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Combination of native mass spectrometry, ion mobility, and collision induced unfolding experiments in the chromatographic time scale to unravel the structure of hemoglobin of bird species

Structural Proteomics Top-down & Middle-down

Abstract #250 Posted on28 March 20259 May 2025 9 May 2025 19h02

Abstract

Hemoglobin has a critical role on oxygen transportation in all vertebrates. Although in humans it is thoroughly characterized, structural information of hemoglobin homologue in birds is still scarce with particularly limited information regarding their native structure.
In this context, an analytical strategy based on the combination of size exclusion chromatography (SEC), native MS, and ion mobility (IM) has been developed to reveal information about composition and global conformation of bird hemoglobin, showing the proof of concept with Darwin’s Rhea samples.
SEC-nMS results show the coexistence of three different tetrameric structures allowing the relative quantification of these populations with the possibility to identify an endogenous cofactor characteristic of bird hemoglobine (IP5). IM and CIU experiments in the chromatographic time-scale allowed to characterize the global conformation of the proteins, and their gas-phase stability highlighting that tetramer stability and compaction strongly depend on tetramer subunit composition. Finally, O2-affinity tests were carried out for the first time on individual tetramer populations, leading to the conclusion that tetramer O2 affinity is driven by the presence of aD tetramer subunits.
This methodology allowed in-depth characterization of Darwin Rhea hemoglobin with straight correlation between structure, and individual tetramer function and can be tailored for a wide range of bird hemoglobin homologues.

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Hemoglobin has a critical role on oxygen transportation in all vertebrates. Although in humans it is thoroughly characterized, structural information of hemoglobin homologue in birds is still scarce with particularly limited information regarding their native structure.
In this context, an analytical strategy based on the combination of size exclusion chromatography (SEC), native MS, and ion mobility (IM) has been developed to reveal information about composition and global conformation of bird hemoglobin, showing the proof of concept with Darwin’s Rhea samples. 
SEC-nMS results show the coexistence of three different tetrameric structures allowing the relative quantification of these populations with the possibility to identify an endogenous cofactor characteristic of bird hemoglobine (IP5). IM and CIU experiments in the chromatographic time-scale allowed to characterize the global conformation of the proteins, and their gas-phase stability highlighting that tetramer stability and compaction strongly depend on tetramer subunit composition. Finally, O2-affinity tests were carried out for the first time on individual tetramer populations, leading to the conclusion that tetramer O2 affinity is driven by the presence of aD tetramer subunits.
This methodology allowed in-depth characterization of Darwin Rhea hemoglobin with straight correlation between structure, and individual tetramer function and can be tailored for a wide range of bird hemoglobin homologues.

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