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