CHAPTER 24 – Evolution of Protein Molecules

https://science.sciencemag.org/content/sci/155/3760/279.full.pdf

Construction of Phylogenetic Trees

High recovery of tryptophan from acid hydrolysates of proteins

A new acid hydrolysis method for determining tryptophan in peptides and proteins.

The structure of present-day ferredoxin, with its simple, inorganic active site and its functions basic to photon-energy utilization, suggests the incorporation of its prototype into metabolism very early during biochemical evolution, even before complex proteins and the complete modern genetic code existed. The information in the amino acid sequence of ferredoxin enables us to propose a detailed reconstruction of its evolutionary history. Ferredoxin has evolved by doubling a shorter protein, which may have contained only eight of the simplest amino acids. This shorter ancestor in turn developed from a repeating sequence of the amino acids alanine, aspartic acid or proline, serine, and glycine. We explain the persistence of living relics of this primordial structure by invoking a conservative principle in evolutionary biochemistry: The processes of natural selection severely inhibit any change a well-adapted system on which several other essential components depend.

https://science.sciencemag.org/content/sci/152/3720/363.full.pdf

Ann M. Benson

Papers

Non-heme Iron Proteins X. THE AMINO ACID SEQUENCES OF FERREDOXINS FROM LEUCAENA GLAUCA

The amino acid sequence of bovine heart cytochrome c.

The Amino Acid Sequence of Bovine Heart Cytochrome c

The amino acid sequence of clostridium pasteurianum ferredoxin

The action of the Bacillus subtilis neutral protease on S-β-aminoethylcysteinyl ferredoxin from Clostridium pasteurianum