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Crystallographic structures of hemoglobin II (HbII) from Lucina Pectinata in the 4–9 pH range
(2011)
Lucina pectinata’s ctenidia contains three hemeproteins: the hydrogen sulfide reactive hemoglobin I (HbI) and the oxygen transporting hemoglobins II and III (HbII and HbIII) that remain unaffected by the presence of H2S. ...
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 ...
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 ...
NMR structural determinants of lucina pectinata hemoglobin I active center moieties
(2013)
The clam Lucina pectinata Hemoglobin I (HbI) is a monomeric protein with a prosthetic group, known as heme group, in which the iron atom can either be in the ferrous (Fe(II)) or the ferric (Fe(III)) oxidation state. This ...
Oxidation reactions of Lucina pectinata hemoglobins: Model system to design heme protein based blood substitutes
(2008)
Today, efforts are focused in the production of a second-generation blood substitutes that minimizes the oxidative stress and the tissue vasoactivity. The infused cell-free hemoglobin’s can act as nitric oxide (NO) scavenger ...
Femtosecond spectroscopy studies of recombinant hemoglobin I of the clam Lucina pectinata (Gmelin, 1791)
(2011)
Lucina pectinata (Gmelin, 1791) is a clam that can be found in sulfide-rich muds in the
coastal mangroves of the southwest coast of Puerto Rico. It contains three different
hemoglobins in the gill tissue, hemoglobin I, ...
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. ...
Sulfheme formation mechanism and spectra analysis using QM/MM and TDDFT
(2018-05)
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 ...
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 ...
Structural characterization of the oxygen reactive heamoglobins from the clam Lucina pectinata
(2014)
Hemoglobins comprise a challenging area of study within biochemical research. They play an
important physiological role in organisms, like oxygen transport and storage. Three hemoglobins were discovered in the ctenidia ...