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 308 for “"cytochrome c"”.
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Cytochrome c-DNA and cytochrome c-enzyme interactions for the construction of analytical signal chains
… approaches, the redox properties of the protein cytochrome c (cyt c), which acts as an electron shuttle in the respiratory chain, was utilized to engineer ET chains on electrode surfaces. With the help of the biopolymer DNA, the redox protein assembles into electro active multilayer (ML) systems, …
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Semisynthetic cytochrome c site-67 substitutions
Highly conserved tyrosine-67 of mitochondrial cytochrome $c$ is thought to be involved in important hydrogen bonding interactions in the hydrophobic heme pocket of the protein. In order to investigate the hydrogen bonding role of this residue, two site-67 analogs were prepared by semisynthetic …
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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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Probing the redox-active residues in cytochrome c peroxidase
The reaction of cytochrome c peroxidase (CCP) with H 2 O 2 results in compound I formation, where the two oxidizing equivalents of H 2 O 2 are stored as an oxyferryl heme and a Trp191 radical. Ferrocytochrome c normally reduces compound I back to the resting enzyme, but in the absence of exogenous …
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Long-range electron transfer in cobalt-labeled cytochrome c
… to various sites on the surface of horse heart cytochrome c. In this way, a second redox site, in addition to the heme, was introduced. Labelling of the protein at several surface sites, allowed several donor/acceptor distances to be evaluated within the same protein system.
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The extraction of Cytochrome C and DsRed2 into reverse micelles
Cytochrome c and DsRed2 were successfully extracted into reverse micelles by the contacting of an aqueous protein-containing phase with an organic phase. Two important properties that differentiate the extraction profiles of these proteins are pI and size. Cytochrome c is a relatively small, …
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Thermodynamics and Kinetics of Iso-1-cytochrome c Denatured State
… simple loops in the denatured state using c-type cytochromes. New insights into how the properties of these loops impact the denatured state are outlined in this thesis. First, studies on a 22-residue loop revealed a previously unreported finding that equilibrium loop formation was not strongly …
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Conformationally gated electron transfer studies of iso-1-cytochrome c
… funnel. Histidine-heme alkaline conformers of cytochrome <italic>c</italic> are used as a model for a late folding intermediate or partially unfolded state that can be exploited to study roughness near the bottom of a folding funnel.<p> In my thesis work, I have developed a novel method using …
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Thermodynamics and Kinetics of Iso-1-cytochrome c Denatured State
… simple loops in the denatured state using c-type cytochromes. New insights into how the properties of these loops impact the denatured state are outlined in this thesis. First, studies on a 22-residue loop revealed a previously unreported finding that equilibrium loop formation was not strongly …
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Conformationally gated electron transfer studies of iso-1-cytochrome c
… funnel. Histidine-heme alkaline conformers of cytochrome <italic>c</italic> are used as a model for a late folding intermediate or partially unfolded state that can be exploited to study roughness near the bottom of a folding funnel.<p> In my thesis work, I have developed a novel method using …
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Structural constraints for the folding, stability and function of cytochrome C
… and function in yeast (Saccharomyces cerevisiae) cytochrome c was studied through the investigation of mutant proteins. Two isozymes of cyto-chrome c can be isolated from yeast, iso-1 and iso-2-cytochrome c. The structure of iso-l-cyto-chrome c had been previously determined in this laboratory …
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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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Studies of Cytochrome C Oxidases From Rhodobacter Sphaeroides and Vibrio Cholerae
Cytochrome c oxidase is the terminal enzyme to accept electrons from cytochrome c in the respiratory chain of mitochondria, bacteria and archaea. It couples the reducing oxygen to water and pumping the protons across the membrane. The second largest group, C-type, is also known as cbb3 cytochrome c …
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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 of cytochrome c oxidases from Rhodobacter sphaeroides and Vibrio cholerae
Cytochrome c oxidase is the terminal enzyme to accept electrons from cytochrome c in the respiratory chain of mitochondria, bacteria and archaea. It couples the reducing oxygen to water and pumping the protons across the membrane. The second largest group, C-type, is also known as cbb3 cytochrome c …
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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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