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Showing 1 to 20 of 115 for “"cytochrome C oxidase"”.
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Infrared Spectroscopy of Cytochrome C Oxidase Intermediate States
Cytochrome c oxidase is a critical player in the process of cellular respiration, performing proton translocation coupled to the four-electron reduction of O2 to H2O. To accomplish this catalytic task, specific changes at the active site influence chemical and physical changes throughout the …
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Toward model compounds for the resting cytochrome c oxidase active site
… analogs of derivatized active-site structures of cytochrome c oxidase. Part II. Imidazolate-bridged, mixed-metal binuclear porphyrin compounds have been reinvestigated to model the proposed imidazolate-bridged (cytochrome $a\sb3\sp{3+}$(imid)Cu$\sp{2+}$) active-site structure of resting cytochrome …
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Assembly of cytochrome c oxidase: the role of hSco1p and hSco2p
COX deficiency in human presents a plethora of phenotypes which is not surprising given the complexity of the enzyme structure and the multiple factors and many steps required for its assembly. A functional COX requires three mitochondrially encoded subunits (Cox1p, Cox2p and Cox3p), at least 10 …
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The Study of Aa3-Type Cytochrome C Oxidase in Rhodobacter Sphaeroides
Cytochrome c oxidase is the final electron acceptor in the respiratory chain and catalyzes the highly exergonic oxygen reduction reaction to water and forms a transmembrane electrochemical proton gradient. This transmembrane gradient is used by ATP synthase to produce ATP. The oxygen chemistry …
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The study of aa3-type cytochrome c oxidase in Rhodobacter sphaeroides
Cytochrome c oxidase is the final electron acceptor in the respiratory chain and catalyzes the highly exergonic oxygen reduction reaction to water and forms a transmembrane electrochemical proton gradient. This transmembrane gradient is used by ATP synthase to produce ATP. The oxygen chemistry …
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Studies on the Proton Pumping Mechanism of Aa(3)-Type Cytochrome C Oxidase
The monomeric form of bovine heart mitochondrial cytochrome c oxidase was used to detect directly the proton uptake and release events during the F-to-O transition. Absorption change of the pH sensitive dye was monitored spectroscopically. Rapid proton release followed by slow proton uptake was …
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Biochemical Studies on the Catalytic Cycle of Cytochrome C Oxidase in Rhodobacter Sphaeroides
Cytochrome c oxidase from Rhodobacter sphaeroides exhibits properties similar to those of mitochondrial bovine oxidase. The X-ray crystal structure of cytochrome c oxidase from Paracoccus denitrificans reveals two proton channels leading to the binuclear center. (Iwata, S., Ostermeier, C., Ludwig, …
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Study of the Proton Pumping Mechanism of the Aa3-Type Cytochrome C Oxidase
Cytochrome c oxidase is the last component of the respiratory chains. It accepts electrons from a water-soluble or membrane-anchored cytochrome c and catalyzes the reduction of O2 to water (O2 + 4e- + 4H+ → 2 H2O). In cytochrome aa3 oxidase (C cO), electrons from cytochrome c are first …
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Electrostatic and quantum chemical investigation of the proton pumping mechanism of cytochrome c oxidase
Cytochrome c oxidase is a crucial enzyme in the respiratory chain. It catalyzes the reduction of oxygen to water and utilizes the free energy of the reduction reaction for proton pumping across the inner-mitochondrial membrane, a process which results in a membrane electrochemical proton gradient. …
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Identification and characterisation of new factors and mechanisms regulating human cytochrome c oxidase biogenesis
Assembly of the mitochondrial complex IV (CIV) or cytochrome c oxidase (COX) is an intricate and highly regulated process in which the three-core mitochondrial DNA (mtDNA) encoded subunits assemble in a coordinated way with the remaining eleven supernumerary nuclear DNA (nDNA) encoded subunits. …
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Using Mitochondrial Cytochrome C Oxidase Subunit I Sequence To Resolve The Springsnail Species Complex: Pyrgulopsis Micrococcus
