Hydrogen Bonding in the Blue-Copper Site. Resonance Raman Study

Hydrogen Bonding in the Blue-Copper Site. Resonance Raman Study

The blue-copper proteins azurin from Pseudomonas aeruginosa, azurin from Alcaligenes denitrificans, and the mutant Met121Gln of azurin from Alcaligenes denitrificans have been investigated by resonance Raman spectroscopy. Large deuterium isotope shifts up to 6 cm-1 have been observed for bands in th...

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Veröffentlicht in:The journal of physical chemistry. B 2002-04, Vol.106 (15), p.4018-4021
Hauptverfasser: van Gastel, M, Nagano, Y, Zondervan, R, Canters, G. W, Jeuken, L. J. C, Warmerdam, G. C. M, de Waal, E. C, Groenen, E. J. J
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container_end_page 4021
container_issue 15
container_start_page 4018
container_title The journal of physical chemistry. B
container_volume 106
creator van Gastel, M
Nagano, Y
Zondervan, R
Canters, G. W
Jeuken, L. J. C
Warmerdam, G. C. M
de Waal, E. C
Groenen, E. J. J
description The blue-copper proteins azurin from Pseudomonas aeruginosa, azurin from Alcaligenes denitrificans, and the mutant Met121Gln of azurin from Alcaligenes denitrificans have been investigated by resonance Raman spectroscopy. Large deuterium isotope shifts up to 6 cm-1 have been observed for bands in the 350−460 cm-1 range after incubation of the apoproteins in D2O and subsequent reconstitution with copper. The shifts derive from the deuteration of the amide hydrogens of Asn47 and Phe114 that form a hydrogen bond with the sulfur of the copper-coordinated cysteine. This observation reveals the coupling of the copper−sulfur and sulfur−hydrogen vibrations and indicates that these amide groups have to be taken into account to properly describe the electronic structure of the blue-copper site.
doi_str_mv 10.1021/jp013839p
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