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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 ...
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. ...
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, ...
The role of position E11 in the stabilization of the HbI-SH2 complex from L. pectinata
(2007)
The bivalve mollusk, Lucina pectinata, contains three hemoglobins: hemoglobin I (HbI) which is a H2S reactive protein, hemoglobin II (HbII) and hemoglobin III (HbIII) which deliver O2 to the organism. HbI is a monomeric ...
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. ...
New crystallographic structures of Oxy-HbII-III and CN-HbII-III forms from Lucina pectinata
(2011)
The clam Lucina pectinata is found in the sulfide-rich southwest coastal sediments of La Parguera, Puerto Rico in the Caribbean Sea. This bivalve mollusk has developed a chemoautotrophic symbiotic relation with the bacteria ...
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 ...
Expression and purification of Lucina pectinata recombinant hemoglobin II and the effect of the oxygen affinity on the heme pocket
(2009)
Lucina pectinata is a bivalve mollusk that inhabits sulfide rich sediments along, the west coast of Puerto Rico. This clam contains three hemoglobins that deliver and transport oxygen (HbII and III) and hydrogen sulfide ...
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 ...
Structural aspects and chemical species involved in the hemeperoxidases catalytic oxidation of hydrogen sulfide by hydrogen peroxide and oxygen
(2018)
Hydrogen sulfide (H2S) has gained attention since it is implied in human physiological functions with potential therapeutically effects. Furthermore, H2S interacts with physiologically important hemeproteins such as ...