Two copper-containing proteins from cucumber (Cucumis sativus)

Markossian, Kira A.; Aikazyan, V.Ts.; Nalbandyan, R.M.

doi:10.1016/0005-2795(74)90130-5

Cited by 46 publications

(24 citation statements)

References 14 publications

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“…bacterial azurins [7], plastocyanin from higher plants [7], and umecyanin from horseradish [8], in that three g values are apparent rather than the two g values normally found. In this respect the copper-protein of the supernatant fraction resembles 'blue' copperproteins like stellacyanin, isolated from the Japanese lacquer tree [9], or plantacyanin, from cucumber [10] or spinach [ 11 ].…”

Section: Epr Properties Of Cells and The Blue Supernatant Fractionmentioning

confidence: 98%

The respiratory chain of Thiobacillus ferrooxidans: The reduction of cytochromes by Fe²⁺ and the preliminary characterization of rusticyanin a novel ‘blue’ copper protein

1975

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Section: Epr Properties Of Cells and The Blue Supernatant Fractionmentioning

confidence: 98%

The respiratory chain of Thiobacillus ferrooxidans: The reduction of cytochromes by Fe²⁺ and the preliminary characterization of rusticyanin a novel ‘blue’ copper protein

1975

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“…Plantacyanins (PNC) are extremely basic, nonglycosylated, single-domain proteins in their mature form. The protein from cucumber was first described in 1974 (Markossian et al, 1974) and over the past years they have been characterized from various plant species (Aikazyan & Nalbandyan, 1981;Sakurai, 1986;Nersissian & Nalbandyan, 1988). Plantacyanin from cucumber seed- (A) and kinetics of the autooxidation (B) of wild-type cucumber stellacyanin and its Q99M mutant.…”

Section: Am Nersissian Et Almentioning

confidence: 99%

Uclacyanins, stellacyanins, and plantacyanins are distinct subfamilies of phytocyanins: Plant‐specific mononuclear blue copper proteins

et al. 1998

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The cDNAs encoding plantacyanin from spinach were isolated and characterized. In addition, four new cDNA sequences from Arubidopsis ESTs were identified that encode polypeptides resembling phytocyanins, plant-specific proteins constituting a distinct family of mononuclear blue copper proteins. One of them encodes plantacyanin from Arubidopsis. while three others, designated as uclacyanin 1, 2, and 3, encode protein precursors that are closely related to precursors of stellacyanins and a blue copper protein from pea pods. Comparative analyses with known phytocyanins allow further classification of these proteins into three distinct subfamilies designated as uclacyanins, stellacyanins, and plantacyanins. This specification is based on (1) their spectroscopic properties, (2) their glycosylation state, (3) the domain organization of their precursors, and (4) their copper-binding amino acids. The recombinant copper binding domain of Arubidopsis uclacyanin I was expressed, purified, and shown to bind a copper atom in a fashion known as "blue" or type 1. The mutant of cucumber stellacyanin in which the glutamine axial ligand was substituted by a methionine (Q99M) was purified and shown to possess spectroscopic properties similar to uclacyanin I rather than to plantacyanins. Its redox potential was determined by cyclic voltammetry to be +420 mV, a value that is significantly higher than that determined for the wild-type protein (+260 mV). The available structural data suggest that stellacyanins (and possibly other phytocyanins) might not be diffusible electron-transfer proteins participating in long-range electron-transfer processes. Conceivably, they are involved in redox reactions occurring during primary defense responses in plants and/or in lignin formation.

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“…Plantacyanins, also known as cucumber basic protein, CBP, are strongly basic mononuclear blue copper proteins from plants (Markossian et al, 1974). According to the X-ray structural data, they have a methionine as an axial ligand rather than glutamine as in stellacyanin (Guss et al, 1988).…”

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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Two copper-containing proteins from cucumber (Cucumis sativus)

Cited by 46 publications

References 14 publications

The respiratory chain of Thiobacillus ferrooxidans: The reduction of cytochromes by Fe²⁺ and the preliminary characterization of rusticyanin a novel ‘blue’ copper protein

The respiratory chain of Thiobacillus ferrooxidans: The reduction of cytochromes by Fe²⁺ and the preliminary characterization of rusticyanin a novel ‘blue’ copper protein

Uclacyanins, stellacyanins, and plantacyanins are distinct subfamilies of phytocyanins: Plant‐specific mononuclear blue copper proteins

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

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Two copper-containing proteins from cucumber (Cucumis sativus)

Cited by 46 publications

References 14 publications

The respiratory chain of Thiobacillus ferrooxidans: The reduction of cytochromes by Fe2+ and the preliminary characterization of rusticyanin a novel ‘blue’ copper protein

The respiratory chain of Thiobacillus ferrooxidans: The reduction of cytochromes by Fe2+ and the preliminary characterization of rusticyanin a novel ‘blue’ copper protein

Uclacyanins, stellacyanins, and plantacyanins are distinct subfamilies of phytocyanins: Plant‐specific mononuclear blue copper proteins

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

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The respiratory chain of Thiobacillus ferrooxidans: The reduction of cytochromes by Fe²⁺ and the preliminary characterization of rusticyanin a novel ‘blue’ copper protein

The respiratory chain of Thiobacillus ferrooxidans: The reduction of cytochromes by Fe²⁺ and the preliminary characterization of rusticyanin a novel ‘blue’ copper protein