… a 621 base pair fragment of the mitochondrial cytochrome c oxidase subunit I (mtCOI) gene was sequenced from 1-6 individuals from thirteen populations, in three river systems in the Death Valley region. Outgroups included regional congeners P. amargosae, P. guilani, P. neritella, P. owensensis, …
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Studies on Critical Proton Pathway Residues in the Aa3-Type Cytochrome C Oxidase From Rhodobacter Sphaeroides
… the cytoplasmic membrane of aerobic prokaryotes. Cytochrome c oxidase, the terminal member of this respiratory chain, catalyzes the four-electron reduction of oxygen to water and uses the free energy of this reaction to translocates protons across the membrane. The oxidase accomplishes oxygen …
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Studies on critical proton-pathway residues in the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides
… the cytoplasmic membrane of aerobic prokaryotes. Cytochrome c oxidase, the terminal member of this respiratory chain, catalyzes the four-electron reduction of oxygen to water and uses the free energy of this reaction to translocates protons across the membrane. The oxidase accomplishes oxygen …
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Cytochrome c oxidase mediates the regulation of mitochondrial function in an in vitro model of Huntington's disease
Mitochondrial dysfunction leading to neurodegenerative diseases involves structural and functional changes of respiratory chain enzyme complexes. The data shown here manifested the effect of 3-nitropropionic acid (NPA), a mitochondrial toxin and in vitro model of Huntington’s disease (HD), on …
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A putative interaction between mitochondrial cytochrome c oxidase subunit II (COX II) to lamin A/C and LAP2α in colon epithelial cells.
… to Lamin A/C and/or LAP2a. It was found Cytochrome c oxidase subunit II (Cox2) is a putative binding partner to Lamin A/C and LAP2 α. Cox2 is encoded by the mitochondrial genome and imported into complex IV (COX) of the mitochondrial respiratory chain (MRC). The majority of mitochondrial …
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The AA3 Type Cytochrome C Oxidase From Rhodobacter Sphaeroides: Insights Into the Proton Pumping Mechanism From the N139D Mutation in the D-Channel
Cytochrome c oxidase, an integral membrane protein, is the final enzyme of the electron transport chain. The two sides of the membrane are denoted as the N side (the cytoplasmic side in bacteria and the matrix side of mitochondria in eukaryotes) and the P side (the periplasmic side in bacteria and …
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Investigating the Tyrosine-Histidine Linkage in the Copper B Site of Cytochrome C Oxidase: Model Studies Utilizing a Zinc Imidazole-Phenol Containing Complex
A chelating ligand (BPAIP) was synthesized incorporating an ortho substituted imidazole-phenol moiety. The resultant Zn(II) complex, [Zn(BPAIP)(Br)]+, was found to exhibit a decreased pK A (8.24) and increased oxidation potential relative to the unbound BPAIP. In addition, the stability of …
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The role of the cytochrome B and cytochrome C oxidase III genes in the immune response of the South African abalone, Haliotis midae
… Two genes of the electron transport system, cytochrome b and cytochrome c oxidase III, were found to be upregulated in a cDNA microarray experiment performed on haemocytes from immunestimulated abalone (Arendze-Bailey, unpublished). The current study sought to confirm these results by …
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Studies on the structure, function and mechanisms of the cbb3 type cytochrome c oxidase from Vibrio cholerae and the cytochrome bo3 ubiquinol oxidase from Escherichia coli
Cytochrome c oxidases (CcO) are terminal oxidases in the respiratory chain and contribute to a large fraction in the heme-copper oxidase superfamily. They are transmembrane protein complexes catalyzing the reduction of dioxygen to water with a variety range of electron donors. During the process, …
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Part I. Spin-state isomerism in crystalline (trifluoromethanesulfonato)(meso-tetraphenylporphinato)iron(III). Part II. Toward refined model compounds for the cytochrome c oxidase active site: A new picket-fence porphyrin with short imidazole pickets
… and reactivity patterns of the active site of cytochrome c oxidase. The enzyme itself contains an (Fe(porphyrin)$\cdots$Cu) binuclear active site of unknown structure. The properties which set N$\sb4$-PH$\sb2$ apart from other binucleating picket-fence porphyrin ligands previously prepared as …
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