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Detection of hydroperoxy complex in the oxidative reactions of myoglobin with hydrogen peroxide
(2008)
A large number of heme enzymes catalyze the heterolysis of hydrogen peroxide (H2O2) and H2O2 is used as a source of oxidizing equivalents for biological oxidative reaction. Despite the increased understanding of the reactions ...
Sulfmyoglobin formation pathway upon reaction of oxy-myoglobin and hydrogen sulfide
(2019-12-03)
Myoglobin (Mb) binds oxygen with high affinity as a low spin singlet complex and thus functions as an oxygen storage protein. Quantum chemical calculations of oxy-Mb models with hydrogen sulfide (H2S) in the active site ...
Crystal structures of hemeproteins: Sulf and H2S myoglobin derivatives and Lucina pectinata Oxy (HbII-HbIII) and Oxy (HbIII-HbIII) systems
(2020-04-21)
As a gasotransmitter, hydrogen sulfide (H2S) biochemistry in humans is of pivotal importance. One relevant reaction of H2S in our bodies is its interaction with hemeproteins. The threshold of its beneficial/harmful effects ...
Effect of the Histidine E7 amino acid in the sulfheme formation of the hemoglobin I from Lucina Pectinata
(2008)
Sulfhemoglobin is a non-functional derivative of hemoglobin known to be produced by exposure to sulfa drugs, air pollution and others. It is formed by the reaction between H2O2, H2S and the heme group in the presence of ...