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Published February 1995 | public
Journal Article

Paramagnetic NMR spectroscopy and coordination structure of cobalt(II) Cys112Asp azurin

Abstract

Paramagnetic ^1H-NMR spectra of Co(II)-substituted Cys112Asp azurin from Pseudomonas aeruginosa have been analyzed and compared with those of the Co(II) wild-type (WT) protein. Hyperfine-shifted signals (including Asp112 β-CH_2 signals in the mutant as well as previously unobserved Cys112 β-CH_2 signals in WT) from all the metal-coordinated residues have been detected and unambiguously assigned. Notably, the spectra indicate that very little if any unpaired spin density is located on the Met121 protons in the Cys112Asp protein. A computer-generated model of the mutant Co(II) structure consistent with electronic absorption as well as the NMR data includes a Gly45 carbonyl, His46, an unusually coordinated Asp112, and His117 in the ligation sphere.

Additional Information

© 1995 American Chemical Society. Received October 6, 1994. We thank Ivano Bertini for many helpful discussions. This work was supported by the National Institutes of Health.

Additional details

Created:
August 20, 2023
Modified:
October 23, 2023