Nagababu E, Rifkind J M
National Institute of Health, National Institute on Aging, Laboratory of Cellular and Molecular Biology, Baltimore, Maryland 21224-6823, USA.
Biochem Biophys Res Commun. 1998 Jun 29;247(3):592-6. doi: 10.1006/bbrc.1998.8846.
Hemoglobin and methemoglobin oxidized by hydrogen peroxide generate ferrylhemoglobin and oxoferrylhemoglobin, respectively. Two fluorescent compounds were found to be produced during the reaction of oxyhemoglobin, but not methemoglobin, with H2O2. These two compounds had excitation wavelengths of 321 nm and 460 nm, respectively, with emission wavelengths of 465 nm and 525 nm, respectively. The formation of the same fluorescent products during the reaction of H2O2 with ferroprotoporphyrin-IX and ferriprotoporphyrin-IX demonstrate that these compounds originate from the heme moiety. The release of heme iron during the formation of these fluorescent compounds indicates that they are associated with heme degradation. The time course for the formation of fluorescent products show that the extent of heme degradation is dependent on H2O2 concentration. The results of this investigation indicate that the heme moiety of Fe(II) hemoglobin undergoes degradation in presence of H2O2. The ability to detect this process by fluorescence provides a sensitive marker in order to asses hemoglobin and RBC oxidative stress under pathological conditions.
被过氧化氢氧化的血红蛋白和高铁血红蛋白分别生成高铁血红蛋白和氧合高铁血红蛋白。在氧合血红蛋白与过氧化氢反应过程中发现产生了两种荧光化合物，但高铁血红蛋白与过氧化氢反应时未产生。这两种化合物的激发波长分别为321nm和460nm，发射波长分别为465nm和525nm。过氧化氢与亚铁原卟啉-IX和高铁原卟啉-IX反应过程中形成相同的荧光产物，表明这些化合物起源于血红素部分。在这些荧光化合物形成过程中血红素铁的释放表明它们与血红素降解有关。荧光产物形成的时间进程表明血红素降解程度取决于过氧化氢浓度。本研究结果表明，在过氧化氢存在下，Fe(II)血红蛋白的血红素部分会发生降解。通过荧光检测这一过程的能力为评估病理条件下血红蛋白和红细胞的氧化应激提供了一个敏感指标。
