Global ETD Search
Search theses and dissertations gathered from participating repositories worldwide. Every result links back to the library that holds it. No account is needed.
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Showing 1 to 20 of 30 for “"Hemes"”.
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Aspects of the hemes and modulation of hydrogen donors in catalases from bovine liver, yeast, and escherichia coli
… molecule. Investigation of the nature of the hemes via absorption spectroscopy of the unmodified catalase proteins and their derived pyridine hemochromes showed that while the bovine and Saccharomyces cerevisiae catalase enzymes are protoheme-containing, the HPII wild type protein contains …
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Structural and spectroscopic studies on the porin-cytochrome complex from Shewanella oneidensis MR-1
… MtrA" construct"containing" the" five"N!terminal"hemes"(MtrA"N)"were"both"observed" to"be"prolate" and"highly"extended" along"one" axis."Through" aligning"MtrA"N"with"MtrA," the"N" terminus" of" the"MtrA"structure"was"identified.""Redox"titration"experiments"were"performed"on"MtrA"as" well" as" N" …
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Biophysical investigation of electron transfer between high-potential hemes in c subunit and special pair of reaction center protein of photosynthetic bacteria Rhodopseudomonas viridis
… Two of them are high redox midpoint potential hemes (cyt-c559; Em = 380 mV and cyt-c556; Em = 310 mV) and other two are low midpoint potential hemes (cyt-c552; Em = 0 mV and cyt-c554; Em = $-$60 mV). The temperature dependence of the rate of oxidation of high potential cytochrome following …
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Structure-function relationship studies of the cytochrome bd oxidase of Escherichia coli
… and the reduction of oxygen to water (hemes $b\sb{595}$ and d) take place. Two histidines, His19 and His186, both in subunit I have been shown to affect the incorporation of the hemes as well as the activity of the oxidase. His19 is proposed to be an axial ligand to either $b\sb{595}$ …
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Molecular biology studies on thecyd operon of Escherichia coli
… is an $\alpha\beta$ hetero-dimer containing hemes $b\sb{558}$, $b\sb{595}$ and d. The cyd locus, which encodes both subunits, has been cloned and mapped genetically. The thesis research described here is focused on further characterization of the cyd gene locus and on the structure/function …
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The Study of Aa3-Type Cytochrome C Oxidase in Rhodobacter Sphaeroides
… ability and the environmental changes of the hemes were detected on the R481 mutant oxidases. The putative exit pathway is very complicated to define due to the network of many water molecules and hydrophilic residues in the area. But clearly, changing the charge status in some of the residues …
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The study of aa3-type cytochrome c oxidase in Rhodobacter sphaeroides
… ability and the environmental changes of the hemes were detected on the R481 mutant oxidases. The putative exit pathway is very complicated to define due to the network of many water molecules and hydrophilic residues in the area. But clearly, changing the charge status in some of the residues …
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Molecular genetic studies of the cytochrome o terminal oxidase complex in Escherichia coli
… the subunit compositions, the locations of the hemes, etc.
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Mutagenesis and Spectroscopic Studies on Cytochrome Bd Quinol Oxidase of Escherichia Coli
… to lose heme b595 while retaining the other two hemes---heme b558 and heme d. Since no clear role has been discovered for heme b595 in the catalytic cycle, the specific knockout of heme b595 is a significant step towards understanding its function. Characterizations of mutants on Arg391 suggest …
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The Structure-Function Interface in the Cytochrome Bc1 Complex Family
… either an iron-sulfur protein (ISP), two b-hemes (cyt b) subunit, or a c-heme (cyt c) were used to study the phylogeny of each of these polypeptides. Cyt b subunit of the bc1 complex from Rhodobacter sphaeroides was modified to introduce two distinctive features of b 6f complexes. The …
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Electron gating and mechanism of proton exit in quinol oxidation in cyt bc1 complex from R. sphaeroides
… electron transfer between the cytochrome bL hemes of the bc1 complex dimer is an essential feature of normal turnover. This functional role of the dimeric structure is suggested by the relatively short distance between the heme bL centers. Although a structural role in aligning the mobile …
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Investigation of the Interaction Between Cytochrome b(H) and the Q(i)-Site in Rhodobacter Sphaeroides
… be substantial redox cooperatively between the hemes of the complex, which is more pronounced in some of the mutants studied. The relationship between b150 and the Qi site SQ was also investigated.
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Molecular Design and Photophysical Characterization of Synthetic Bacteriochlorins for Solar Energy Conversion and Photodynamic Therapy
… e.g., chlorophylls) and porphyrins: e.g., hemes) have one and zero reduced pyrrole rings. Molecular design characteristics are revealed by understanding the effects of substituent types and patterns and the central metal ion on the photophysical properties and electronic structure. These …
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Binding Affinity of Flavins to the Dehydrogenase Domain of SpNOX
… end of the redox chain until its transfer to the hemes within the transmembrane domain. The FAD binding sites could serve as focus point in drug discovery for NOX’s. In this study, we examine the binding affinity of flavins (FAD, FMN, and riboflavin) to the DH domain of NOX.</p>
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Studies on cytochromes and electron transport in Methanosarcina thermophila strain TM-1
… protein was found to contain two hemes and had an M<sub>r</sub> of 28,000 Da. Heterodisulfide reductase was isolated from the soluble fraction by anion exchange chromatography and assayed using methyl viologen as an artificial electron donor. Electron transport from CO to the …
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Studies on the cytochrome bd-type oxygen reductase superfamily and the discovery of a novel nitric oxide reductase
… This enzyme was shown to have three hemes b instead of two hemes b and one heme d, as is typical of enzymes of this superfamily. The enzyme is highly active, using ubiquinol as substrate. This is the first example in which a member of the cytochrome bd superfamily lacking heme d has …
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Interaction between RSNO and H2S: The formation, stability, and NO-donating capacity of SSNO- and the effect of SSNO- on platelet activation
… reaction. SSNO- reacts with ferrous and ferri-hemes, but more efficiently with ferrihemoglobin (metHb). I have further demonstrated the stability of SSNO- in platelet-rich plasma, in which, the inhibition of platelet activation in platelets treated with SSNO- is comparable to those treated with …
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Magneto-optical studies of RirA and cytochrome cd1
… cd1s has allowed quantitation of the two hemes and shows that there are no populations of the FeIII-NO• product-bound active site heme.
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Purification and Characterization of the Cytochrome BC(1) Complex From Rhodobacter Sphaeroides
… that the two thermodynamically distinct $b$-hemes and cytochrome $c\sb1$ possessed spectral features and redox midpoint potentials similar to those found in chromatophores. Redox titrations of the Rieske iron-sulfur center were monitored by low-temperature EPR spectroscopy, and its midpoint …
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Magneto-optical spectroscopic studies of multi-heme enzymes
… binding to at least one of the three c-type hemes.
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