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Showing 1 to 20 of 108 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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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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ΑΝΑΛΥΣΗ ΤΩΝ ΑΛΛΗΛΕΠΙΔΡΑΣΕΩΝ ΑΝΘΡΑΚΥΚΛΙΝΩΝ-ΣΙΔΗΡΟΠΟΡΦΥΡΙΝΩΝ ΣΤΟ ΑΙΜΟΠΟΙΗΤΙΚΟ ΣΥΣΤΗΜΑ
… COMPLEXES. THESE COMPONENTS ARE ENRICHED IN CYTOCHROME C OXIDASE. DETAILED ANALYSIS OF HOW CYTOCHROME C OXIDASE INTERACTS WITH [3H(G)]-DAU INDICATES THAT [3H(G)]-DAU PREFERENTIALLY INTERACTS WITH PEPTIDES CARRYING HEME AS PROSTHETIC GROUPS AND LESS SELECTIVELY WITH CARDIOLIPIN, A PHOSPHOLIPID …
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