Open AccessHemoglobin – source of reactive oxygen species
Author(s) -
Ewa Zapora,
Iwona Jarocka
Publication year - 2013
Publication title -
postępy higieny i medycyny doświadczalnej
Language(s) - Uncategorized
Resource type - Journals
SCImago Journal Rank - 0.275
H-Index - 34
eISSN - 1732-2693
pISSN - 0032-5449
DOI - 10.5604/17322693.1043334
Subject(s) - chemistry , hemoglobin , hydrogen peroxide , heme , reactive oxygen species , carbon monoxide , biliverdin , heme oxygenase , oxygen , lipid peroxidation , biochemistry , inorganic chemistry , enzyme , catalysis , organic chemistry
Erythrocytes are especially vulnerable to reactive oxygen species because of their direct role in oxygen transport. Moreover, hemoglobin contains iron ions (Fe²⁺), which catalyze both the Fenton reaction and lipid peroxidation. Reactive oxygen species in erythrocytes are also generated through nonenzymatic and enzymatic processes of heme degradation. The nonenzymatic process of heme degradation is initiated by e.g. hydrogen peroxide, whereas the process of enzymatic degradation is under the influence of heme oxygenase. In both cases biliverdin, carbon monoxide (CO) and iron ions (Fe²⁺) are generated. These products of heme degradation can initialize the oxidative processes within erythrocytes, but at low concentrations exhibit cytoprotective properties.