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Showing 1 to 14 of 14 for “"Heme Copper Oxidases"”.
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Examining the Proton Channels in Heme -Copper Oxidases
Previous work on the mutant enzyme KI-362M indicated that a block in the K-channel would result in the blockage of the catalytic cycle between the oxidized state and the two electron reduced state. This blockage occurs because an electron cannot enter the binuclear center without a proton to …
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Rational design of functional heme copper oxidases in myoglobin
… uses relatively few metal complexes, such as heme cofactors or iron sulfur clusters or metal ions, considering the number of functions that metalloproteins perform. Also, nature uses a surprisingly small number of protein domains and folds compared the number of possible folds. In …
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Biochemical characterization of a-type heme-copper oxidases in escherichia coli, bacillus subtilis and thermus thermophilus
Heme-copper oxidases (HCOs) couple the free energy of oxygen reduction and translocate protons across membrane to generate a proton electrochemical gradient, which was used to produce ATP by ATP synthase. Based on the sequences and structures of core subunits, they are classified into 3 types. …
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Exploring the Roles of Heme Type and Histidine -Tyrosine Cross -Link in Heme-Copper Oxidases Using a Myoglobin Model
… the CuBMb model in this study: (1) synthetic heme cofactors are used to replace the natural one of the protein, resulting in ∼20 fold inhibition of the side reaction; (2) a novel semi-synthetic system (Expressed Protein Ligation) is also established that may introduce new features such as …
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Exploring the Structure-Function Relationships and Dynamics of the Heme/copper Oxidase Superfamily Using Cytochrome Bo(3) From Escherichia Coli as a Model System
Finally, the first study of the heme/copper oxidases by attenuated total reflectance (ATR) FTIR is presented, and preliminary results are shown, which demonstrate that cytochrome bo3 can be constituted into stable thin films, suitable for ATR-FTIR work.
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Using myoglobin models of oxidases for mechanistic understanding of the oxygen reduction reaction
… reaction to take place in metalloenzymes like oxidases, but strangely, there is a high degree of variance in the active site of these enzymes. Studying the native enzymes has proven difficult using traditional methods due to the insoluble nature of oxidases along with many complicating features …
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Engineering the interface of cytochrome b5 and myoglobin for in vitro and in vivo applications
Heme-copper oxidases (HCOs) are large membrane proteins found in both bacteria and in eukaryotes. They catalyze about 90% of oxygen reduction in the atmosphere. They utilize a heme-copper center, which is comprised of a heme and a copper ion coordinated with three histidines, to catalyze the …
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Metalloprotein engineering with unnatural amino acids: application in functional heme-copper oxidase and azurin
… all have their own advantages and disadvantages. Heme copper oxidases (HCOs) catalyzes reduction of O2 to H2O and harvest energy at the end of respiration chain. The enzyme plays a pivotal role in aerobic respiration and thus is important for life on earth. The oxygen reduction reaction is …
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Characterization of the quinol nitric oxide reductase from Peresephonella marina
qNOR is a nitric oxide reductase in the heme-copper oxidoreductase superfamily that catalyzes the two electron reduction of NO to N2O using electrons derived from quinol. In this study, we heterologously expressed and characterized the qNOR from the thermophilic, denitrifying bacteria Persephonella …
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Studies on Critical Proton Pathway Residues in the Aa3-Type Cytochrome C Oxidase From Rhodobacter Sphaeroides
… cross-link found at the active site of all heme-copper oxidases. We have also speculated on the radical chemistry at the active site that may have lead to its formation.
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Studies on critical proton-pathway residues in the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides
… cross-link found at the active site of all heme-copper oxidases. We have also speculated on the radical chemistry at the active site that may have lead to its formation.
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Characterizing a structural and functional model of nitric oxide reductase performing NO and O2 reduction in engineered myoglobin
… structurally homologous to subunit I of HCOs (heme-copper oxidases); however, the copper site (CuB) in HCOs is replaced with a non-heme iron site (FeB) in NOR, and each metal contains a different primary and secondary coordination sphere.1 NOR and HCO also have cross-reactivity, though they are …
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Characterization and design of hydrogen bonding interactions in oxygen reduction by engineered myoglobins
… Moreover, many of these systems, such as the oxidases and photosystems responsible for respiration and photosynthesis, respectively, are large, difficult to purify, and contain multiple cofactors that complicate investigations of the active site chemistry. Therefore, in the Lu lab, we have …
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Engineering heme-copper and multi-copper oxidases for efficient oxygen reduction catalysis
… this goal, my thesis focuses on mimicking the heme-copper oxidase and engineering a multi-copper oxidase for efficient oxygen reduction with high turnover frequency and low overpotential Heme-copper oxidases catalyze four-electron reduction of oxygen to water, and the energy harvested is …