Abstract
The amino acid sequence of ferredoxin from a thermophilic anaerobic bacterium, Clostridium thermocellum, has been determined. This heat-stable ferredoxin is a small acidic protein composed of 55 amino acid residues with a molecular weight of 5605 excluding the two (4Fe-4S) clusters and lacks histidine, arginine, tryptophan, methionine and leucine. From the comparison of the amino acid sequences of two (4Fe-4S) ferredoxins isolated from mesophilic and thermophilic bacteria, special characteristics of thermostable ferredoxins are discussed. A three-dimensional model of C. thermocellum ferredoxin has been derived from the Peptococcus aerogenes crystallographic structure. This model indicates that thermostability could arise from hydrophobic substitutions on the surface of the molecule together with the formation of specific salt bridges specially involving the N and C terminal ends.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Enzymology
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