Variations in the Type I Copper Protein Coordination Group: Resonance Raman Spectrum of 34S-, 65Cu-, and 15N-Labeled Plastocyanin

Qiu, Di; Dong, Shoulian; Ybe, Joel A.; Hecht, Michael H.; Spiro, Thomas G.

doi:10.1021/ja00129a005

Cited by 50 publications

(78 citation statements)

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“…This might be contributed from the stretching between copper and coordinated imidazole nitrogen atom of solvent exposed His 90 . The overall similarity of the resonance Raman spectrum to those of blue copper proteins suggests that the coordination at the copper site of Dryopteris plastocyanin is generally similar to that in higher plant plastocyanins (38,39).…”

Section: Resultsmentioning

confidence: 82%

The Structure and Unusual pH Dependence of Plastocyanin from the Fern Dryopteris crassirhizoma

Kohzuma¹,

Inoue²,

Yoshizaki³

et al. 1999

Journal of Biological Chemistry

114

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Spectroscopic properties, amino acid sequence, electron transfer kinetics, and crystal structures of the oxidized (at 1.7 Å resolution) and reduced form (at 1.8 Å resolution) of a novel plastocyanin from the fern Dryopteris crassirhizoma are presented. Kinetic studies show that the reduced form of Dryopteris plastocyanin remains redox-active at low pH, under conditions where the oxidation of the reduced form of other plastocyanins is inhibited by the protonation of a solvent-exposed active site residue, His 87 (equivalent to His 90 in Dryopteris plastocyanin). The x-ray crystal structure analysis of Dryopteris plastocyanin reveals -stacking between Phe 12 and His 90 , suggesting that the active site is uniquely protected against inactivation. Like higher plant plastocyanins, Dryopteris plastocyanin has an acidic patch, but this patch is located closer to the solvent-exposed active site His residue, and the total number of acidic residues is smaller. In the reactions of Dryopteris plastocyanin with inorganic redox reagents, the acidic patch (the "remote" site) and the hydrophobic patch surrounding His 90 (the "adjacent" site) are equally efficient for electron transfer. These results indicate the significance of the lack of protonation at the active site of Dryopteris plastocyanin, the equivalence of the two electron transfer sites in this protein, and a possibility of obtaining a novel insight into the photosynthetic electron transfer system of the first vascular plant fern, including its molecular evolutionary aspects. This is the first report on the characterization of plastocyanin and the first three-dimensional protein structure from fern plant.

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Section: Resultsmentioning

confidence: 82%

The Structure and Unusual pH Dependence of Plastocyanin from the Fern Dryopteris crassirhizoma

Kohzuma¹,

Inoue²,

Yoshizaki³

et al. 1999

Journal of Biological Chemistry

114

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“…, is significantly lower in nitrite reductase 80,81 (360 cm -1 ) than in plastocyanin 82,83 (420 cm -1 ) which implies that the Cu-S(Cys) bond is weaker. If all the S K-edge pre-edge intensity were to arise from the S(Cys)-Cu interaction, the longer, weaker Cu-S(Cys) bond should result in less sulfur covalency in the HOMO; however, reduced sulfur covalency in nitrite reductase is not observed.…”

Section: Results and Analysismentioning

confidence: 92%

Electronic Structure of the Perturbed Blue Copper Site in Nitrite Reductase: Spectroscopic Properties, Bonding, and Implications for the Entatic/Rack State

et al. 1996

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Low-temperature optical absorption, circular dichroism, magnetic circular dichroism, and sulfur K-edge X-ray absorption spectra have been measured for the green "blue" copper center (type 1) in Achromobacter cycloclastes nitrite reductase. Combined with density functional calculations, the results of these spectroscopies have been used to define the extremely "perturbed" electronic structure of this site relative to that of the prototypical "classic" site found in plastocyanin. Experimentally calibrated density functional calculations have been further used to determine the specific geometric distortions which generate the perturbed electronic structure. These studies indicate that the principal electronic structure changes in nitrite reductase, relative to plastocyanin, are a rotation of the Cu d 2 . These changes in Cu-ligand interactions result in the redistribution of absorption intensity in the charge transfer and ligand field transitions. Additionally, the new S(Met)-Cu interaction accounts for the unexpectedly high sulfur covalency in the HOMO. The increase in ligand field strength shifts all the d f d transitions in nitrite reductase to ∼1000 cm -1 higher energy than their counterparts in plastocyanin, which accounts for the EPR spectral differences between the type 1 sites in these complexes. The geometric distortion primarily responsible for the electronic structure changes in nitrite reductase, relative to plastocyanin, is determined to involve a coupled angular movement of the Cys and Met residues toward a more flattened tetrahedral (toward square planar) structure. This movement is consistent with a tetragonal Jahn-Teller distortion resulting from the shorter Cu-S(Met) bond in nitrite reductase relative to plastocyanin. This increased Jahn-Teller distortion implies that the type 1 site is "less entatic" than that in plastocyanin.

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“…Because the strongest peak in the RR spectra of blue copper proteins results from a predominantly Cu-S(Cys) stretching vibrational mode (Dave et al, 1993;Andrew et al, 1994;Qiu et al, 1995), the Cu-S bond strength in the two proteins should be very similar. The positions of the other three major peaks differ, however, and are shifted -5 4 cm" toward the higher frequencies relative to those of R. vemicifera stellacyanin.…”

Section: Spectroscopic Propertiesmentioning

confidence: 99%

Cloning, expression, and spectroscopic characterization of Cucumis sativus stellacyanin in its nonglycosylated form

et al. 1996

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The cDNA encoding the 182 amino acid long precursor stellacyanin from Cucumis sariwus was isolated and characterized. The protein precursor consists of four sequence domains: I, a 23 amino acid hydrophobic N-terminal signal peptide with features characteristic of secretory proteins; 11, a 109 amino acid copper-binding domain; 111, a 26 amino acid hydroxyproline-and serine-rich peptide characteristic of motifs found in the extensin family, extracellular structural glycoproteins found in plant cell walls; and IV, a 22 amino acid hydrophobic extension. Maturation of the protein involves posttranslational processing of domains I and IV. The copper-binding domain (domain 11), which shares high sequence identity with other stellacyanins, has been expressed without its carbohydrate attachment sites, refolded from the Escherichia coli inclusion bodies, purified, and characterized by electronic absorption, EPR, ESEEM, and RR spectroscopy. Its spectroscopic properties are nearly identical to those of stellacyanin from the Japanese lacquer tree Rhus verniciferu, the most extensively studied and best characterized stellacyanin, indicating that this domain folds correctly, even in the absence of its carbohydrate moiety. The presence of a hydroxyproline-and serine-rich domain I11 suggests that stellacyanin may have a function other than that of a diffusible electron transfer protein, conceivably participating in redox reactions localized at the plant cell wall, which are known to occur in response to wounding or infection of the plant.

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Variations in the Type I Copper Protein Coordination Group: Resonance Raman Spectrum of 34S-, 65Cu-, and 15N-Labeled Plastocyanin

Cited by 50 publications

References 1 publication

The Structure and Unusual pH Dependence of Plastocyanin from the Fern Dryopteris crassirhizoma

The Structure and Unusual pH Dependence of Plastocyanin from the Fern Dryopteris crassirhizoma

Electronic Structure of the Perturbed Blue Copper Site in Nitrite Reductase: Spectroscopic Properties, Bonding, and Implications for the Entatic/Rack State

Cloning, expression, and spectroscopic characterization of Cucumis sativus stellacyanin in its nonglycosylated form

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