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Detection of hydroperoxy complex in the oxidative reactions of myoglobin with hydrogen peroxide
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 ...
Effect of the Histidine E7 amino acid in the sulfheme formation of the hemoglobin I from Lucina Pectinata
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 ...
Sulfheme formation mechanism and spectra analysis using QM/MM and TDDFT
Since the 1863 discovery of a new green hemoglobin derivative called “sulfhemoglobin”, the nature of its characteristic 618 nm absorption band and formation mechanism has been the subject of several hypotheses. Many ...
Global and local structural analysis of the sulfheme complex: A role in the decrease of myoglobin functionality
When the human body is exposed to high concentration of hydrogen sulfide (H2S, recently identified as a signaling gas), a rare type of anemia called sulfhemoglobinemia is developed. This condition is triggered by the ...
Crystal structures of hemeproteins: Sulf and H2S myoglobin derivatives and Lucina pectinata Oxy (HbII-HbIII) and Oxy (HbIII-HbIII) systems
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 ...
Sulfmyoglobin formation pathway upon reaction of oxy-myoglobin and hydrogen sulfide
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 ...