Recombinant Hemoglobin II From Lucina pectinata: A Large-Scale Method For Hemeprotein Expression in E. coli
نویسندگان
چکیده
منابع مشابه
Expression and purification of recombinant hemoglobin I from Lucina pectinata.
Hemoglobin I (HbI) from Lucina pectinata reacts with hydrogen sulfide to form the ferric sulfide complex needed to transport H2S to the bacterial endosymbiont. To further study HbI, expression studies of this protein were performed in Escherichia coli. This is the first time that the recombinant HbI was produced using a recombinant DNA expression system. Hemoglobin I cDNA was amplified and clon...
متن کاملStructure and ligand selection of hemoglobin II from Lucina pectinata.
Lucina pectinata ctenidia harbor three heme proteins: sulfide-reactive hemoglobin I (HbI(Lp)) and the oxygen transporting hemoglobins II and III (HbII(Lp) and HbIII(Lp)) that remain unaffected by the presence of H(2)S. The mechanisms used by these three proteins for their function, including ligand control, remain unknown. The crystal structure of oxygen-bound HbII(Lp) shows a dimeric oxyHbII(L...
متن کاملCharacterization and Expression of the Lucina pectinata Oxygen and Sulfide Binding Hemoglobin Genes
The clam Lucina pectinata lives in sulfide-rich muds and houses intracellular symbiotic bacteria that need to be supplied with hydrogen sulfide and oxygen. This clam possesses three hemoglobins: hemoglobin I (HbI), a sulfide-reactive protein, and hemoglobin II (HbII) and III (HbIII), which are oxygen-reactive. We characterized the complete gene sequence and promoter regions for the oxygen react...
متن کاملLarge-scale synthesis of globotriose derivatives through recombinant E. coli.
The carbohydrate chains decorating cell membranes and secreted proteins participate in a range of important biological processes. However, their ultimate significance and possible therapeutic potential have not been fully explored due to the lack of economical methods for their production. This study is an example of the use of a genetically engineered bacterial strain in the preparation of div...
متن کاملEffects of active site mutations in haemoglobin I from Lucina pectinata: a molecular dynamic study
Haemoglobin I from Lucina pectinata is a monomeric protein consisting of 142 amino acids. Its active site contains a peculiar arrangement of phenylalanine residues (PheB10, PheCD1 and PheE11) and a distal Gln at position E7. Active site mutations at positions B10, E7 and E11 were performed in deoxy haemoglobin I (HbI), followed by 10 ns molecular dynamic simulations. The results showed that the...
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ژورنال
عنوان ژورنال: The Protein Journal
سال: 2010
ISSN: 1572-3887,1573-4943
DOI: 10.1007/s10930-010-9234-8