Journal of the American Society for Mass Spectrometry · 2015Article
- Supercharging with m-nitrobenzyl alcohol and propylene carbonate: forming highly charged ions with extended, near-linear conformations.Analytical chemistry · 2015Article
- What protein charging (and supercharging) reveal about the mechanism of electrospray ionization.Journal of the American Society for Mass Spectrometry · 2014Article
- Characterization of native protein complexes using ultraviolet photodissociation mass spectrometry.Journal of the American Chemical Society · 2014Article
- Anions in electrothermal supercharging of proteins with electrospray ionization follow a reverse Hofmeister series.Analytical chemistry · 2014Article
- Investigation of stable and transient protein-protein interactions: Past, present, and future.Proteomics · 2013Review
- Electrothermal supercharging in mass spectrometry and tandem mass spectrometry of native proteins.Analytical chemistry · 2013Article
- Ligand migration in the gaseous insulin-CB7 complex--a cautionary tale about the use of ECD-MS for ligand binding site determination.Journal of the American Society for Mass Spectrometry · 2012Article
- Electrothermal supercharging of proteins in native electrospray ionization.Analytical chemistry · 2012Article
- Supercharging protein complexes from aqueous solution disrupts their native conformations.Journal of the American Society for Mass Spectrometry · 2012Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
His64 and His93 are the two well-known sites of heme binding in water-dissolved holo-myoglobin, with His93 being a proximal, strongly binding partner, while the distal His64 weakly coordinates to the heme through a small-molecule ligand, e.g., water or O(2). The heme bonding scheme in a water-free environment is as yet unclear. Here we employed electron transfer dissociation tandem mass spectrometry to study the preferential attachment site of the ferri-heme (Fe(3+)) in electrospray-produced 12+, 14+, and 16+ holo-myoglobin ions. Contrary to expectations, in lower-charge complexes that should have a structure resembling that in solution, the heme seems to be preferentially attached to the "distal" histidine. In contrast, in the highest studied charge state, the "proximal" histidine is the site of preferential attachment; the 14+ charge state is an intermediate case. This surprising finding raises a question of heme coordination in proteins transferred to water-free environment, as well as the effect of the protonation sites on heme bonding.
Indexed as
Identifiers
21952890What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.