Structure, function and evolution of bacterial ferredoxins

During the past few years, the field of ironsulfur proteins has not ceased expanding. This evolution is due to the development of sophisticated methods such as electron paramagnetic resonance, M~Sssbauer or X-ray crystallography and to a fruitful interdisciplinary collaboration between biochemists, chemists and physicists. These advances have brought to light how widespread the non-heme iron proteins are, and their importance amongst the electron carrier proteins together with the flavoproteins, cytochromes and cuproproteins. With some exceptions, all organisms are dependent upon transducing electron transport chains for the production of ATP. The two metals, iron and copper, naturally selected during biological evolution, have two easily accessible oxidation states. The iron-sulfur clusters are among the simplest electron transfer groups and have been suggested as the first to have been produced during