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

Piccioli, Mario and Luchinat, Claudio and Mizoguchi, Tadashi J. and Ramirez, Benjamin E. and Gray, Harry B. and Richards, John H. (1995) Paramagnetic NMR spectroscopy and coordination structure of cobalt(II) Cys112Asp azurin. Inorganic Chemistry, 34 (3). pp. 737-742. ISSN 0020-1669. doi:10.1021/ic00107a027.

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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.

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Gray, Harry B.0000-0002-7937-7876
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.
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Issue or Number:3
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Official Citation:Paramagnetic NMR spectroscopy and coordination structure of cobalt(II) Cys112Asp azurin Mario Piccioli, Claudio Luchinat, Tadashi J. Mizoguchi, Benjamin E. Ramirez, Harry B. Gray, and John H. Richards Inorganic Chemistry 1995 34 (3), 737-742 DOI: 10.1021/ic00107a027
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:57238
Deposited By: Tony Diaz
Deposited On:06 May 2015 16:39
Last Modified:10 Nov 2021 21:10

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