For many streptomycetes, a distinct dependence on the “bioavailability” of copper ions for their morphological development has been reported. Analysis of the Streptomyces coelicolor genome reveals a number of gene products encoding for putative copper-binding proteins. One of these appears as an unusual copper-binding protein with a lipoprotein signal sequence and a cupredoxin-like domain harboring a putative Type-1 copper-binding motif. Cloning of this gene from S. coelicolor and subsequent heterologous expression in Escherichia coli has allowed for a thorough spectroscopic interrogation of this putative copper-binding protein. Optical and electron paramagnetic resonance spectroscopies have confirmed the presence of a “classic” Type-1 copper site with the axial ligand to the copper a methionine. Paramagnetic NMR spectroscopy on both the native Cu(II) form and Co(II)-substituted protein has yielded active-site structural information, which on comparison with that of other cupredoxin active sites reveals metal-ligand interactions most similar to the “classic” Type-1 copper site found in the amicyanin family of cupredoxins. Despite this high structural similarity, the Cu(II)/(I) midpoint potential of the S. coelicolor protein is an unprecedented +605 mV vs normal hydrogen electrode at neutral pH (amicyanin +250 mV), with no active-site protonation of the N-terminal His ligand observed. Suggestions for the physiological role/function of this high-potential cupredoxin are discussed.

Spectroscopic characterization of a high-potential Lipo-cupredoxin found in Streptomyces coelicolor / J. A. R., Worrall; M. C., Machczynski; B. J. F., Keijser; DI ROCCO, Giulia; S., Ceola; M., Ubbink; E., Vijenboom; G. W., Canters. - In: JOURNAL OF THE AMERICAN CHEMICAL SOCIETY. - ISSN 0002-7863. - ELETTRONICO. - 128 (45):(2006), pp. 14579-14589. [10.1021/ja064112n]

Spectroscopic characterization of a high-potential Lipo-cupredoxin found in Streptomyces coelicolor

DI ROCCO, Giulia;
2006

Abstract

For many streptomycetes, a distinct dependence on the “bioavailability” of copper ions for their morphological development has been reported. Analysis of the Streptomyces coelicolor genome reveals a number of gene products encoding for putative copper-binding proteins. One of these appears as an unusual copper-binding protein with a lipoprotein signal sequence and a cupredoxin-like domain harboring a putative Type-1 copper-binding motif. Cloning of this gene from S. coelicolor and subsequent heterologous expression in Escherichia coli has allowed for a thorough spectroscopic interrogation of this putative copper-binding protein. Optical and electron paramagnetic resonance spectroscopies have confirmed the presence of a “classic” Type-1 copper site with the axial ligand to the copper a methionine. Paramagnetic NMR spectroscopy on both the native Cu(II) form and Co(II)-substituted protein has yielded active-site structural information, which on comparison with that of other cupredoxin active sites reveals metal-ligand interactions most similar to the “classic” Type-1 copper site found in the amicyanin family of cupredoxins. Despite this high structural similarity, the Cu(II)/(I) midpoint potential of the S. coelicolor protein is an unprecedented +605 mV vs normal hydrogen electrode at neutral pH (amicyanin +250 mV), with no active-site protonation of the N-terminal His ligand observed. Suggestions for the physiological role/function of this high-potential cupredoxin are discussed.
128 (45)
14579
14589
Spectroscopic characterization of a high-potential Lipo-cupredoxin found in Streptomyces coelicolor / J. A. R., Worrall; M. C., Machczynski; B. J. F., Keijser; DI ROCCO, Giulia; S., Ceola; M., Ubbink; E., Vijenboom; G. W., Canters. - In: JOURNAL OF THE AMERICAN CHEMICAL SOCIETY. - ISSN 0002-7863. - ELETTRONICO. - 128 (45):(2006), pp. 14579-14589. [10.1021/ja064112n]
J. A. R., Worrall; M. C., Machczynski; B. J. F., Keijser; DI ROCCO, Giulia; S., Ceola; M., Ubbink; E., Vijenboom; G. W., Canters
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11380/625036
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