Metal sites of copper proteins. III. Symmetry of copper in bovine superoxide dismutase and its functional significance

Rotilio, Giuseppe; Morpurgo, Laura; Giovagnoli, Carlo; Calabrese, Lilia; Mondovı̀, Bruno

doi:10.1021/bi00761a028

Cited by 165 publications

(80 citation statements)

References 19 publications

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“…MHz. Thus we have found that, of the three nearly equivalent nitrogens previously reported [4,8] only two are equivalent as determined by both ENDOR and EPR.…”

Section: I(i+i) %N =A=s:i: + P=( I~ 3 ] --Gnflnhoizsupporting

confidence: 50%

“…The extremely low NMR relaxivity of the monocyano derivative [8] suggests that water molecules cannot bind directly to the Cu(II), thus implying that the displaced histidine is coordinated as an axial ligand. This model is consistent with, but not proven by, these spectral observations.…”

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

“…Moreover, the electron paramagnetic resonance (EPR) spectrum of holoprotein changes markedly on binding CN-, and the resulting spectrum reveals the presence of three nearly equivalent nitrogens in the copper hyperfine spectrum [7][8][9][10][11]. Rotilio et al [8] and Haffner and Coleman [12] showed, using 13CN-, that the cyanide binds to the copper via its carbon atom. Lieberman et al [13] have recently described cyanide-induced changes in the g-tensor principal axis system as seen through the EPR of crystalline dismutase, and cyanide has been shown to induce changes in the electronic structure of the remote imidazole nitrogen as observed [14] by the electron spin echo effect (ESE).…”

Section: Introductionmentioning

confidence: 99%

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An examination of the cyanide derivative of bovine superoxide dismutase with electron-nuclear double resonance

Camp¹,

Sands

Fee

1982

Biochimica et Biophysica Acta (BBA) - Protein Structure and Mol

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The Cu(ll) sites of native, azido-and cyano-derivatives of bovine superoxide dismutase (superoxide:superoxide oxidoreduetase, EC 1.15.1.1) have been examined by electron-nuelear double resonance OENDOR). The ENDOR spectrum of the native protein taken at the g ll extreme shows resolved structure due to the directly coordinated N-atoms of the histidine ligands. These spectra are too complex for interpretation but suggest ineqnivalent coupling between the electronic spin and the four ligand N-atoms. By contrast, the azido protein reveals one type of nitrogen with well-resolved hypedine and quadrupole splittings (A~ = 37.9 + --1 MHz, P~ = 1.54+-0.02 MHz), and the cyano form reveals one well-resolved set of nitrogen lines (A~ =47.8 +-0.4 ME[z, P~ =1.62+-0.01 MHz) and one type of partially resolved nitrogen (A,~ =37.0+-1 Mltz). The cyano form also reveals a complex spectrum in the low-frequency domain (1-10 MHz). Through isotopic substitution and computer simulation, the spectrum is shown to be a composite of the ENDOR from the remote imidazole nitrogens and the cyanide nitrogen. The component of the hypedine constant perpendicular to the CI4N bond axis is ANx =3.9+-0.3 MHz and along the bond axis is A~ -----5.7 MHz. The quadrupole interaction appears to be greatest along the CN axiswith Qz'z' = 1.0---0.1 MHz and Q~,,,y,y, ~0. Based on an analysis of the hypedine and quadrupole interactions seen at two extremes of the electron paramagnetic spectrum, we propose a square-planar arrangement of three imidazole nitrogen and one CN-carbon around the copper. Within this plane two imidazole nitrogens are strongly coupled and magnetically equivalent, the third is inequivalent (slightly weaker hypedine interaction) and forms a trans relationship with the cyanide. This model is consistent with other observations on the cyano-derivative.

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“…MHz. Thus we have found that, of the three nearly equivalent nitrogens previously reported [4,8] only two are equivalent as determined by both ENDOR and EPR.…”

Section: I(i+i) %N =A=s:i: + P=( I~ 3 ] --Gnflnhoizsupporting

confidence: 50%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

An examination of the cyanide derivative of bovine superoxide dismutase with electron-nuclear double resonance

Camp¹,

Sands

Fee

1982

Biochimica et Biophysica Acta (BBA) - Protein Structure and Mol

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“…The lack of reactivity with ferrocyanide and azide is in line with the absence of superoxide dismutase activity. A similar result was obtained with Cu/Zn superoxide dismutase when copper is bound to the zinc site [14]. Cyanide on the other hand was capable of entering the first coordination sphere of the metal giving rise to a complex with an EPR spectrum very reminiscent of that already described for the copper-cyanide complex of copper/zinc superoxide dismutase [14].…”

Section: Resultssupporting

confidence: 78%

Replacement of Mn(III) with Cu(II) in Bacillus stearothermophilus superoxide dismutase

1985

Self Cite

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Copper(II) was substituted for manganese(III) in Bacillus stearothermophilus Mn‐superoxide dismutase. The (EPR) spectrum of the Cu(II) is distinctly rhombic, overlapping that of Cu(II) replacing zinc in copper/zinc Superoxide dismutase. The copper‐cyanide complex of the bacterial enzyme gives an EPR spectrum nearly identical to the cyanide‐copper complex of the Cu/Zn enzyme, indicating three nitrogens as metal ligands. These results support the suggestion that metal coordination in B. stearothermophilus Mn‐dismutase is a tetrahedral arrangement of three imidazoles and a carboxylate group and indicate copper as a good spectroscopic probe for studying the active site of Mn‐ and Fe‐superoxide dismutases.

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Copper‐Zinc Superoxide Dismutase in Prokaryotes and Eukaryotes

Bordo¹,

Pesce²,

Bolognesi³

et al. 2004

Handbook of Metalloproteins

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Cu,Zn superoxide dismutases (SODs) are ubiquitous enzymes catalyzing the conversion of superoxide radical anions into O 2 and H 2 O 2 . In eukaryotes, Cu,Zn SOD is a dimeric protein (2 × 16 k Da); each protomer hosts the binuclear Cu,Zn catalytic center. In prokaryotes, Cu,Zn SODs can be monomeric or dimeric, their quaternary structure differing from that of the eukaryotic homologs. The protein tertiary structure (based on an eight‐stranded antiparallel β‐barrel) is conserved through species. Crystal structures and mutational analysis indicate that Cu,Zn SOD activity is based on a redox cycle, whereby the catalytic Cu(II) species is first reduced (to Cu(I)), and then oxidized (back to Cu(II)) by successive encounters with the substrate. The Zn ion plays a key structural role in maintaining active site structural integrity during the catalytic cycle. Efficient electrostatic steering of the anionic substrate to the active site accounts for the very high (diffusion limited) catalytic turnover displayed by all Cu,Zn SODs. Mutations in human cytoplasmic Cu,Zn SOD have been related to the onset of FALS (familial amyotrophic lateral sclerosis , or Lou Gehring disease), a fatal motoneuron degenerative disease.

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Metal sites of copper proteins. III. Symmetry of copper in bovine superoxide dismutase and its functional significance

Cited by 165 publications

References 19 publications

An examination of the cyanide derivative of bovine superoxide dismutase with electron-nuclear double resonance

An examination of the cyanide derivative of bovine superoxide dismutase with electron-nuclear double resonance

Replacement of Mn(III) with Cu(II) in Bacillus stearothermophilus superoxide dismutase

Copper‐Zinc Superoxide Dismutase in Prokaryotes and Eukaryotes

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