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The complete amino acid sequence, obtained by direct protein sequencing, of the pseudoazurin from Thiosphaera pantotropha is reported. It shows sequence identities varying from 46 to 66% with previously sequenced pseudoazurins. Previously identified conserved residues with key functions in pseudoazurins are found in the protein from T. pantotropha with the exception of glycine-39, the carbonyl group of which has been considered as a ligand to the copper, which is replaced by a serine residue. Electrospray-ionization MS (ESI-MS) has shown that pseudoazurin from T. pantotropha often contains two polypeptide species differing in molecular mass by 16 Da, presumably owing to oxidation of a methionine residue to a sulphoxide derivative. These two species have different endoproteinase Arg-C digestion patterns. Conditions for ESI-MS were identified that permitted either the retention or the loss of the single copper ion associated with the pseudoazurin. The aberrant tendency of T. pantotropha pseudoazurin to form a disulphide-bridged dimer on SDS/PAGE under some conditions is described.

Original publication

DOI

10.1042/bj3080585

Type

Journal article

Journal

Biochem J

Publication Date

01/06/1995

Volume

308 ( Pt 2)

Pages

585 - 590

Keywords

Amino Acid Sequence, Azurin, Base Sequence, Circular Dichroism, Gas Chromatography-Mass Spectrometry, Gram-Negative Bacteria, Molecular Sequence Data, Molecular Weight, Sequence Alignment, Sequence Homology, Amino Acid