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Showing 1 to 11 of 11 for “"heme copper oxidase"”.
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Understanding structure-function relations in heme-copper oxidase using myoglobin-based enzyme models
Heme-copper oxygen reductases (HCOs) are respiratory enzymes that utilize a heme-copper center to perform the four-electron reduction of oxygen to water. The HCOs share significant structural and sequence homology to another class of metalloenzyme, nitric oxide reductase (NOR), that in turn, …
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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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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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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 …
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EPR and solid-state NMR studies on the mechanism of cytochrome bo3 ubiquinol oxidase from escherichia coli
Cytochrome bo3 ubiquinol oxidase from E. coli is a member of heme-copper oxidase superfamily. This trans-membrane enzyme complex catalyzes two-electron oxidation of ubiquinol and reduction of molecular oxygen to water. During the process, the protons from ubiquinol are released to the periplasmic …
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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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Studies on the cytochrome bd-type oxygen reductase superfamily and the discovery of a novel nitric oxide reductase
… the bd-type oxygen reductase superfamily and the heme-copper oxidoreductase superfamily. The bd-type oxygen reductases are present in bacteria and archaea and catalyze the 4-electron reduction of oxygen to water. Electrons from membrane bound quinols first reduce a low spin heme b from which they …
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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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Engineering an oxygen storage metalloprotein into carbon dioxide and oxygen reduction metalloenzymes
Made available in DSpace on 2021-09-17T04:03:56Z (GMT). No. of bitstreams: 4 DWARAKNATH-DISSERTATION-2021.pdf: 5841120 bytes, checksum: ce2ff36f34d268a44ae248b23c61d93f (MD5) Dissertation Master Document_SD3.doc: 122368 bytes, checksum: 4309f4f0e2e18bdcfb871a2e77a38be9 (MD5) LICENSE.txt: 4217 …
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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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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. …