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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 E11 amino acid on the ligand binding in Hemoglobin I from Lucina pectinata
(2007)
Hemoglobin I (HbI) from Lucina pectinata (clam) is a protein that binds and transports H2S to the bacteria in the clam. HbI is one of the few known hemoglobins that carries H2S, toxic gas, in its active site, which contains ...
(His)6 -tag recombinant hemoglobin I from Lucina Pectinata: A novel hydrogen sulfide protein donor
(2020-07)
Hydrogen Sulfide (H2S) is a gasotransmitter involved in physiological and pathological
processes in humans and animals. It is produced endogenously in humans through enzymatic
pathways. H2S is associated with the ...