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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 26 for “"heme protein"”.
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De Novo Heme Protein Design
… way to explain this is that OR is a metalloprotein. We have found a consensus sequence ""HXXCE"" in the 4--5 loop of ORs, which not only binds strongly to Cu2+ and Zn2+, but also turns alpha helical after metal binding. Since the 4--5 loop is as hydrophobic as the fourth helix of OR, charge …
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Heme protein structure and ligand binding
Binding of carbon monoxide to a variety of heme proteins is a multistep process and can be described by a sequence of activation barriers. In the separated alpha and beta chains of hemoglobin three barriers are found which are sensitive to the structural differences between the two chains. The …
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Metalloprotein Engineering Using Heme Protein Scaffolds to Investigate the Oxidation of Endogenous Aromatic Amino Acids and Exogenous Substrates
Protein engineering by rational design has been used to study heme proteins and artificial Mn-salen containing metalloenzymes using heme protein scaffolds. Heme proteins perform a wide variety of functions including the catalysis of numerous different reactions. Some of the structural features …
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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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Long-lived states induced by extended illumination of carbonmonoxy-myoglobin
Myoglobin is a heme-protein that binds small ligands, such as O$\sb2$ and CO. A photon of visible light absorbed by the protein can break the protein ligand bond. At low temperatures ($>$160K) the kinetics of recombination of photodissociated carbonmonoxy-myoglobin are non-exponential, having …
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Identification of the Matrix Targeting and Stop Transfer Domains in the Presequence of the Mitochondrial Intermembrane Space Protein Cytochrome C Peroxidase
The presequence of CCP, an intermembrane space heme protein, has been proposed to be composed of an amino-terminal basic domain, a stretch of hydrophobic residues and a basic, carboxy-terminal domain (Kaput et al, 1982). Results from previous in vitro import experiments with a mutant ccp that was …
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Long lived states induced by extended illumination of carbonmonoxy-myoglobin
"Myoglobin is a heme-protein that binds small ligands, such as 02 and CO. A photon of visible light absorbed by the protein can break the protein ligand bond. At low temperatures (> 160K) the kinetics of recombination of photodissociated carbonmonoxymyoglobin are non-exponential, having amplitude …
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Pectoralis muscle of turkey displays divergent function as correlated with meat quality
… which include muscle fiber type composition and heme protein concentrations. These factors either contribute to or are subject to the biochemical events involved in the conversion of muscle to meat. Subtle deviations in the processing environment can also result in aberrant fresh meat quality …
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Interactions Between Heme-Globins and Ligands
Neuroglobin (Ngb) is a hexacoordinated heme protein closely related to the pentacoordinated hemoglobin (Hb) and myoglobin (Mb) and in the central and peripheral nervous systems with expression in some endocrine tissues.1–5 Ngb is believed to play roles in: sustaining ATP production under anaerobic …
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Regulatory network built by Cytochrome c with Histone Chaperones in response to DNA damage
… activation, this network is tightly regulated by protein phosphatases, such as Protein Phosphatase 2A (PP2A). Moreover, histone chaperones assist the DNA repair mechanisms altering chromatin dynamics through their nucleosome assembly activity. Recent studies have reported that the mitochondrial …
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Electron spin-lattice relaxation in proteins, model heme complexes and ferricyanide solutions at helium temperatures
… 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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Expression of Recombinant Chloroperoxidase
… the filamentous fungus Caldariomyces fumago is a heme protein with a unique structure and broad catalytic activities. In this thesis research, we report on the development of protein expression systems for chloroperoxidase. Both prokaryotic and eukaryotic expression systems were investigated. …
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Mössbauer and EPR studies of iron-containing proteins
"We have studied the iron-sulfur protein rubredoxin (Rd) and the heme protein horseradish peroxidase (HRP) using Mossbauer spectroscopy (MS) and electron paramagnetic resonance (EPR). Both methods are sensitive probes of the electronic structure of the iron at the active site of the protein. In all …
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The Physical Chemistry Underlying the Assembly and Midpoint Potential Control in a Series of Designed Protein-Maquettes
In nature, oxidoreductase proteins are responsible for many enzymatic processes critical to life. These proteins often rely on the presence of non-proteinaceous cofactors to take part in the enzymatic function. The most common, central to my thesis, is heme B. Depending on the protein environment, …
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A role for neuroglobin in the inhibition of cytochrome c-mediated apoptosome formation
… membrane and subsequent release of the heme-protein cytochrome c from mitochondria into the cytosol. Thereafter, cytosolic cytochrome c mediates the formation of the apoptosome complex, which cleaves the initiator caspase 9, thereby activating the caspase signalling cascade. Apoptosome …
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Electron spin resonance study of single crystals of cytochrome P450 from Pseudomonas putida
The magnetic properties of the ferric heme iron in single crystals of cytochrome P450 have been studied by electron spin resonance. Spectra were recorded for orthorhombic crystals (space group P222l , 114 molecules/ unit cell) of the native, substrate-free enzyme (mo),which showed a single signal …
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Characterization of cytochromes and plastocyanin in the cyanobacterium Synechocystis sp. PCC 6803
… cyanobacterium Synechocystis 6803. Two soluble proteins, the heme-protein cytochrome c553 and the copper protein plastocyanin, were isolated from this species and specific antibodies were raised to each protein. Using antibodies as probes, the reciprocal accumulation of the two proteins in …
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Investigation of photoprotection of photosystem II by cytochrome b559
… oxygen and can ultimately lead to degradation of proteins within the reaction center. Photoinhibitory reactions caused by ultraviolet B radiation (280-320 nm) are of particular concern since decreased stratospheric ozone is predicted to enhance levels of this radiation incident on the earth's …
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Rational design of functional heme copper oxidases in myoglobin
Proteins are involved in nearly every process that occurs in living systems, either as a main participant in the process or preforming a supporting role. It is estimated that approximately half of proteins in living systems are associated with a metal in some fashion. With such a high percentage of …
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