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Showing 1 to 9 of 9 for “"Copper proteins"”.
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Dynamics of blue copper proteins
Studies of small molecules binding to heme proteins have yielded a large amount of information about protein dynamics and conformational substates (CS) in proteins. However, heme proteins are very similar in their active site structures, and relatively little work exists on non-heme proteins which …
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Structure/function relationships of the copper proteins nitrite reductase and rusticyanin
… the structure/function relationships of two copper proteins, nitrite reductase and rusticyanin using a combined approach of site-directed mutagenesis and X-ray crystallography. Dissimilatory nitrite reductase (NiR) catalyses the reduction of nitrite to nitric oxide (NO) as part of the key …
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The role of copper proteins in the ammonia oxidation pathway of Nitrosopumilus maritimus
… oxidising pathways relying predominantly on proteins utilising haem c active sites. However, homologues for these proteins (or indeed genes for any proteins containing the characteristic haem c CXXCH motif) are absent in AOA, suggesting a completely different pathway in AOA. Novel …
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Electron spin-lattice relaxation in two heme iron and two blue-copper proteins at liquid helium temperatures
… temperature dependence of the Raman rates in proteins are shown to be insufficient, including two fractal models. In addition, it is shown that any model based exclusively on the protein structure fails due to the diversity of the data under various solvent conditions. A general functional …
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Structural characterization of the two copper proteins nitrous oxide reductase from Pseudomonas stutzeri and laccase Lcc5 from Coprinopsis cinerea
Obwohl die Reduktion von Distickstoffoxid (N2O) stark exergonisch ist, verhindert eine hohe Aktivierungsenergie eine spontane Reaktion. Wie Distickstoff benötigt N2O ein komplexes Metallzentrum, um aktiviert zu werden. Das einzige bekannte Enzym, welches die Reduktion von N2O zu N2 katalysieren …
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Expanding the metallomics toolbox: Development of chemical and biological methods in understanding copper biochemistry
Copper is an essential trace element and required for various biological processes, but free copper is toxic. Therefore, copper is tightly regulated in living cells and disruptions in this homeostatic machinery are implicated in numerous diseases. The current understanding of copper homeostasis is …
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Electron spin-lattice relaxation in proteins, model heme complexes and ferricyanide solutions at helium temperatures
… are reported for frozen solutions of the blue-copper proteins azurin and plastocyanin, the low-spin iron heme protein cytochrome-c, two (bis)imidazole ferric heme complexes in three different organic solvents and two ferricyanide solutions. Measurements were performed at X-band frequencies and …
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Fine���tuning the reduction potential of Cupredoxin proteins by altering secondary coordination sphere interactions
… and Em seen in natural ET catalysts, these proteins utilize only a limited number of redox active cofactors. Of metal based redox cofactors, the entirety of the required Em range is covered by Fe‐S clusters, heme, non‐heme iron, copper, manganese and molybdenum ions. Many of these cofactors …
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Metalloprotein engineering with unnatural amino acids: application in functional heme-copper oxidase and azurin
Metalloproteins, proteins with metal ion cofactors, are estimated to make up more than a third of total proteome. They involve in key biological processes such as photosynthesis, respiration, and nitrogen fixation. The important roles and potential applications of metalloprotein urges the need for …