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 11 of 11 for “"Redox cofactor"”.
-
Mechanistic Insights into MftR-Dependent Regulation of the Redox Cofactor Mycofactocin
<p>Organic redox cofactors are essential for life. While classic flavins and nicotinamides are widely distributed across all domains of life, nature has also evolved niche cofactors in subsets of life domains. For example, in <em>Actinobacteria</em>, coenzyme F420 is commonly used in place of …
-
Biochemical Studies of the Sodium -Translocating NADH:ubiquinone Oxidoreductase
… to be essential to the binding of the FAD cofactor. By mutagenesis and spectroscopic characterization, the four conserved cysteines are confirmed to be the ligands for the 2Fe-2S center, and R210, Y212, S245 are confirmed to be important for the binding of the FAD cofactor in Na +-NQR. …
-
Development Towards an Ethylene Sensing Artificial Metalloenzyme
… peptide (RiPP) hypothesized to function as a redox cofactor in bacteria, particularly the Mycobacteria genus, which includes M. tuberculosis. In order to further elucidate the function of MFT and its associated proteins, a synthetic route was desired to the small molecule. A viable synthetic …
-
Control of Cellular Redox State and Biomass Synthesis
… undergo oxidation reactions that require the redox cofactor NAD+ as an electron acceptor. Thus, the cellular redox state, measured by the NAD+/NADH ratio, can constrain the synthesis of oxidized biomass. This dissertation aims to uncover the determinants of the cellular NAD+/NADH ratio and how …
-
Sensitivity of Radical SAM Enzyme MftC to Molecular Oxygen
… synthesized post-translationally modified (RiPP) redox cofactor shown to be essential for the survival of bacteria in the <em>Mycobacterium</em> genus in the presence of cholesterol as a carbon source and for the sequestration of ethanol. MftC catalyzes the C – terminal decarboxylation of tyrosine …
-
Structural Studies of Catalysis and Processing in Galactose
… earliest examples of a protein derived radical cofactor. A covalent bond, formed between the active site cysteine and the Cc of a tyrosine act as a site for radical formation, allowing the enzyme to catalyse the two electron oxidation of primary alcohols to their corresponding aldehydes, with …
-
NAD+ salvage by Nicotinamide phosphoribosyltransferase (Nampt) mediates lipogenesis, energy homeostasis, and survival in prostate cancer
… (NAD<super>+</super>) is recognized as a redox cofactor which participates in numerous metabolic reactions. However, new evidence shows that many enzymes consume NAD+ as a substrate to regulate activities from posttranslational modifications to DNA repair and apoptosis. The rate-limiting …
-
New Insights into Mycofactocin Biosynthesis, Structure and Function
… modified peptide (RiPP)-derived redox cofactor. Its biosynthesis is accomplished through the dedicated actions of the products of six conserved genes, <em>mftABCDEF</em>. The mycofactocin pathway is one of the most widely distributed RiPP systems in bacteria however, this …
-
Yeast engineering for pharmaceutical and nutraceutical purposes
… a key role in cytosolic acetyl-CoA synthesis and redox balance of Saccharomyces, new metabolic engineering approaches not to knock out its ethanol pathway but to minimize the overflow metabolism are needed for increasing productivities of acetyl-CoA derivatives, growth-dependent metabolites, and …
-
Metalloenzymes required for glycan processing and morphological development in Streptomyces lividans
… with a mononuclear Cu site and possess a Cys-Tyr redox cofactor capable of housing a protein radical, comparable to the fungal galactose oxidase (Gox). The tertiary structure of GlxA revealed a unique domain arrangement, atypical spectroscopic properties compared to Gox and a lack of enzymatic …
-
Long-range extracellular electron transport by dissimilatory metal-reducing bacteria across a physical separation
… as a diffusible electron shuttle, but as a bound redox cofactor. The high binding affinity of riboflavin reported for outer membrane c-type cytochromes (c-Cyts) suggests that riboflavin was bound to OmcS, a c-Cyt that decorates the nanowire surface. Upon addition of a soluble electron shuttle …