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Design of a New Mimochrome with Unique Topology by Angela Lombardi; Flavia Nastri; Daniela Marasco; Ornella Maglio; Giampiero De Sanctis; Federica Sinibaldi; Roberto Santucci; Massimo Coletta; Vincenzo Pavone is a Chemistry article available to read on EtoBox.

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## Abstract Peptide‐based metalloprotein models represent useful systems to help understand how metalloproteins can support different functions, by the use of similar metal ion cofactors. In order to shed light on the role of the protein matrix in modulating the heme properties, we developed new models: mimochromes. They are pseudo‐__C__~2~ symmetric systems, composed of two helical peptides covalently linked to the deuteroporphyrin. The use of __C__~2~ symmetry is particularly advantageous, because it simplifies the design, synthesis and characterization. However, it leaves the problem of possible diastereomeric forms. In the cobalt complex of the first derivative, mimochrome I, Λ and Δ isomers were indeed experimentally observed. All the insights derived from the Co^III^–mimochrome I structure were used to obtain a re‐designed molecule, mimochrome IV. The spectroscopic characterization of the iron and cobalt derivatives suggested the presence of the Λ isomer as unique species. The NMR solution structure of the diamagnetic Co^III^–mimochrome IV confirmed the ability of the molecule to adopt a unique topology, and revealed the peptide chains to be in helical conformation, as design

Who reads Design of a New Mimochrome with Unique Topology?

Author

Angela Lombardi; Flavia Nastri; Daniela Marasco; Ornella Maglio; Giampiero De Sanctis; Federica Sinibaldi; Roberto Santucci; Massimo Coletta; Vincenzo Pavone

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Ltd.; Wiley (ISSN 0947-6539)

Published

2003

Language

EN

Field

Chemistry (Physical Sciences)