Mollan, Todd L.Banerjee, SambuddhaWu, GangSiburt, Claire J.ParkerTsai, Ah-LimOlson, John S.Weiss, Mitchell J.Crumbliss, Alvin L.Alayash, Abdu I.2013-02-012014-02-022012Mollan, Todd L., Banerjee, Sambuddha, Wu, Gang, et al.. "Alpha-hemoglobin stabilizing protein (AHSP) markedly decreases the redox potential and reactivity of alpha subunits of human HbA with hydrogen peroxide." <i>Journal of Biological Chemistry,</i> (2012) The American Society for Biochemistry and Molecular Biology, Inc.: http://dx.doi.org/10.1074/jbc.M112.412064.https://hdl.handle.net/1911/69913Background: AHSP modifies redox properties of bound α subunits. Results: Isolated hemoglobin subunits exhibit significantly different redox properties compared to HbA. A significant decrease in the reduction potential of α subunits bound to AHSP results in preferential binding of ferric α. Conclusion: AHSP:α subunit complexes do not participate in ferric-ferryl heme redox cycling. Significance: AHSP binding to α subunits inhibits subunit pseudoperoxidase activity.engArticle is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.Journal articlehttp://dx.doi.org/10.1074/jbc.M112.412064