Impact of copper ligand mutations on a cupredoxin with a green copper center.

[1]  D. Stahl,et al.  A Purple Cupredoxin from Nitrosopumilus maritimus Containing a Mononuclear Type 1 Copper Center with an Open Binding Site. , 2016, Journal of the American Chemical Society.

[2]  L. Alcaraz,et al.  Blue Copper Proteins: A rigid machine for efficient electron transfer, a flexible device for metal uptake. , 2015, Archives of biochemistry and biophysics.

[3]  Lucas B. Harrington,et al.  Site-directed mutagenesis of the highly perturbed copper site of auracyanin D. , 2014, Archives of biochemistry and biophysics.

[4]  G. Sciara,et al.  Spectroscopic Characterization of a Green Copper Site in a Single-Domain Cupredoxin , 2014, PloS one.

[5]  Yi Lu,et al.  Metalloproteins Containing Cytochrome, Iron–Sulfur, or Copper Redox Centers , 2014, Chemical reviews.

[6]  Li Tian,et al.  Copper active sites in biology. , 2014, Chemical reviews.

[7]  M. dal Peraro,et al.  Molecular dynamics simulations of apocupredoxins: insights into the formation and stabilization of copper sites under entatic control , 2014, JBIC Journal of Biological Inorganic Chemistry.

[8]  Robert Eugene Blankenship,et al.  Metalloproteins diversified: the auracyanins are a family of cupredoxins that stretch the spectral and redox limits of blue copper proteins. , 2013, Biochemistry.

[9]  M. Roger,et al.  Mineral respiration under extreme acidic conditions: from a supramolecular organization to a molecular adaptation in Acidithiobacillus ferrooxidans. , 2012, Biochemical Society transactions.

[10]  M. Zaballa,et al.  Flexibility of the metal-binding region in apo-cupredoxins , 2012, Proceedings of the National Academy of Sciences.

[11]  V. Davidson,et al.  Cupredoxins--a study of how proteins may evolve to use metals for bioenergetic processes. , 2011, Metallomics : integrated biometal science.

[12]  Kevin M. Clark,et al.  Transforming a blue copper into a red copper protein: engineering cysteine and homocysteine into the axial position of azurin using site-directed mutagenesis and expressed protein ligation. , 2010, Journal of the American Chemical Society.

[13]  M. Ilbert,et al.  An Unconventional Copper Protein Required for Cytochrome c Oxidase Respiratory Function under Extreme Acidic Conditions , 2010, The Journal of Biological Chemistry.

[14]  Kathleen S. McGreevy,et al.  Cellular copper management—a draft user's guide , 2010 .

[15]  A. Dey,et al.  Thermodynamic equilibrium between blue and green copper sites and the role of the protein in controlling function , 2009, Proceedings of the National Academy of Sciences.

[16]  Jianshe Liu,et al.  The sulfhydryl group of Cys138 of rusticyanin from Acidithiobacillus ferrooxidans is crucial for copper binding. , 2007, Biochimica et biophysica acta.

[17]  V. Davidson,et al.  Generation of novel copper sites by mutation of the axial ligand of amicyanin. Atomic resolution structures and spectroscopic properties. , 2007, Biochemistry.

[18]  C. Dennison,et al.  Engineering copper sites in proteins: loops confer native structures and properties to chimeric cupredoxins. , 2007, Journal of the American Chemical Society.

[19]  Yi Lu,et al.  Reduction potential tuning of the blue copper center in Pseudomonas aeruginosa azurin by the axial methionine as probed by unnatural amino acids. , 2006, Journal of the American Chemical Society.

[20]  E. Solomon,et al.  Spectroscopic methods in bioinorganic chemistry: blue to green to red copper sites. , 2006, Inorganic chemistry.

[21]  Hein J. Wijma,et al.  A rearranging ligand enables allosteric control of catalytic activity in copper-containing nitrite reductase. , 2006, Journal of molecular biology.

[22]  R. Strange,et al.  Atomic resolution crystal structures, EXAFS, and quantum chemical studies of rusticyanin and its two mutants provide insight into its unusual properties. , 2006, Biochemistry.

[23]  C. Dennison.  Investigating the structure and function of cupredoxins , 2005 .

[24]  M. J. Ellis,et al.  High resolution structural studies of mutants provide insights into catalysis and electron transfer processes in copper nitrite reductase. , 2005, Journal of molecular biology.

[25]  K. Hodgson,et al.  Spectroscopic and density functional studies of the red copper site in nitrosocyanin: role of the protein in determining active site geometric and electronic structure. , 2005, Journal of the American Chemical Society.

[26]  C. Chothia,et al.  The linked conservation of structure and function in a family of high diversity: the monomeric cupredoxins. , 2004, Structure.

[27]  Robert K Szilagyi,et al.  Electronic structures of metal sites in proteins and models: contributions to function in blue copper proteins. , 2004, Chemical reviews.

[28]  E. Solomon,et al.  Spectroscopic studies of the Met182Thr mutant of nitrite reductase: role of the axial ligand in the geometric and electronic structure of blue and green copper sites. , 2003, Journal of the American Chemical Society.

[29]  Yi Lu,et al.  Probing the role of axial methionine in the blue copper center of azurin with unnatural amino acids. , 2003, Journal of the American Chemical Society.

[30]  K. Hodgson,et al.  Spectroscopic investigation of stellacyanin mutants: axial ligand interactions at the blue copper site. , 2003, Journal of the American Chemical Society.

