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. 2020 Jun 24;9(6):549. doi: 10.3390/antiox9060549

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© 2020 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Matrix assisted laser desorption mass spectrometry-time of flight (MALDI-TOF) mass spectrometric analysis of ascorbic acid-mediated reversal of heme-protein crosslinks in H₂O₂-reacted metMb. (A) (Bottom spectra) MetMb tryptic digests that were reacted with 100 μM H₂O₂ displayed loss of the N-terminal peptide (1815.9 m/z) indicated by arrows in the untreated MetMb (top spectra). (B–D) Tryptic digests of H₂O₂-reacted metMb that was then treated with ascorbic acid revealed the re-appearance of the N-terminal peptide. (E). MetMb monomer (bottom) and dimer (top) tryptic digests that were reacted with 300 µM H₂O₂ and analyzed with MALDI-TOF MS. The arrow indicates a peak at 1993 m/z, which suggests presence of a heme crosslinked to a peptide containing the distal histidine of Mb helix E.