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Axial Ligand Modulation of the Electronic Structures of Binuclear Copper Sites:  Analysis of Paramagnetic ^1H NMR Spectra of Met160Gln Cu_A

Fernández, Claudio O. and Cricco, Julia A. and Slutter, Claire E. and Richards, John H. and Gray, Harry B. and Vila, Alejandro J. (2001) Axial Ligand Modulation of the Electronic Structures of Binuclear Copper Sites:  Analysis of Paramagnetic ^1H NMR Spectra of Met160Gln Cu_A. Journal of the American Chemical Society, 123 (47). pp. 11678-11685. ISSN 0002-7863. https://resolver.caltech.edu/CaltechAUTHORS:20150504-115753848

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Abstract

Cu_A is an electron-transfer copper center present in heme-copper oxidases and N_2O reductases. The center is a binuclear unit, with two cysteine ligands bridging the metal ions and two terminal histidine residues. A Met residue and a peptide carbonyl group are located on opposite sides of the Cu2S2 plane; these weaker ligands are fully conserved in all known Cu_A sites. The Met160Gln mutant of the soluble subunit II of Thermus thermophilus ba_3 oxidase has been studied by NMR spectroscopy. In its oxidized form, the binuclear copper is a fully delocalized mixed-valence pair, as are all natural Cu_A centers. The faster nuclear relaxation in this mutant suggests that a low-lying excited state has shifted to higher energies compared to that of the wild-type protein. The introduction of the Gln residue alters the coordination mode of His114 but does not affect His157, thereby confirming the proposal that the axial ligand-to-copper distances influence the copper−His interactions (Robinson, H.; Ang, M. C.; Gao, Y. G.; Hay, M. T.; Lu, Y.; Wang, A. H. Biochemistry 1999, 38, 5677). Changes in the hyperfine coupling constants of the Cys β-CH_2 groups are attributed to minor geometrical changes that affect the Cu−S−C_β−H_β dihedral angles. These changes, in addition, shift the thermally accessible excited states, thus influencing the spectral position of the Cys β-CH_2 resonances. The Cu−Cys bonds are not substantially altered by the Cu−Gln160 interaction, in contrast to the situation found in the evolutionarily related blue copper proteins. It is possible that regulatory subunits in the mitochondrial oxidases fix the relative positions of thermally accessible Cu_A excited states by tuning axial ligand interactions.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1021/ja0162515DOIArticle
http://pubs.acs.org/doi/abs/10.1021/ja0162515PublisherArticle
ORCID:
AuthorORCID
Gray, Harry B.0000-0002-7937-7876
Additional Information:© 2001 American Chemical Society. Received May 22, 2001. Publication Date (Web): October 31, 2001. This work was supported by NIH Grants R01-DK19038 to H.B.G. and R01-GM16424 to J.H.R. and FIRCA-NIH Grant R03-TW000985-01 to H.B.G. and A.J.V. C.O.F. and A.J.V. are staff members at CONICET. J.A.C. is recipient of a fellowship from CONICET. We thank Ramiro Rodríguez for help with protein purification and Sergio Dalosto for helpful discussions. C.O.F. and A.J.V. thank CERM (University of Florence) for allowing C.O.F. to record the 800 MHz spectra and for the hospitality offered to C.O.F. Accession Codes: PDB: 2cua PDB: file+2cua PDB: file+1ar1
Funders:
Funding AgencyGrant Number
NIHR01-DK19038
NIHR01-GM16424
FIRCA-NIHR03-TW000985-01
Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET)UNSPECIFIED
Issue or Number:47
Record Number:CaltechAUTHORS:20150504-115753848
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20150504-115753848
Official Citation:Axial Ligand Modulation of the Electronic Structures of Binuclear Copper Sites:  Analysis of Paramagnetic 1H NMR Spectra of Met160Gln CuA Claudio O. Fernández, Julia A. Cricco, Claire E. Slutter, John H. Richards, Harry B. Gray, and Alejandro J. Vila Journal of the American Chemical Society 2001 123 (47), 11678-11685 DOI: 10.1021/ja0162515
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:57196
Collection:CaltechAUTHORS
Deposited By: George Porter
Deposited On:04 May 2015 20:16
Last Modified:22 Nov 2019 09:58

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