Structures of oxidized and reduced azurin II from Alcaligenes xylosoxidans at 1.75 A resolution.

Crystallographic structures of oxidized and reduced forms of azurin II are reported at 1.75 A 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 confidence at current resolution. A comparison with the three-dimensional EXAFS reveals a good correspondence for all the ligand distances except for Cu-His46, where a larger deviation of approximately 0.12-0.18 A is observed, indicating that this ligand is more tightly restrained in the crystallographic refinement at the current resolution.

[1]  B. Roos,et al.  The cupric geometry of blue copper proteins is not strained. , 1996, Journal of molecular biology.

[2]  R J Williams,et al.  Energised (entatic) states of groups and of secondary structures in proteins and metalloproteins. , 1995, European journal of biochemistry.

[3]  E. Solomon,et al.  ELECTRONIC STRUCTURE OF THE REDUCED BLUE COPPER ACTIVE SITE : CONTRIBUTIONS TO REDUCTION POTENTIALS AND GEOMETRY , 1995 .

[4]  B. Malmström.  Rack-induced bonding in blue-copper proteins. , 1994, European journal of biochemistry.

[5]  D. Lowe,et al.  Purification and characterization of the dissimilatory nitrite reductase from Alcaligenes xylosoxidans subsp. xylosoxidans (N.C.I.M.B. 11015): evidence for the presence of both type 1 and type 2 copper centres. , 1993, The Biochemical journal.

[6]  J. G. Grossmann,et al.  X-ray scattering using synchrotron radiation shows nitrite reductase from Achromobacter xylosoxidans to be a trimer in solution. , 1993, Biochemistry.

[7]  J. Thornton,et al.  PROCHECK: a program to check the stereochemical quality of protein structures , 1993 .

[8]  A. Brunger.  Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. , 1992 .

[9]  R. Huber,et al.  Crystal structure analysis of oxidized Pseudomonas aeruginosa azurin at pH 5.5 and pH 9.0. A pH-induced conformational transition involves a peptide bond flip. , 1991, Journal of molecular biology.

[10]  R. Huber,et al.  Accurate Bond and Angle Parameters for X-ray Protein Structure Refinement , 1991 .

[11]  N. Sakabe.  X-ray diffraction data collection system for modern protein crystallography with a Weissenberg camera and an imaging plate using synchrotron radiation , 1991 .

[12]  J. Zou,et al.  Improved methods for building protein models in electron density maps and the location of errors in these models. , 1991, Acta crystallographica. Section A, Foundations of crystallography.

[13]  Edward N. Baker,et al.  Copper coordination geometry in azurin undergoes minimal change on reduction of copper(II) to copper(I) , 1990 .

[14]  E N Baker,et al.  Structure of azurin from Alcaligenes denitrificans refinement at 1.8 A resolution and comparison of the two crystallographically independent molecules. , 1987, Journal of molecular biology.

[15]  J. Guss,et al.  Crystal structure analyses of reduced (CuI) poplar plastocyanin at six pH values. , 1987, Journal of molecular biology.

[16]  M. C. Feiters,et al.  The pH and redox-state dependence of the copper site in azurin from Pseudomonas aeruginosa as studied by EXAFS. , 1986, Biochimica et biophysica acta.

[17]  Yoshiyuki Amemiya,et al.  A new type of X-ray area detector utilizing laser stimulated luminescence , 1986 .

[18]  R. Read.  Improved Fourier Coefficients for Maps Using Phases from Partial Structures with Errors , 1986 .

[19]  R. Marcus,et al.  Electron transfers in chemistry and biology , 1985 .

[20]  J. Guss,et al.  Structure of oxidized poplar plastocyanin at 1.6 A resolution. , 1983, Journal of molecular biology.

[21]  B F Anderson,et al.  Structure of azurin from Alcaligenes denitrificans at 2.5 A resolution. , 1983, Journal of molecular biology.

[22]  K. Hodgson,et al.  Polarized x-ray absorption spectra of oriented plastocyanin single crystals. Investigation of methionine-copper coordination , 1982 .

[23]  G. N. Ramachandran,et al.  Conformation of polypeptides and proteins. , 1968, Advances in protein chemistry.