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Electrochemistry of Hemoglobin I from Lucina pectinata immobilized on a modified gold electrode with cysteine or 3-mercaptopropionic acid: Electrochemical activity for hydrogen sulfide
(2012)
The extraordinary affinity of recombinant hemoglobin I from Lucina pectinata (rHbI) for hydrogen sulfide (H2S) allow to postulate it as substrate for the preparation of the hydrogen sulfide sensors. The modification of a ...
Hemoglobin I from Lucina pectinata: A model for hydrogen sulfide reactivity within hemeproteins
(2009)
The hemoglobin I (HbI) from the clam Lucina pectinata is an intriguing hemeprotein that binds and transports H2S to chemoautotrophic bacteria to maintain a symbiotic relationship and to protect the mollusk from H2S toxicity. ...
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 ...
Global and local structural analysis of the sulfheme complex: A role in the decrease of myoglobin functionality
(2016)
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
(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 ...
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 ...