Metal coordination of azurin in the unfolded state

FEBS Letters

Donaire, Antonio²  Moratal, José Marı́a¹  Romero, Carmen¹ 

[1] Departamento de Quı́mica Inorgánica, Universitat de Valencia, C/ Dr. Moliner 50, 46100-Burjassot, Valencia, Spain;Centro de Estudios Universitarios ‘San Pablo', Universitat de Valencia, Montcada, Valencia, Spain

关键词: Protein folding;    Rack mechanism;    Azurin;    Blue copper protein;    Nuclear magnetic resonance;    BCPs;    blue copper proteins;    GuHCl;    guanidine hydrochloride;   

DOI  :  10.1016/S0014-5793(98)01438-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

¹H NMR data applied to the paramagnetic cobalt(II) derivative of azurin from Pseudomonas aeruginosa have made it possible to show that the metal ion is bound to the protein in the unfolded state. The relaxation data as well as the low magnetic anisotropy of the metal ion indicate that the cobalt ion is tetrahedral in the unfolded form. The cobalt ligands have been identified as the residues Gly45, His46, Cys112 and His117. Met121 is not coordinated in the unfolded state. In this state, the metal ion is not constrained to adopt a bipyramidal geometry, as imposed by the protein when it is folded. This is clear confirmation of the rack-induced bonding mechanism previously proposed for the metal ion in azurin.

【 授权许可】

Unknown