2007
DOI: 10.1016/j.bbapap.2006.11.005
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Inactivation of alcohol dehydrogenase (ADH) by ferryl derivatives of human hemoglobin

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Cited by 11 publications
(9 citation statements)
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“…3c ). Consistent with the previous reports 23 24 25 , the half autoreduction time of ferryl-Hb was 35-fold longer than that of ROS, and the cytotoxicity of ROS could be greatly promoted by oxidizing Hb to cytotoxic ferryl-Hb in I-ARCs mediated PDT. Due to the prolonged lifetime, ferryl-Hb could diffuse a much longer distance in cells than ROS, thus creating a far more persistent oxidative damage, subsequently led to cell death 26 .…”
Section: Resultssupporting
confidence: 91%
See 1 more Smart Citation
“…3c ). Consistent with the previous reports 23 24 25 , the half autoreduction time of ferryl-Hb was 35-fold longer than that of ROS, and the cytotoxicity of ROS could be greatly promoted by oxidizing Hb to cytotoxic ferryl-Hb in I-ARCs mediated PDT. Due to the prolonged lifetime, ferryl-Hb could diffuse a much longer distance in cells than ROS, thus creating a far more persistent oxidative damage, subsequently led to cell death 26 .…”
Section: Resultssupporting
confidence: 91%
“…It indicated that, the bounteous ROS production was essential for ferryl-Hb conversion. As reported, the half-life of ferryl-Hb was prolonged by several orders of magnitude, compared to ROS 23 24 25 . The level of ROS in I-ARCs quickly declined in solution within 5 min after laser irradiation, confirming its short life span, but the level of ferryl-Hb in I-ARCs remained 94.8% under the same conditions ( Fig.…”
Section: Resultssupporting
confidence: 55%
“…Ferryl derivatives are formed upon haemoglobin irradiation under air in the reaction of H 2 O 2 with methaemoglobin (Winterbourn 1990, McArthur & Davies 1993. We have demonstrated previously (Kowalczyk et al 2007) that ferryl derivatives of Hb inactivate ADH. Miura et al (1995Miura et al ( , 1997 have also shown that ferryl derivatives of myoglobin inactivates glyceraldehydes-3-phosphate dehydrogenase, alcohol dehydrogenase and creatine kinase, enzymes with 7SH groups at the active sites.…”
Section: Discussionmentioning
confidence: 96%
“…In vivo, these reactions are of physiological relevance un-der ischemic conditions (Patel et al, 1996). Ferryl hemoglobin is able to oxidize proteins, nucleic acids and lipids (Kanner & Harel, 1985;Everse et al, 1994;Goldman et al, 1998;Kowalczyk et al, 2007). The globin radical in ferrylHb is very unstable and rapidly decays to a longer-lived radical-free ferryl form (McArthur & Davies, 1993).…”
Section: Introductionmentioning
confidence: 99%
“…The globin radical in ferrylHb is very unstable and rapidly decays to a longer-lived radical-free ferryl form (McArthur & Davies, 1993). FerrylHb undergoes slow acid-catalyzed autoreduction to the ferric (met) form (Tresoriere et al, 2001), but the regenerated metHb is not identical with the initial met state: some hemichrome and dimers of Hb subunits are also formed (Kowalczyk et al, 2007). The reduction of the ferryl form of hemoglobin is facilitated by some reducing compounds, including ascorbate (Giulivi & Davies, 1990), rutin (Grinberg et al, 1994), urate (Everse & Hsia, 1997), melatonin (Tresoriere et al, 2001), trolox (Tresoriere et al, 2001, and epigallocatechin (Jia & Alayash, 2008).…”
Section: Introductionmentioning
confidence: 99%