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1	Structural and functional studies on two molybdopterin and iron-sulfur containing enzymes transhydroxylase from pelobacter acidigallici and acetylene hydratase from pelobacter acetylenicus / Seiffert, Grażyna Bernadeta. January 2007 (has links) Konstanz, Univ., Diss., 2007. / Ersch. auch im Verl. Hartung-Gorre, Konstanz. ISBN 3-86628-176-5.
2	Understanding the role of anaerobic respiration in Burkholderia thailandensis and B. pseudomallei survival and virulence Andreae, Clio Alexandra Martin January 2014 (has links) Burkholderia pseudomallei is the causative agent of melioidosis, a disease endemic in Northern Australia and Southeast Asia. Melioidosis can present with acute, chronic and latent infections and can relapse several months or years after initial presentation. Currently not much is known about the ways in which B. pseudomallei can persist within the host, although it has been speculated that the ability to survive within an anaerobic environment will play some role. B. pseudomallei is able to survive anaerobically for extended periods of time but little is known about the molecular basis of anaerobic respiration in this pathogenic species. Bioinformatic analysis was used to determine the respiratory flexibility of both B. pseudomallei and B. thailandensis, identifying multiple genes required for aerobic and anaerobic respiration, and molybdopterin biosynthesis. Using B. thailandensis as a model organism a transposon mutant library was created in order to identify genes required for anaerobic respiration. From this library one transposon mutant was identified to have disrupted moeA, a gene required for the molybdopterin biosynthetic pathway. This B. thailandensis transposon mutant (CA01) was unable to respire anaerobically on nitrate, exhibiting a significant reduction in nitrate reductase activity, altered motility and biofilm formation, but did not affect virulence in Galleria mellonella. It was hypothesised that the reduction in nitrate reductase activity was contributing to the phenotypes exhibited by the B. thailandensis moeA transposon mutant. To determine whether this was true an in-frame narG deletion mutant was created in B. pseudomallei. Deletion of B. pseudomallei narG (ΔnarG) resulted in a significant reduction in nitrate reductase activity, anaerobic growth, motility and altered persister cell formation, and but did not affect virulence in G. mellonella or intracellular survival within J774A.1 murine macrophages. This study has highlighted the importance of anaerobic respiration in the survival of B. thailandensis and B. pseudomallei. 500
3	Synthese und DFT-Studien von Modellkomplexen molybdopterinhaltiger Enzyme / Synthesis and DFT studies of molybdopterin containing model complexes Starke, Kerstin 30 October 2007 (has links) No description available. 540 Chemie Mathematics and Computer Science Molybdopterin Molybdän Wolfram DFT ab initio molybdopterin molybdenum tungsten DFT ab initio 35.11 35.43
4	Structural Studies On Bovine Pancreatic Phospholipase A2 And Proteins Involved In Molybdenum Cofactor Biosynthesis Kanaujia, Shankar Prasad 10 1900 (has links) (PDF) We have carried out structural studies on bovine pancreatic phospholipase A2 (BPLA2) and two proteins involved in molybdenum cofactor (Moco) biosynthesis pathway. In addition, molecular-dynamics simulations and other analyses have been performed to corroborate the findings obtained from the crystal structures. Crystal structures of the three active-site mutants (H48N, D49N and D49K) of BPLA2 were determined to understand the mechanism by which the mutant H48N is able to catalyze the reaction of phospholipid hydrolysis and to see the effect of the loss of Ca 2+ ion in the active site of D49N and D49K mutants. We found that Asp49 could possibly play the role of a general base instead of His48 in the case of the H48N mutant. In the case of D49N and D49K mutants, the active site of the enzyme is perturbed, whereas the overall tertiary structure of these mutants is intact. In addition, a total of 24 invariant water molecules were identified in all of the crystal structures of BPLA2 available in its archive, PDB. Out of these, four water molecules are essential for the catalytic activity, whereas, the remaining water molecules play a role in the stability of the enzyme. In addition, structural studies on two proteins MoaC and MogA involved in Moco biosynthesis pathway have been carried out. For the first time, crystal structure of MoaC bound with GTP molecule has been reported. The gene id TTHA0341, which is mentioned as MoaB in the CMR database, was annotated as MogA based the comparative analysis of sequences and structures (with the present work and the structures available in the literature). The role of N-and C-termini of MoaB and MogA proteins were proposed that these residues might stabilize the substrate and/or product molecule in the active site. In addition, the residues involved in the oligomerization are compared with MD simulations. The molecular docking studies show that MoaB proteins show more preference to GTP than ATP. The comparison of the two active (MPT and AMP-binding) sites revealed that MPT-binding site is preferred over AMP-binding site for nucleotide binding. Proteins Phosphoproteins Pancreatic Phospholipase Molybdenum Biosynthesis Protein Crystallography Molecular Dynamics Simulations Molybdenum Cofactor Biosynthesis Thermus thermophilus HB8 MoaC MogA Molybdopterin Synthase Biochemistry
5	Verbindungen von Molybdän und Wolfram in den Oxidationsstufen IV - VI als Modelle für Molybdän- und Wolfram-Cofaktoren / Compounds of molybdenum and tungsten in the oxidation states IV-VI to mimic molybdenum and tungsten cofactors Döring, Alexander 11 October 2010 (has links) No description available. 540 Chemie Chemistry Elektrochemie Molybdän Wolfram Molybdopterin Cofaktoren Katalyse DFT-Rechnungen Redoxpotentiale electrochemistry molybdenum tungsten molybdopterin cofactor catalysis DFT-calculation redox potential 35.17 35.27 35.31 35.40 35.42 35.43 35.45 35.60 35.79 SHC 000: Elektrochemie STO 500: Molybdän {Anorganische Chemie} STO 550: Wolfram {Anorganische Chemie}

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