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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 ...
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 ...
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. ...
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 ...
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 ...
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 ...
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 ...
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 ...