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Title: New perspectives on bacterial ferredoxin evolution. Author: George DG, Hunt LT, Yeh LS, Barker WC. Journal: J Mol Evol; 1985; 22(1):20-31. PubMed ID: 3932661. Abstract: Recent evidence indicates that a gene transposition event occurred during the evolution of the bacterial ferredoxins subsequent to the ancestral intrasequence gene duplication. In light of this new information, the relationships among the bacterial ferredoxins were reexamined and an evolutionary tree consistent with this new understanding was derived. The bacterial ferredoxins can be divided into several groups based on their sequence properties; these include the clostridial-type ferredoxins, the Azotobacter-type ferredoxins, and a group containing the ferredoxins from the anaerobic, green, and purple sulfur bacteria. Based on sequence comparison, it was concluded that the amino-terminal domain of the Azotobacter-type ferredoxins, which contains the novel 3Fe:3S cluster binding site, is homologous with the carboxyl-terminal domain of the ferredoxins from the anaerobic photosynthetic bacteria. A number of ferredoxin sequences do not fit into any of the groups described above. Based on sequence properties, these sequences can be separated into three groups: a group containing Methanosarcina barkeri ferredoxin and Desulfovibrio desulfuricans ferredoxin II, a group containing Desulfovibrio gigas ferredoxin and Clostridium thermoaceticum ferredoxin, and a group containing Desulfovibrio africanus ferredoxin I and Bacillus stearothermophilus ferredoxin. The last two groups differ from all of the other bacterial ferredoxins in that they bind only one Fe:S cluster per polypeptide, whereas the others bind two. Sequence examination indicates that the second binding site has been either partially or completely lost from these ferredoxins. Methanosarcina barkeri ferredoxin and Desulfovibrio desulfuricans ferredoxin II are of interest because, of all the ferredoxins whose sequences are presently known, they show the strongest evidence of internal gene duplication.(ABSTRACT TRUNCATED AT 400 WORDS)[Abstract] [Full Text] [Related] [New Search]