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.
Results
Showing 1 to 20 of 942 for “"Cytochrome"”.
-
Human Cytochrome P450 2E1: Functional Comparison to Cytochrome 2A13 and 2A6
The cytochrome P450 (CYP) superfamily of enzymes plays the predominant role in human phase I xenobiotic metabolism. The CYP2 family, in particular, is known for it extensive Phase I metabolism of a majority of the xenobiotic compounds [1]. The goal of this project is to determine the structural …
-
The role of electrostatics in macromolecular associations: The cytochrome b(5)-cytochrome c complex
… interactions, including the association between cytochrome b$\sb5$ and cytochrome c. The dependence of stability of the association between cytochrome b$\sb5$ and cytochrome c on ionic strength and pH conditions is indicative of the charge-charge interactions in the interfacial domain.
-
Characterization of Maize Cytochrome P450s
Messenger RNAs encoded by other maize P450 clones (CYP71C1, CYP51, CYP73A7, CYP73A6, CYP92A1, CYP95A1, and the ESTs 6c06b11 and 7c02c12) were also characterized with regard to their induction response to naphthalic anhydride and triasulfuron treatment. In addition, maize seedlings were also …
-
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, …
-
Characterization of Monomeric Human Cytochrome P450 3A4 and Cytochrome P450 Reductase in Nanoscale Phospholipid Bilayer Discs
… either CYP3A4 or CYP3A4 and its redox partner, cytochrome P450 reductase, as a coincorporated complex are described and further characterized for substrate binding, rates of dithionite dependent reduction, NADPH utilization rates, and testosterone metabolic rates as a function of substrate …
-
Exploring the Function of Cytochrome c6A
The electron transfer protein cytochrome c6 (c6) of photosynthesis was believed to have been lost in plants until a ubiquitous and highly conserved homologue, named cytochrome c6A (c6A), was identified. Soon after its discovery, c6A was shown to be unable to replace c6 (or plastocyanin) …
-
Crystalline Cytochrome B1 From Escherichia Coli
Made available in DSpace on 2014-12-09T17:34:53Z (GMT). No. of bitstreams: 1 6408372.pdf: 4879635 bytes, checksum: 1adaafe1b90c03b17de7b22e97b56c0f (MD5) Previous issue date: 1964
-
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 …
-
Bioorganic activation of cytochrome P-450cam
The Cytochrome P-450 class of monoxygenases carry out a wide variety of hydroxylation, epoxidation and heteroatom oxidation reactions. The cytochrome P-450cam enzyme from P. putida has been widely studied as a model for other P-450s due to the availability of a high resolution X-ray crystal …
-
Structure and Function Relationships in Cytochrome Bo(3) Oxidase and Cytochrome Bd-I Oxidase From Escherichia Coli
… in Escherichia coli have been investigated. Cytochrome bo3 oxidase, a member of the heme/copper superfamily, is found to have a semiquinone intermediate during turnover of quinol. Additionally, after the quinol is consumed and turnover stops, the enzyme is found in a mixture of oxidation …
-
STRUCTURE REFINEMENT OF CYTOCHROME C555 (CHLOROBIUM, THIOSULFATOPHILUM).
The structure of cytochrome c₅₅₅ from the green sulfur bacterium Chlorobium thiosulfatophilum was determined by using a single isomorphous derivative, K₂HgI₄, in combination with its anomalous signal. The initial 2.25 angstrom map was modified by the technique of Fourier inversion. The smoothing …
-
A Thermostable Cytochrome P450 From Sulfolobus Solfataricus
… involved in electron transfer to the P450 cytochromes. The crystal structures of CYP119 indicate that increased stability may be due to a combination of increased factors involved in stabilizing secondary and tertiary structural interactions, such as aromatic stacking, increased salt link …
-
Enzymatic activation of cytochrome P-450(cam)
Cytochrome P-450$\sb{\rm cam}$, a camphor monoxygenase from Pseudomonas putida, has served as a model system for the entire family of the P-450s in exploring structure-function relationships, molecular recognition, substrate specificity, and oxygen activation. There are several universal features …
-
Catalytic site mutagenesis of cytochrome P450 6B1v1
Cytochromes P-450 form a large superfamily of heme-containing monooxygenases that are found in species ranging from bacteria to insects, plants, and mammals. In insects, P-450s have several functional roles, including growth, development, feeding, resistance to pesticides, and tolerance to plant …
-
The Ancestry and Function of Cytochrome c6A
Cytochrome c6A is a homologue of cytochrome c6 found in eukaryotic green algae and higher plants. However it is thought to perform a different function from cytochrome c6. Two current hypotheses exist for this function: that cytochrome c6A acts as a ‘safety valve’, providing an alternative path for …
-
Cytochrome P450 whole cell biohydroxylation of alkanes
… pathways to produce value added chemicals. Cytochrome P450 (CYP) monooxygenases such as CYP153A6 have previously shown excellent 95% selectivity for hydroxylation at the terminal carbon on n-octane and CYP153A13 has shown promising activity on n-octane and n-decane. In the present study, …
-
Effect of citrate on the redox properties of cytochrome C and its kinetic and binding behaviour with cytochrome oxidase /
… ionic strength (30 mM) decreases the rate of cytochrome ~ reduction by ascorbate. This effect is also seen at both high (600 mM) and low (19 mM) ionic strengths, and the Kapp for citrate increases with increasing ionic strength. Citrate binds d both ferri -and ferrocytochrome ~, but with a …
Page 1 of 48