The iron-sulphur proteins: Evolution of a ubiquitous protein from model systems to higher organisms

Details The iron-sulphur proteins: Evolution of a ubiquitous protein from model systems to higher organisms The iron-sulphur proteins: Evolution of a ubiquitous protein from model systems to higher organisms

Jul 1974

adsabs.harvard.edu/cgi-bin/nph-data_query?bibcode=1974orli....5..363h&link_type=abstract

Origins of Life, Volume 5, Issue 3-4, pp. 363-386

Mathematics

Logic

6

Scientific paper

Ferredoxins are Fe-S proteins with low molecular weight (6 12000) which act as electron carriers at very low redox potentials eg. -300 to -500 mV, in diverse biochemical processes such as bacterial and plant photosynthesis, N2 fixation, carbon metabolism, oxidative phosphorylation and steroid hydroxylation. They are found in a wide range of organisms from the ‘primitive’ obligate anaerobic bacteria, through photosynthetic bacteria, blue-green and green algae, to all higher plants and animals. Three types of ferredoxins are known -8 Fe+8 S, 4 Fe+4 S and 2 Fe+2 S. All three have been found in bacteria while the 2 Fe and some 8 Fe ferredoxins have been found in plants and animals possibly representing an evolutionary sequence. The 8 Fe ferredoxin may all be composed of two 4 Fe units. We have proposed that because of the simplicity of the 8 Fe ferredoxins (only 9 common simple amino acids in clostridia, 6 of which have been detected in the Murchison meteorite) they may have been amongst the earliest proteins formed during the origin of life. A simple peptide of about 27 amino acids could incorporate inorganic Fe+S (or possibly an existing Fe-S complex) into it nonenzymatically under anaerobic conditions to form a protein carrying one or two electrons at the potential of the H2 electrode. More than ten Fe-S model compounds have been proposed as analogues of the 4 Fe or 2 Fe containing active centres; inorganic, organometallic and peptide complexes have been synthesized. A few have many of the properties of ferredoxins but none as yet fulfills a sufficient number of criteria to substitute for ferredoxins chemically and biologically — a goal which will provide many clues to primitive peptide systems undergoing biological electron transfer reactions.

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