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• W2019923078 abstract "Abstract 1. 1. Amino acid analysis of molybdoferredoxin from Clostridium pasteurianum showed a majority of acidic amino acids, which is consistent with its electrophoretic behavior. Other features of the amino acid composition are the presence of 3 tryptophan residues and 20 half-cystine residues per 110 000 daltons. 2. 2. Azoferredoxin has a preponderance of aspartic and glutamic acids over basic amino acids. Tryptophan is absent in this protein. There are 12 half-cystine residues per 55 000 daltons. 3. 3. Molybdoferredoxin has been resolved into its two types of composite subunits, one with a molecular weight of 60 000 and one of 50 000. A comparison of the amino acid composition of native molybdoferredoxin with that of an equimolar combination of subunits shows good agreement. 4. 4. Comparison of the amino acid compositions of the nitrogenase components from C. pasteurianum with published compositions of Klebsiella pneumoniae and Azotobacter vinelandii (the MoFe protein only) show that the half-cystine, histidine and proline residues are almost identical. But although the general pattern of the remaining amino acids is similar, there are considerable differences in the tryptophan content of molybdoferredoxin from these three organisms. 5. 5. C-terminal analysis of molybdoferredoxin indicated the presence of alanine and leucine, consistent with the presence of two different subunits. Detection of leucine as the single C-terminal residue in azoferredoxin is compatible with two identical subunits in azoferredoxin dimer. 6. 6. Far ultraviolet circular dichroism spectra of both azoferredoxin and molybdoferredoxin showed pronounced differences in the secondary structure between the air-oxidized and reduced state. 7. 7. Circular dichroism data on the mersalyl derivatives of both proteins exhibited decrease in α-helical structure." @default.
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• W2019923078 date "1973-05-01" @default.
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• W2019923078 title "Structural investigation of nitrogenase components from Clostridium pasteurianum and comparison with similar components of other organisms" @default.
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• W2019923078 doi "https://doi.org/10.1016/0005-2795(73)90007-x" @default.
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