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• W1591126935 abstract "Here we report the structural and functional characterization of a covalent complex (MKP) obtained by cross-linking microperoxidase (Mp), the haem-undecapeptide obtained by the peptic digestion of cytochrome c, with a 21-residue synthetic peptide (P21) analogous to the S-peptide of the RNase A. The covalent complex has been prepared by introducing a disulphide bond between Cys-1 of P21 and Lys-13 of Mp, previously modified with a thiol-containing reagent. On formation of the complex (which is a monomer), the helical content of P21 increases significantly. The results obtained indicate that His-13 of P21 co-ordinates to the sixth co-ordination position of the haem iron, thus leading to the formation of a complex characterized by an equilibrium between an ‘open’ and a ‘closed’ structure, as confirmed by molecular dynamics simulations. Under acidic pH conditions, where His-13 of P21 is loosely bound to the haem iron (‘open’ conformation), MKP displays appreciable, quasi-reversible electrochemical activity; in contrast, at neutral pH (‘closed’ conformation) electrochemical behaviour is negligible, indicating that P21 interferes with the electron-transfer properties typical of Mp. On the whole, MKP is a suitable starting material for building a miniature haem system, with interesting potential for application to biosensor technology." @default.
• W1591126935 created "2016-06-24" @default.
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• W1591126935 date "1997-12-15" @default.
• W1591126935 modified "2023-10-16" @default.
• W1591126935 title "Covalent complex of microperoxidase with a 21-residue synthetic peptide as a maquette for low-molecular-mass redox proteins" @default.
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• W1591126935 doi "https://doi.org/10.1042/bj3280833" @default.
• W1591126935 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1218994" @default.
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