[31]  Hein J. Wijma,et al.  Reconstitution of the type-1 active site of the H145G/A variants of nitrite reductase by ligand insertion. , 2003, Biochemistry.

[32]  L. Krippahl,et al.  Electrochemical studies on small electron transfer proteins using membrane electrodes , 2003 .

[33]  A. Hooper,et al.  Nitrosocyanin, a red cupredoxin-like protein from Nitrosomonas europaea. , 2002, Biochemistry.

[34]  M. J. Ellis,et al.  Biochemical and crystallographic studies of the Met144Ala, Asp92Asn and His254Phe mutants of the nitrite reductase from Alcaligenes xylosoxidans provide insight into the enzyme mechanism. , 2002, Journal of molecular biology.

[35]  A. Rosenzweig,et al.  Crystal structure of a novel red copper protein from Nitrosomonas europaea. , 2001, Biochemistry.

[36]  Lars J. C. Jeuken,et al.  Role of the Surface-Exposed and Copper-Coordinating Histidine in Blue Copper Proteins: The Electron-Transfer and Redox-Coupled Ligand Binding Properties of His117Gly Azurin , 2000 .

[37]  A. Messerschmidt,et al.  Axial Ligation in Blue-Copper Proteins. A W-Band Electron Spin Echo Detected Electron Paramagnetic Resonance Study of the Azurin Mutant M121H , 2000 .

[38]  R. Strange,et al.  Role of the axial ligand in type 1 Cu centers studied by point mutations of met148 in rusticyanin. , 1999, Biochemistry.

[39]  C. Scholes,et al.  Spectroscopic, kinetic, and electrochemical characterization of heterologously expressed wild-type and mutant forms of copper-containing nitrite reductase from Rhodobacter sphaeroides 2.4.3. , 1998, Biochemistry.

[40]  H. Gray,et al.  Paramagnetic NMR Spectroscopy of Cobalt(II) and Copper(II) Derivatives of Pseudomonas aeruginosa His46Asp Azurin. , 1997, Inorganic chemistry.

[41]  A. Sannazzaro,et al.  Alkaline transition of Rhus vernicifera stellacyanin, an unusual blue copper protein. , 1997, Biochemistry.

[42]  H. Nar,et al.  X-ray structure determination and characterization of the Pseudomonas aeruginosa azurin mutant Met121Glu. , 1997, Biochemistry.

[43]  R. Strange,et al.  Effect of pH and ligand binding on the structure of the Cu site of the Met121Glu mutant of azurin from Pseudomonas aeruginosa. , 1996, Biochemistry.

[44]  David Eisenberg,et al.  A missing link in cupredoxins: Crystal structure of cucumber stellacyanin at 1.6 Å resolution , 1996, Protein science : a publication of the Protein Society.

[45]  K. Harata,et al.  Mutant Met121Ala of Pseudomonas aeruginosa azurin and its azide derivative: crystal structures and spectral properties. , 1996, Acta crystallographica. Section D, Biological crystallography.

[46]  W. Hagen,et al.  The mutation Met121-->His creates a type-1.5 copper site in Alcaligenes denitrificans azurin. , 1996, European journal of biochemistry.

[47]  K. Hodgson,et al.  Electronic structure of the perturbed blue copper site in nitrite reductase: spectroscopic properties, bonding and implications for the entatic/rack state. , 1996 .

[48]  N. Bonander,et al.  Environment of copper in Pseudomonas aeruginosa azurin probed by binding of exogenous ligands to Met121X (X = Gly, Ala, Val, Leu, or Asp) mutants. , 1996, Biochemistry.

[49]  H. Hill,et al.  Spectroscopic and mechanistic studies of type-1 and type-2 copper sites in Pseudomonas aeruginosa azurin as obtained by addition of external ligands to mutant His46Gly. , 1996, Biochemistry.

[50]  J. Germanas,et al.  Novel Biological Copper Proteins through Anion Addition to the Mutant Met121Gly of Pseudomonas aeruginosa Azurin , 1995 .

[51]  H. Dyson,et al.  Gene synthesis, high-level expression, and mutagenesis of Thiobacillus ferrooxidans rusticyanin: His 85 is a ligand to the blue copper center. , 1995, Biochemistry.

[52]  G. Gilardi,et al.  Engineering type 1 copper sites in proteins , 1993, FEBS letters.

[53]  T. Pascher,et al.  Reduction potentials and their pH dependence in site-directed-mutant forms of azurin from Pseudomonas aeruginosa. , 1993, European journal of biochemistry.

[54]  G. Canters,et al.  Creation of type-1 and type-2 copper sites by addition of exogenous ligands to the Pseudomonas aeruginosa azurin His117Gly mutant , 1993 .

[55]  Tanneke den Blaauwen,et al.  Type I and II copper sites obtained by external addition of ligands to a His117Gly azurin mutant , 1991 .

[56]  T. Pascher,et al.  Cassette mutagenesis of Met121 in azurin from Pseudomonas aeruginosa. , 1991, Protein engineering.

[57]  J. Peisach,et al.  Structural implications derived from the analysis of electron paramagnetic resonance spectra of natural and artificial copper proteins. , 1974, Archives of biochemistry and biophysics.

[58]  A. Nersissian,et al.  Blue copper-binding domains. , 2002, Advances in protein chemistry.

[59]  C. Buning,et al.  Loop-Directed Mutagenesis of the Blue Copper Protein Amicyanin from Paracoccus versutus and Its Effect on the Structure and the Activity of the Type-1 Copper Site , 2000 .

[60]  E T Adman,et al.  Copper protein structures. , 1991, Advances in protein chemistry.