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Showing 1 to 12 of 12 for “"Hemoprotein"”.
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Functional Analysis of the N -Terminal Transmembrane/signal -Anchor Sequence and Linker Domain of Cytochrome P450 2C2
… of the signal anchor decreases assembly of P450 hemoprotein in E. coli but does not change the in vivo distribution of the protein. However, it alters the nature of membrane interaction such that P450 2C2 is no longer an integral membrane protein. Moreover, the results show that the linker domain …
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Investigation of a Heme Uptake System in Acinetobacter baumannii
… gene clusters functions to support growth in hemoprotein scarce conditions. This gene cluster encodes an outer membrane translocon that secretes a hemophore called HphA into the environment. HphA binds to Hb and passively scavenges its heme, which is then shuttled to the outer membrane …
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Partial structural characterization of the cytoplasmic hemoglobin of Nostoc commune UTEX 584 expressed in Escherichia coli
… Nostoc commune revealed a gene encoding for a hemoprotein, known as cyanoglobin. The cyanoglobin gene was isolated and subcloned into Escherichia coli previously. The study presented here encompasses the optimization of growth conditions for the transformed F. coli, with subsequent induction of …
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Cytochrome c peroxidase : its role in nitrosative stress and purification as a GST-fusion protein
Cytochrome c Peroxidase (CCP) is a hemoprotein found in the intermembrane space of yeast mitochondria. One of its roles is to protect the cell against oxidative stress by reducing mitochondrial H 2 O 2 to H 2 O. Titration of CCP with peroxynitrite [ONOO(H)] formed a species with an absorption …
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Structural and Functional Characterization of Cyanoglobin: A Peripheral Membrane Hemoglobin in Nostoc commune UTEX 584 (Cyanobacteria)
… commune UTEX 584 revealed a gene encoding a hemoprotein, named cyanoglobin. The cyanoglobin gene was isolated and subcloned into Escherichia coli previously. Cyanoglobin possesses a high oxygen affinity. The study presented here investigated the functional role of cyanoglobin, and encompassed …
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Purification and characterization of the hepatic microsomal monooxygenase system from the coastal marine fish Stenotomus chrysops
… or S. aureus V8 protease. An additional hemoprotein fraction called cytochrome P-450 fraction D was also resolved and partially purified. This cytochrome P-450 preparation was characterized by a red shift in the CO-ligated, reduced difference spectrum with a chromophore near 451 nm. The …
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The Physical Chemistry Underlying the Assembly and Midpoint Potential Control in a Series of Designed Protein-Maquettes
… a key parameter underlying the diversity of hemoprotein functions. The findings from my work provide the first views of heme and maquette assembly: spontaneous, rapid and with high affinity association. They also provide a foundation for understanding what controls redox potentials of the …
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Destruction of biological tetrapyrrole macrocycles by hypochlorous acid and its scavenging by lycopene
… acid (HOCl) is a potent oxidant generated by the hemoprotein myeloperoxidase. Although HOCl plays an important role in the innate immune response,sustained high levels of HOCl has been implicated to play a harmful role. In several pathological conditions such as atherosclerosis, endometriosis and …
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Developing assays to study and screen engineered Escherichia coli NADPH-dependent sulfite reductase
… oxidative flavoprotein subunit and a reductase hemoprotein subunit that assemble in a unique asymmetrical stoichiometry to efficiently coordinate the large-volume electron transfer reaction. This oxidoreductase lends itself to numerous design opportunities due to (i) available crystal structures …
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Understanding the Effects of Higher-Order Assembly on the Structure of Sulfite Reductase
… of a flavoprotein (SiRFP) and four subunits of a hemoprotein (SiRHP). SiRFP is a diflavin reductase, a homolog of cytochrome P450 reductase (CPR) that is composed of the following domains: a FMN binding flavodoxin (Fld)-like-domain, a connection domain interrupting FAD/NADPH bind- ing FNR …
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Nouveau rôle pour la ferriréductase Frp1 dans l’acquisition de l’hème par la voie Shu1-dépendante chez la levure Schizosaccharomyces pombe
Le fer est un élément essentiel pour toutes les cellules eucaryotes. Cet oligo-élément est requis pour le déroulement de nombreux processus biologiques fondamentaux. Une source importante de fer est la molécule d’hème, qui elle, constitue également un cofacteur indispensable pour plusieurs …