Summer Science Research at Bryn Mawr

'Burgmayer, Dr. Sharon' Archive

Synthesis and Characterization of Pterin-Based Molybdenum Cofactor

Posted July 28, 2011

Abstract: Suyin Lee Mentor: Dr. Sharon Burgmayer Molybdenum is an essential transition element that forms a catalytic center of enzymes such as nitrogenase, nitrate reductases, sulfite oxidase and xanthine oxidoreductases. Some of these enzymes play important roles in carbon, nitrogen and sulfur cycles in the ecosystem while others are essential for proper human neurological development. […]

Summer Research Abstract: Molybdenum Pterin Dithiolene Chemistry

Posted July 26, 2011

Abstract: Yichun Fu Mentor: Dr. Sharon Burgmayer The pterin dithiolene ligand plays an important role in the biochemical functions of the molybdenum cofactor due to its ability to transfer electrons and store charges. The pterin-dithiolene molybdenum complex, has various redox paths that contribute to its multiple functions for the enzyme. Studying the forms and interchange […]

Synthesis and Characterization of Molybdenum Tetrasulfide Complexes and Pterinyl Alkyne

Posted July 26, 2011

Abstract: Suyin Lee Mentor: Dr. Sharon Burgmayer The molybdenum co-factor (Moco) forms the active site of redox reactions in all eukaryotic molybdenum enzymes such as nitrogenase, nitrate reductases, sulfite oxidase and zanthin oxidoreductases. Two different systems, molybdopterin (Figure 1) and iron-molybdenum co-factor have been found to control redox and catalytic functions of molybdenum which serves […]

Exploration into Potential Anti-Tumor Properties of Ruthenium (II) Tris-Chelate Complexes

Posted July 26, 2011

Abstract: Meredith Skiba Mentor: Sharon Burgmayer Following the success of the chemotherapeutic drug cisplatin, there is an increased curiosity regarding the effects of other transition metal complexes on normal cellular structures and functions. Complexes with the ability to distort and cleave DNA are of particular interest as they may inhibit the activity of DNA replication enzymes, […]

The Pathway to BMOPP

Posted July 10, 2011

Abstract: Hannah Gilbert Mentor: Dr. Sharon Burgmayer This research will deal mainly with pterin chemistry in relation to the molybdenum cofactor in molybdenum-containing enzymes. As molybdenum enzymes are required within every living organism and as there is little study in the field of molybdopterin chemistry, it is very relevant to investigate the character of molybdenum […]

Molybdenum Cofactor

Posted June 24, 2010

The objective of this research is to improve the efficacy of the molybdenum dithiolene complex synthesis. Using collective methodologies from previous research projects of the Burgmayer group members, including several procedures pioneered by Kelly Matz, this research focuses on a larger-scaled reproduction of the synthesis and the convergence of [Et4N]+[Tp*Mo+4(S)S4]-, the tetrasulfide, and BMOPP, a dimethylated, pterinyl alkyne, in hopes of products with better purity and higher yields. In addition, several experiments with other pterinyl alkyne reagents will be carried out with the objective of shielding and protecting the sulfurs in the molybdenum dithiolene complexes produced.

Synthesizing and Modeling the Molybdenum Cofactor

Posted June 24, 2010

Molybdenum is a 4d transition metal. It has crucial biological functions in many enzymes. Despite the differences among the Mo-containing enzymes, they all have a Molybdenum cofactor named as Moco, which promotes the catalytic activities of an enzyme. The Moco utilizes a dithiolene ligand, Molybdopterin. The Burgmayer group conducted successful research to synthesize Molybdopterin via two pathways, using tetrasulfide and pterinyl alkynes.

The effect of Ruthenium (II) tris-chelate compounds on DNA

Posted June 23, 2010

In order to stop tumor growth, replication enzymes responsible for the increase in cells can be inhibited. Several transition metal compounds may inhibit these enzymes’ activity through their ability to intercalate and photocleave. Intercalation occurs when a molecule slides in between the base pairs of a DNA molecule distorting DNA’s helical shape. This change in shape prevents the replication enzyme from properly interacting with the DNA and thus prevents cell growth. Similarly, photocleavage of DNA further inhibits DNA replication by breaking and uncoiling DNA after UV light exposure. The mechanism by which photocleavage occurs is unclear. However, it is believed that reactive oxygen species may play a role.

The Photoclevage Abilities of Ru Compounds

Posted June 22, 2010

In the Burgmayer lab, a family of ruthenium (II) tris-chelate compounds are synthesized and examined for their potential anticancer pharmaceutical properties. Ruthenium compounds are thought to distort the helical shape of DNA which can potentially inhibit the excess replication of tumor cells. In many cases, the insertion of a Ru compound between DNA base pair steps in the DNA helix distorts the shape.

Synthesis of Bis(bpy)-Ru-L-Pteridine

Posted June 22, 2010

I will attempt to create and isolate the unsubstituted pteridine ligand complex and determine its ability to intercalate and photocleave.

Next Page »