Research Interests

 

In our research lab, we are focusing on redox enzymes that involve electron transfer. APS reductase is a key enzyme in the sulfate assimilation pathways found in bacteria, archaea, fungi, and plants. We are attempting to elucidate the mechanism of APS reductases using a bacteria expression system. We are studying electron transfer in APS reductases and looking at the dithiol/disulfide couple and cofactors in the mechanism.

In addition of APS reductases, we are working on arsenate reductases and their electron donor glutaredoxins.

X-ray structure of a gluatredoxin from Synechocystis

Arsenate reductases lie in the center of the protection defense against arsenic toxicity in many cells. The understanding of the arsenate reductases mechanism may pave a way to design a transgenic plant that may remove arsenic contamination in rural environments.

Another project that we are investigating is the discovery of possible drugs or detecting materials using SELEX (Systematic Evolution of Ligands by Exponential enrichment), an in vitro selection technique that allows screening for a particular functionality, such as the binding to proteins. Functional molecules, called aptamers, that are suitable for the enrichment of any desired property are selected from a large, random pool of RNA or DNA (the great majority of pool members are non-functional) by selection techniques. The immense complexity of the generated pool justifies the assumption that there may be a few molecules with secondary and/or tertiary structures that will allow tight and highly specific binding to target molecules, resulting in inhibition of the enzymatic activity (metallo-beta-lactamases – for more information, click Chemical Additive to Antibiotics Could Make Them Newly Effective Against Resistant Bacteria) or development of detecting materials against target molecules (bacteria, toxins, etc)

Aptamer binds to metallo-beta-lactamase