Abdulhamid I

No ORCID on file · 3 papers in corpus · active 2011-2014
2014
Disruption of heme-peptide covalent cross-linking in mammalian peroxidases by hypochlorous acid.
Journal of inorganic biochemistry ·doi:10.1016/j.jinorgbio.2014.06.018

Myeloperoxidase (MPO), lactoperoxidase (LPO) and eosinophil peroxidase (EPO) play a central role in oxidative damage in inflammatory disorders by utilizing hydrogen peroxide and halides/pseudo halides to generate the corresponding hypohalou…

2013
Myeloperoxidase acts as a source of free iron during steady-state catalysis by a feedback inhibitory pathway.
Free radical biology & medicine ·doi:10.1016/j.freeradbiomed.2013.04.009

Myeloperoxidase (MPO) is a heme-containing enzyme that generates hypochlorous acid (HOCl) from chloride (Cl(-)) and hydrogen peroxide (H₂O₂). It is implicated in the pathology of several chronic inflammatory conditions such as cardiovascula…

2011
Mechanism of hypochlorous acid-mediated heme destruction and free iron release.
Free radical biology & medicine ·doi:10.1016/j.freeradbiomed.2011.03.040

Here, we show that hypochlorous acid (HOCl), a potent neutrophil-generated oxidant, can mediate destruction of free heme (Ht) and the heme precursor, protoporphyrin IX (PPIX). Ht displays a broad Soret absorbance peak centered at 365 and 39…