Antioxidative Pseudoenzymatic Mechanism of NAD(P)H Coexisting with Oxyhemoglobin for Suppressed Methemoglobin Formation

Oxyhemoglobin (HbO2) coexisting with equimolar NADH retards autoxidation and oxidant-induced metHb formation based on the pseudocatalase (CAT) and pseudosuperoxide dismutase (SOD) activities. In this work, we compared the effects of NADH with those of NADPH and estimated the binding site of NAD(P)H...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Biochemistry (Easton) 2019-03, Vol.58 (10), p.1400-1410
Hauptverfasser:	Yamada, Magohei, Matsuhira, Takashi, Yamamoto, Keizo, Sakai, Hiromi
Format:	Artikel
Sprache:	eng
Schlagworte:	Antioxidants - metabolism Binding Sites - genetics Catalase - metabolism Hemoglobins Hydrogen Peroxide Methemoglobin - biosynthesis Methemoglobin - metabolism NAD - metabolism NADP - metabolism Oxidants Oxidation-Reduction Oxyhemoglobins - metabolism Superoxide Dismutase - metabolism
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Beschreibung
Zusammenfassung:	Oxyhemoglobin (HbO2) coexisting with equimolar NADH retards autoxidation and oxidant-induced metHb formation based on the pseudocatalase (CAT) and pseudosuperoxide dismutase (SOD) activities. In this work, we compared the effects of NADH with those of NADPH and estimated the binding site of NAD(P)H to HbO2 to elucidate the antioxidative mechanisms. The results clarified that pseudo-CAT and pseudo-SOD activities of HbO2 coexisting with NADPH were similar to activities obtained with NADH. Prompt MetHb formation (
ISSN:	0006-2960 1520-4995
DOI:	10.1021/acs.biochem.8b01314