Coordination environment for the type 3 copper center of tree laccase and CuB of cytochrome c oxidase as determined by electron nuclear double resonance.

Cline, John F.; Reinhammar, Bengt; Jensen, Per H.; Venters, Ronald A.; Hoffman, Brian M.

doi:10.1016/s0021-9258(18)32547-x

Cited by 66 publications

(19 citation statements)

References 16 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Table S1 (Supporting Information) summarizes 14 N ESEEM-derived nqi parameters for several copper(II)-containing proteins, as well as the nqi parameters derived here for pMMO, e 2 qQ = 1.60 and η = 0.98. Furthermore, the observed ESE-ENDOR features yield a hyperfine coupling of ∼38 MHz for the 14 N -labeled sample, which agrees with literature values for imidazole nitrogens from histidine residues bound to Cu(II) centers in metalloproteins and model compounds. − Thus, we conclude the existence of histidine coordination for at least one of the copper ions in the active site of pMMO.…”

supporting

confidence: 89%

Pulsed EPR Studies of Particulate Methane Monooxygenase from Methylococcus Capsulatus (Bath): Evidence for Histidine Ligation

et al. 1998

View full text Add to dashboard Cite

supporting

confidence: 89%

Pulsed EPR Studies of Particulate Methane Monooxygenase from Methylococcus Capsulatus (Bath): Evidence for Histidine Ligation

et al. 1998

View full text Add to dashboard Cite

“…0006-2960/87/0426-2091 $01.50/0 et al, 1978) and isotopically substituted [(2H)Cys and (15N)His] enzymes from the yeast Saccharomyces cerevisiae (Stevens et al, 1982) have revealed hyperfine interactions between the copper unpaired electron and a nitrogen from at least one histidine ligand and protons from at least one cysteine ligand. Similar ENDOR studies on a CuB EPR signal observed during turnover conditions have revealed hyperfine interactions from three nitrogenous ligands (Cline et al, 1983). While X-ray absorption measurements can in principle provide some insight into the ligands for both coppers, definite assignment of the ligand atom scattering contributions to each copper site has been difficult due to the overlap of the CuA and CuB absorption edges.…”

mentioning

confidence: 60%

“…The three (N, O) ligands in the inner coordination sphere of CuB are in accord with earlier spectroscopic studies on this site. Using ENDOR, Cline et al (1983) identified three distinctly inequivalent nitrogen hyperfine interactions associated with an EPR-visible CuB species trapped during turnover. Experiments on (15N)His-substituted yeast oxidase are in progress to identify these nitrogenous ligands.…”

Section: Discussionmentioning

confidence: 99%

Extended x-ray absorption fine structure of copper in CuA-depleted, p-(hydroxymercuri)benzoate-modified, and native cytochrome c oxidase

Li¹,

Gelles²,

Chan³

et al. 1987

Biochemistry

View full text Add to dashboard Cite

Cytochrome c oxidase contains four redox-active metal centers: two heme irons, cytochromes a and a3, and two copper ions, CuA and CuB. Due to the paucity of spectroscopic signatures for both copper sites in cytochrome c oxidase, the ligands and structures for these sites have remained ambiguous. The specific depletion of CuA from the p-(hydroxymercuri)benzoate- (pHMB-) modified cytochrome c oxidase recently reported [Gelles, J., & Chan, S. I. (1985) Biochemistry 24, 3963-3972] is herein described. Characterization of this enzyme shows that the structures of the remaining metal centers are essentially unperturbed by the CuA modification and depletion (P. M. Li, J. Gelles, and S. I. Chan, unpublished results). Copper extended X-ray absorption fine structure (EXAFS) measurements on the CuA-depleted cytochrome c oxidase reveal coordination of three (N, O) ligands and one (S, Cl) ligand at the CuB site. Comparison of EXAFS results obtained for the CuA-depleted, pHMB-modified, and "unmodified control" enzymes has allowed the deconvolution of the EXAFS in terms of the inner coordination spheres for CuA as well as CuB. On the basis of these data, it is found that the structure for the CuA site is consistent with two (N, O) ligands and two S ligands.

show abstract

“…Spectroscopic data concerning the nature of the Cub ligands are equivocal. ENDOR studies of the mammalian oxidase suggest two or three histidines ligated to Cub (Cline et al, 1983) and as many as four histidines ligated to CuB in the baytypc oxidase from Thermus thermophilus (Surerus et al, 1992). EXAFS studies on the fully oxidized mammalian oxidase (Powers et al, 1981) and on the aaytypz quinol oxidase from Bacillus subtilis (Powers et al, 1994) have been interpreted in terms of two histidine ligands plus one oxygen (or nitrogen) at a long distance (2.8 A).…”

Section: Discussionmentioning

confidence: 99%

Site-Directed Mutagenesis of Residues within Helix VI in Subunit I of the Cytochrome bo3 Ubiquinol Oxidase from Escherichia coli Suggests That Tyrosine 288 May Be a CuB Ligand

Thomas¹,

Calhoun²,

Lemieux³

et al. 1994

Biochemistry

View full text Add to dashboard Cite

The heme-copper oxidase superfamily contains all of the mammalian mitochondrial cytochrome c oxidases, as well as most prokaryotic respiratory oxidases. All members of the superfamily have a subunit homologous to subunit I of the mammalian cytochrome c oxidases. This subunit provides the amino acid ligands to a low-spin heme component as well as to a heme-copper binuclear center, which is the site where dioxygen is reduced to water. The amino acid sequence of transmembrane helix VI of subunit I is the most highly conserved within the superfamily. Previous efforts have demonstrated that one of the residues in this region, H284, is critical for oxidase activity and for the assembly of CuB. This paper presents the analysis of additional site-directed mutants in which other highly conserved residues in helix VI (P285, E286, Y288, and P293) have been substituted. Most of the mutants are enzymatically inactive. Structural perturbations reported by Fourier transform infrared absorption difference spectroscopy of CO adducts of the mutant oxidases confirm the previous suggestion that this region is adjactent to CuB. Furthermore, the analysis of five different substitutions for Y288 indicates that all lack CuB. On the basis of these data, it is proposed that Y288 may be a CuB ligand along with H333, H334, and H284, and a plausible molecular model of the CuB site is presented.

show abstract

Coordination environment for the type 3 copper center of tree laccase and CuB of cytochrome c oxidase as determined by electron nuclear double resonance.

Cited by 66 publications

References 16 publications

Pulsed EPR Studies of Particulate Methane Monooxygenase from Methylococcus Capsulatus (Bath): Evidence for Histidine Ligation

Pulsed EPR Studies of Particulate Methane Monooxygenase from Methylococcus Capsulatus (Bath): Evidence for Histidine Ligation

Extended x-ray absorption fine structure of copper in CuA-depleted, p-(hydroxymercuri)benzoate-modified, and native cytochrome c oxidase

Site-Directed Mutagenesis of Residues within Helix VI in Subunit I of the Cytochrome bo3 Ubiquinol Oxidase from Escherichia coli Suggests That Tyrosine 288 May Be a CuB Ligand

Contact Info

Product

Resources

About