Towards a Protocol for Solution Structure Determination of Copper(II) Proteins: the Case of Cu II Zn II  Superoxide Dismutase | Zendy

Bertini Ivano | Zendy; Felli Isabella C. | Zendy; Luchinat Claudio | Zendy; Parigi Giacomo | Zendy; Pierattelli Roberta | Zendy

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Towards a Protocol for Solution Structure Determination of Copper(II) Proteins: the Case of Cu II Zn II Superoxide Dismutase

Author(s) -

Bertini Ivano,

Felli Isabella C.,

Luchinat Claudio,

Parigi Giacomo,

Pierattelli Roberta

Publication year - 2007

Publication title -

chembiochem

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.05

H-Index - 126

eISSN - 1439-7633

pISSN - 1439-4227

DOI - 10.1002/cbic.200700006

Subject(s) - homonuclear molecule , chemistry , carboxylate , copper , crystallography , metalloprotein , metal , superoxide dismutase , spectral line , proton , ion , metal ions in aqueous solution , stereochemistry , molecule , enzyme , biochemistry , organic chemistry , physics , astronomy , quantum mechanics

We have developed an optimized protocol to solve the solution structure of copper(II) proteins. After assignment, proton–proton NOEs are used for the shell where 1 H spectra are conveniently observed. In a shell closer to the metal ion, 13 C NMR spectra with band‐selective homonuclear decoupling provide the assignment of all nuclei except for those of the metal ligands. A convenient method for the measurement of 13 C longitudinal‐relaxation rates ( R 1 ) of carbonyls and carboxylate moieties is proposed. 1 H NOEs and 1 H and 13 C R 1 data are sufficient to produce a good/reasonable solution structure, as demonstrated for a monomeric species of superoxide dismutase, a 153‐residue protein.

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