In plants, three Fe-S cluster assembly pathways exist namely SUF, ISC and CIA, involved in the maturation of iron sulfur proteins in the plastid, mitochondria and cytosol respectively. In this talk, we report on anaerobic purification of three classes of recombinant mitochondrial Fe-S cluster carrier proteins from A. thaliana, namely GRXS15, ISCA1a/2, and NFU4/5, and characterization of their Fe-S cluster content using UV-visible absorption/CD, resonance Raman, EPR, and analytical studies.

Ever since its discovery in 1988 by two research groups in France and Germany, Giant Magnetoresistance (GMR) has revolutionized the application of magnetic sensors in hard disk drives and magnetic memories.^1,2 It also offers an inspiration for their use in magnetic biodetections, a growing field with great promises.

Iron sulfur clusters are common cofactors found in almost all living organisms. They have diverse biological functions, ranging from electron transfer and catalysis to regulation of gene expression and enzyme activity.

Sulfurous acid is hypothesized to be a nucleation center for aerosols, but its isolation and characterization have been described as one of the greatest challenges of inorganic chemistry. Consequently, most information about sulfurous acid has come from the more than twenty theoretical studies examining it.