Publication | Open Access
Non-heme Iron Proteins
68
Citations
22
References
1968
Year
Iron MetabolismBacteriologyMolecular BiologyIron DeficiencyRedox BiologyOxidative StressSingle Polypeptide ChainProteomicsBiochemistryNon-heme Iron ProteinsActive SiteHeme SignalingHeme TransportMolecular MicrobiologyHeme HomeostasisPeptostreptococcus Elsdenii RubredoxinPeriodic Surface StructuresNatural SciencesMicrobiologyMedicineHepcidin
Abstract The determination of the complete amino acid sequence of Peptostreptococcus elsdenii rubredoxin has shown that the molecule consists of a single polypeptide chain of 52 residues. When it is compared with the sequence of rubredoxin from Micrococcus aerogenes which contains 53 residues, matching amino acid residues are found in 24 positions. The 4 cysteines which are bound to the iron, 2 lysines, 2 tyrosines, and the sole tryptophan occur in identical positions in the two proteins. The possible importance of these findings for the active site of this non-heme iron protein is discussed.
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