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Showing 1 to 12 of 12 for “"putidaredoxin"”.

  1. Moessbauer Studies of Putidaredoxin

    Made available in DSpace on 2015-05-12T21:41:46Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 6812098.PDF: 1077854 bytes, checksum: cfa38534f2741f0b6c0f188c4f19f324 (MD5) Previous issue date: 1968

    uiuc Repository record for Moessbauer Studies of Putidaredoxin (opens in a new tab)

  2. Mössbauer studies of putidaredoxin

    Putidaredoxin is the iron sulfide protein component of an enzyme system which hydroxylates a methylene group with O2 to form a secondary alcohol. It contains, in a molecular weight of 12,000, two atoms each of iron and acid labile sulfur. We have used the Mossbauer effect to study the symmetry of …

    uiuc Repository record for Mössbauer studies of putidaredoxin (opens in a new tab)

  3. Moessbauer Study of Reduced Putidaredoxin in Zero and Intermediate Applied Fields

    … active center of the redox and effector protein, putidaredoxin, is reported. Putidaredoxin is a prototype of a 2Fe-2S protein; it functions as an electron shuttle in a bacterial enzyme system. Several 2Fe-2S proteins, including putidaredoxin, have already been subjected to numerous Mossbauer and …

    uiuc Repository record for Moessbauer Study of Reduced Putidaredoxin in Zero and Intermediate Applied Fields (opens in a new tab)

  4. Mössbauer study of reduced putidaredoxin in zero and intermediate applied fields

    Submitted by Carolyn Mead (cmead2@illinois.edu) on 2011-06-08T18:00:38Z No. of bitstreams: 1 1983_valentine.pdf: 4470175 bytes, checksum: 271832f34e34978d84af9a04202dd08d (MD5)

    uiuc Repository record for Mössbauer study of reduced putidaredoxin in zero and intermediate applied fields (opens in a new tab)

  5. Energy Transfer and Segregation: Mixed Function Oxidation by Cytochrome P450(cam) and Putidaredoxin

    Made available in DSpace on 2014-12-10T23:24:37Z (GMT). No. of bitstreams: 1 7514136.pdf: 12157378 bytes, checksum: 1620a37478728ff7a2d6d5374a686927 (MD5) Previous issue date: 1975

    uiuc Repository record for Energy Transfer and Segregation: Mixed Function Oxidation by Cytochrome P450(cam) and Putidaredoxin (opens in a new tab)

  6. A Reduced Oxy Intermediate of Cytochrome P450(cam) Involved in Dioxygen Activation

    … camphor hydroxylation (GC), reduced putidaredoxin oxidation (EPR) were measured in parallel for the reaction of ferrous deoxy P450 and reduced putidaredoxin with dioxygen. This reaction initially formed oxy P450, which subsequently reacted with the reduced putidaredoxin. Within the …

    uiuc Repository record for A Reduced Oxy Intermediate of Cytochrome P450(cam) Involved in Dioxygen Activation (opens in a new tab)

  7. A kinetic and equilibrium description of camphor hydroxylation by the P450cam monoxygenase system

    … (2) a Fe2S*2 Cys4 iron-sulfur redoxin termed putidaredoxin (Pd) and (3) cytochrome P450cam, abbreviated cytochrome m for monoxygenase. The interaction of Pd and cytochrome m in the overall monoxygenase reaction is studied by equilibrium and kinetic techniques. Three compounds (termed …

    uiuc Repository record for A kinetic and equilibrium description of camphor hydroxylation by the P450cam monoxygenase system (opens in a new tab)

  8. Genetic Variants in the Putidaredoxin-Cytochrome P-450(cam) Electron Transfer Complex: Identification of the Residue Responsible for Redox-State Dependent Complex Stabilization

    … and a two-protein electron transfer chain, putidaredoxin and putidaredoxin reductase (Tyson et al., (1972) J Biol. Chem. 274, 5777-5784). The enzymatic removal of putidaredoxin's C-terminal tryptophan is known to cause a much reduced rate of enzymatic activity in the reconstituted camphor …

    uiuc Repository record for Genetic Variants in the Putidaredoxin-Cytochrome P-450(cam) Electron Transfer Complex: Identification of the Residue Responsible for Redox-State Dependent Complex Stabilization (opens in a new tab)

  9. Development and Integration of Bioinformatic and Electrostatic Techniques With Application to Biological Systems

    … a member from each protein family, P450 cam and Putidaredoxin. These two proteins function as an electron-transfer pair and bind using charge complementary sites on their surface. The specific binding site is unknown. Three dimensional Brownian dynamics methods were developed and applied to …

    uiuc Repository record for Development and Integration of Bioinformatic and Electrostatic Techniques With Application to Biological Systems (opens in a new tab)

  10. Sequence, Expression, and Mutagenesis of the Pseudomonas Putida Cytochrome P450(cam) Gene in Escherichia Coli

    … flanking sequence. The gene encoding putidaredoxin reductase, camA, was located 22 nucleotides downstream from the camC gene. The camA gene initiated with a novel GUG codon, the first such initiator documented in Pseudomonas.

    uiuc Repository record for Sequence, Expression, and Mutagenesis of the Pseudomonas Putida Cytochrome P450(cam) Gene in Escherichia Coli (opens in a new tab)

  11. Macromolecular recognition in the cytochrome P450(cam) enzyme system

    … this reaction are supplied physiologically by putidaredoxin, a Fe$\sb2$S$\sb2$ iron-sulfur protein. The mammalian cytochromes P-450 are also known to interact with cytochrome b$\sb5$, a small redox protein for which a high resolution crystal structure is available. To characterize the molecular …

    uiuc Repository record for Macromolecular recognition in the cytochrome P450(cam) enzyme system (opens in a new tab)

  12. Bioorganic activation of cytochrome P-450cam

    … center of P-450cam's electron transport partner, putidaredoxin (Pdx), is determined using a combination of site-directed mutagenesis and EPR spectroscopy. The identity of the rapidly reacting cysteine in P-450cam, which has been used as an attachment site for probes of Pdx-P450cam interaction, is …

    uiuc Repository record for Bioorganic activation of cytochrome P-450cam (opens in a new tab)