Myeloperoxidase acts as a source of free iron during steady-state catalysis by a feedback inhibitory pathway

Free Radical Biology and Medicine

Volumn 63, Issue , 2013, Pages 90-98

  Maitra, Dhiman ^a   Shaeib, Faten ^a   Abdulhamid, Ibrahim ^b   Abdulridha, Rasha M ^a   Saed, Ghassan M ^a   Diamond, Michael P ^c   Pennathur, Subramaniam ^d   Abu Soud, Husam M ^a,e  

^a WAYNE STATE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b CHILDREN'S HOSPITAL OF MICHIGAN   (United States)

^c MEDICAL COLLEGE OF GEORGIA   (United States)

^d UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

^e WAYNE STATE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Feedback inhibition; Free iron; Free radicals; Hypochlorous acid; Inflammation; Myeloperoxidase; Oxidative stress

Indexed keywords

CHLORIDE; FERROZINE; HEME; HYDROGEN PEROXIDE; HYPOCHLOROUS ACID; IRON; MYELOPEROXIDASE;

ARTICLE; CATALYSIS; ELECTRODE; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME KINETICS; HUMAN; HUMAN CELL; IRON BINDING CAPACITY; IRON KINETICS; NEGATIVE FEEDBACK; PRIORITY JOURNAL; STEADY STATE; SYNTHESIS; ULTRAVIOLET SPECTROSCOPY;

EID: 84878428854     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2013.04.009     Document Type: Article

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