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Showing 1 to 16 of 16 for “"cytochrome c peroxidase"”.
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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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Cytochrome c peroxidase : its role in nitrosative stress and purification as a GST-fusion protein
Cytochrome c Peroxidase (CCP) is a hemoprotein found in the intermembrane space of yeast mitochondria. One of its roles is to protect the cell against oxidative stress by reducing mitochondrial H 2 O 2 to H 2 O. Titration of CCP with peroxynitrite [ONOO(H)] formed a species with an absorption …
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Encapsulation of Achiral Mn(Salen) Complexes Into Cytochrome C Peroxidase: Spectroscopic Characterizations and Epoxidation Studies
The powerfulness and potential of this strategy have been successfully demonstrated. Other achiral catalytic metal complexes can also be incorporated into CcP or other protein scaffolds to produce a library of biocatalysts to perform various organic transformations.
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The effects of elevated mitochondrial hydrogen peroxide in S. cerevisiae : a physiological role for cytochrome c peroxidase
The role of cytochrome c peroxidase (CCP), found in yeasts and some bacteria, is not clear. However, it is believed to play a role in H 2 O 2 detoxification. To probe the physiological role of CCP, a yeast strain deficient in the gene encoding CCP (x ccp1 ) was engineered and characterized with …
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Complex, non-native heteronuclear metal centers designed in cytochrome c peroxidase: Expanding the limits of biosynthetic modeling
Made available in DSpace on 2019-02-07T20:44:07Z (GMT). No. of bitstreams: 19 MIRTS-DISSERTATION-2018.pdf: 9903869 bytes, checksum: fe284a4efb732c6dc2261e44d5f1f1dc (MD5) 1-Rightslink by Copyright Clearance Center.pdf: 98582 bytes, checksum: 7d88fb171a37ad188eaccd5c88b44354 (MD5) 10-RightsLink …
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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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Part I. The Synthesis of Hyaluronan Oligosaccharides and the Mild Cleavage of 2-Amino-2-Deoxy-D-Glucoside Methoxycarbonyl Derivatives With Methytrichlorosilane. Part II. The Design and Engineering of a Manganese Binding Site in Cytochrome C Peroxidase
Part II. A manganese binding site has been creating in CcP corresponding to the Mn-binding domain in MnP by site directed mutagenesis. Several spectroscopic techniques including paramagnetic NMR and EPR were employed to characterize the CcP mutant (MnCcP). The data is consistent with a newly formed …
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Design and Synthesis of Redox or Catalytically Active Artificial Metalloproteins Containing Non-Native Inorganic and Organometallic Complexes
… salen (Mn(Salen)) to the active sites of cytochrome c peroxidase (CcP) and sperm whale myoglobin (Mb) using cysteine residues. The new metalloproteins were characterized by UV-Vis, CD, electrospray mass spectroscopy and cyclic voltammetry. Together with chemical reactivity studies, these …
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Transcriptomics-Guided Biodiscovery of Peroxidases from Macroalgae
Peroxidases are versatile enzymes with applications in laboratory analytics and industrial processes. Despite their relevance, many applications rely on a few well-characterized terrestrial enzymes, particularly horseradish peroxidase (HRP), whose complex post-translational modifications hinder …
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Metalloprotein Engineering Using Heme Protein Scaffolds to Investigate the Oxidation of Endogenous Aromatic Amino Acids and Exogenous Substrates
… thesis. Heme protein models have been made of peroxidases and P450 to gain insight into the native function of these enzymes. The role of role of redox active amino acids in heme proteins was studied by mutating Trp an Tyr residues in cytochrome c peroxidase (CcP). Sequential mutation of these …
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INTRA-MITOCHONDRIAL INJURY DURING ISCHEMIA-REPERFUSION
… project identifies a novel pathological role of cytochrome c in depleting cardiolipin during ischemia after which the mitochondria are in a defective condition that leads to additional cell death during reperfusion. During ischemia oxidants from complex III oxidize cytochrome c, forming a …
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Delineation of the active site structure of chloroperoxidase from C. fumago
Chloroperoxidase, a heme-containing glycoprotein from Caldariomyces fumago, is secreted in prodigious amounts in the presence of fructose. Production of 90% pure, mycelium-free enzyme for 200 days from a single inoculum was facilitated by continuous and semi-continuous bioreactors designed and …
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Aspects of the hemes and modulation of hydrogen donors in catalases from bovine liver, yeast, and escherichia coli
… Escherichia coli contains two catalases. Hydroperoxidase I (HPI) is a bifunctional catalase-peroxidase. Hydroperoxidase II (HPII) is only catalytically active toward H202. Expression of the genes encoding these proteins is controlled by different regimes. HPJI is thought to be a hexamer, having …
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Isolating, characterizing, and engineering novel Cu-proteins and peroxidases
… functionalities in one of our model scaffolds, cytochrome c peroxidase (CcP). Chapter 7 describes the work done to enhance the Mn(II) oxidation activity in a designed model of manganese peroxidase within the CcP scaffold based on modifications of the second coordination sphere around the Mn(II) …
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Bioremediation of hexavalent chromium using gram-negative bacteria.
… or otherwise removing Cr (VI). The di-heme cytochrome c peroxidase is also a possible candidate enzyme of reducing chromium (VI), since it is known to be present in the periplasm and to play a role in reducing peroxides generated by oxidative metabolism.Inductively coupled plasma mass …
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Oxidative stress in anoxic habitats
Oxygen and its reactive species —hydrogen peroxide (H2O2), superoxide (O2-) and hydroxyl radicals (HO•)— can cause a plethora of damages in the cell, from DNA damage to inactivation of iron containing enzymes. Virtually all life forms experience oxidative stress to some degree, and they are all …