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Miniaturized heme proteins: crystal structure of Co(III)-mimochrome IV

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Miniaturized heme proteins: crystal structure of Co(III)-mimochrome IV

Content Provider	Springer Nature Link
Author	Costanzo, Luigi Geremia, Silva Randaccio, Lucio Nastri, Flavia Maglio, Ornella Lombardi, Angela Pavone, Vincenzo
Copyright Year	2004
Abstract	Protein design provides an attractive approach to test the essential features required for folding and function. Previously, we described the design and structural characterization in solution of mimochromes, a series of miniaturized metalloproteins, patterned after the F-helix of the hemoglobin β-chain. Mimochromes consist of two medium-sized helical peptides, covalently linked to the deuteroporphyrin. CD and NMR characterization of the prototype, mimochrome I, revealed that the overall structure conforms well to the design. However, formation of Δ and Λ diastereomers was observed. To overcome the problem of diastereomer formation, we re-designed mimochrome I, by engineering intramolecular, interchain interactions. The resulting model was mimochrome IV: the solution structural characterization showed the presence of the Λ isomer as a unique form. To examine the extent to which the stereochemical stability and uniqueness of mimochrome IV was retained in the solid state, the crystal structure of Co(III)-mimochrome IV was solved by X-ray diffraction, and compared to the solution structure of the same derivative. Co(III)-mimochrome IV structures, both in solution and in the solid state, are characterized by the following common features: a bis-His axial coordination, a Λ configuration around the metal ion, and a predominant helical conformation of the peptide chains. However, in the crystal structure, intrachain Glu1–Arg9 ion pairs are preferred over the designed, and experimentally found in solution, interchain interactions. This ion pairing switch may be related to strong packing interactions.
Starting Page	1017
Ending Page	1027
Page Count	11
File Format	PDF
ISSN	09498257
Journal	JBIC Journal of Biological Inorganic Chemistry
Volume Number	9
Issue Number	8
e-ISSN	14321327
Language	English
Publisher	Springer-Verlag
Publisher Date	2004-11-13
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Miniaturized hemeproteins Model compounds Protein design Structure X-ray diffraction
Content Type	Text
Resource Type	Article
Subject	Biochemistry Inorganic Chemistry

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