The pH and redox-state dependence of the copper site in azurin from Pseudomonas aeruginosa as studied by EXAFS

Groeneveld, C. M.; Feiter, M.C.; Hasnain, S. Samar; Rijn, J. Van; Reedijk, Jan; Canters, Gerard W.

doi:10.1016/0167-4838(86)90048-8

Cited by 38 publications

(19 citation statements)

References 36 publications

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“…When looking at the data for oxidized amicyanin (Table II) Table III), although a Cu-N distance of 1.86-1.89 A is shorter than found in most cases (see Table III). A similar short Cu-N distance was obtained from the analysis of the Cu-EXAFS of P. aeruginosa azurin [32], somewhat at variance with the crystallographic data on azurin (see Table Ill). Also for plastocyanin EXAFS distances appear to be sfightly shorter than the crystallographically measured values [33].…”

Section: Copper Coordinationsupporting

confidence: 72%

EXAFS analysis of the pH dependence of the blue-copper site in amicyanin from Thiobacillus versutus

Lommen

Pandya

Koningsberger

et al. 1991

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

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The room temperature Cu K-edge EXAFS (extended X-ray absorption fine structure) spectrum of reduced and oxidized amicyanin, the blue copper protein from Thiobacillus versutus, was measured at low and high pH. The data interpretation was partly based on independent NMR evidence for the occurrence of a ligand histidine protonation at low pH (pKa = 6.9) in the reduced protein. In the oxidized protein two nitrogen-donors (from two histidines; Cu-N distances 1.95-2.01 A and 1.86-1.89 A) and a sulfur-donor (from a cysteine; Cu-S distance 2.11-2.13 A) were identified and the coordination appears independent of pH. Upon reduction at high pH the Cu-S bond and one of the Cu-N bonds lengthen slightly (from 2.11 to 2.19 A and from 2.01 to 2.18 A, respectively). Upon lowering of the pH one of the N-donors of the Cu in reduced amicyanin disappears from the Cu EXAFS and a second S-donor (from a methionine) becomes visible at 2.41 A from the Cu. The Debye-Waller factors are compatible with a Cu-N vibrational stretch frequency in the range of 150-250 cm-1 and one greater than 285 cm-1, and a Cu-S vibrational stretch frequency of about 150 cm-1 (Cu-Smet; reduced amicyanin at low pH) and one in the range of 230-800 cm-1 (Cu-Scys).

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Section: Copper Coordinationsupporting

confidence: 72%

EXAFS analysis of the pH dependence of the blue-copper site in amicyanin from Thiobacillus versutus

Lommen

Pandya

Koningsberger

et al. 1991

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

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“…Dodd et al, 2000); the exceptions being amicyanin (Durley et al, 1993) and plastocyanin (Guss et al, 1986), where at low pH one of the copper-ligating histidine is moved by nearly 1 A Ê . In contrast, EXAFS data have suggested a signi®cant change for azurins (Groenveld et al, 1986), while con®rming the dissociation of one of the His ligands in amicyanin (Lommen et al, 1991) and plastocyanin (Penner-Hahn et al, 1989; Murphy et al, 1991).…”

Section: Resultsmentioning

confidence: 99%

3D EXAFS refinement of the Cu site of azurin sheds light on the nature of structural change at the metal centre in an oxidation–reduction process: an integrated approach combining EXAFS and crystallography

Cheung

Strange

Hasnain

2000

Acta Crystallogr D Biol Cryst

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“…Such an environment should result in a lowering of the activation energy between the two redox states allowing rapid electron transfer to take place. To date, only AzAD has been studied crystallographically in the two redox states and, contrary to EXAFS results (Groenveld et al, 1986;Murphy et al, 1990), little or no structural change was detected at the Cu site upon reduction. In order to de®ne the upper limit of structural changes, both EXAFS and crystallographic studies have been carried out on azurin II.…”

Section: Introductionmentioning

confidence: 85%

Structures of oxidized and reduced azurin II fromAlcaligenes xylosoxidansat 1.75 Å resolution

Dodd

Abraham

Eady

et al. 2000

Acta Crystallogr D Biol Cryst

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Crystallographic structures of oxidized and reduced forms of azurin II are reported at 1.75 A Ê resolution. Data were collected using one crystal in each case and by translating the crystal after each oscillation range to minimize photoreduction. Very small differences are observed at the Cu site upon reduction and these cannot be determined with con®dence at current resolution. A comparison with the three-dimensional EXAFS reveals a good correspondence for all the ligand distances except for CuÐHis46, where a larger deviation of $0.12±0.18 A Ê is observed, indicating that this ligand is more tightly restrained in the crystallographic re®nement at the current resolution.

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The pH and redox-state dependence of the copper site in azurin from Pseudomonas aeruginosa as studied by EXAFS

Cited by 38 publications

References 36 publications

EXAFS analysis of the pH dependence of the blue-copper site in amicyanin from Thiobacillus versutus

EXAFS analysis of the pH dependence of the blue-copper site in amicyanin from Thiobacillus versutus

3D EXAFS refinement of the Cu site of azurin sheds light on the nature of structural change at the metal centre in an oxidation–reduction process: an integrated approach combining EXAFS and crystallography

Structures of oxidized and reduced azurin II fromAlcaligenes xylosoxidansat 1.75 Å resolution

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