Iron Sulfr Protein Lab Report

Structures, Biosynthesis and Biofunctions of Iron-sulfer proteins
Yiming Chen, Brown University, May 11th, 2011

I. Introduction
Iron-sulfur proteins are the proteins which contain iron-sulfur clusters, like sulfide-linked di-, tri-, and tetrairon centers with various oxidative states 1. An excess of 120 distinct types of enzymes and proteins are known to contain Fe-S clusters2. Iron-sulfur proteins are known for the role of the oxidation-reduction reactions of mitochondrial electron transportation. They are also discovered in a series of metalloproteins procedures, for example, ferredoxins 3, Coenzyme Qcytochrome c reductase 4, succinate-coenzyme Q reductase
5

and nitrogenase 6. The iron-sulfur

proteins have many functions including catalysis, generate radicals, and also can play as sulfur donors in the biosynthesis of lipoic acid and biotin. Additionally some of the Fe-S proteins are able to regulate the gene expression. Furthermore, the discoveries of new iron-sulfur proteins and iron-sulfur clusters has led to lots of interests of their amazing functional and structural diversity, which reflects the versatility of both iron and sulfur in biochemical processes.
Thus theory claims that the early life on earth probaby formed on the surface of some iron sulfide minerals. It has been well developed by retrodiction from extant biochemistry and some chemical experiments. It has been reported that Fe-S proteins presumably were involved in the first catalysts that nature had to work