Published in J Am Chem Soc on September 19, 2012
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Direct metal transfer between periplasmic proteins identifies a bacterial copper chaperone. Biochemistry (2008) 1.44
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X-ray absorption spectroscopy of the copper chaperone HAH1 reveals a linear two-coordinate Cu(I) center capable of adduct formation with exogenous thiols and phosphines. J Biol Chem (2003) 1.38
Human Sco1 and Sco2 function as copper-binding proteins. J Biol Chem (2005) 1.37
Yeast Sco1, a protein essential for cytochrome c oxidase function is a Cu(I)-binding protein. J Biol Chem (2001) 1.31
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Spectroscopic studies of metal binding and metal selectivity in Bacillus subtilis BSco, a Homologue of the Yeast Mitochondrial Protein Sco1p. J Am Chem Soc (2005) 1.17
Probing the role of axial methionine in the blue copper center of azurin with unnatural amino acids. J Am Chem Soc (2003) 1.15
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Crystal structure of a novel red copper protein from Nitrosomonas europaea. Biochemistry (2001) 0.97
Selenomethionine-substituted Thermus thermophilus cytochrome ba3: characterization of the CuA site by Se and Cu K-EXAFS. Biochemistry (1999) 0.95
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. J Am Chem Soc (2003) 0.94
A selenocysteine variant of the human copper chaperone for superoxide dismutase. A Se-XAS probe of cluster composition at the domain 3-domain 3 dimer interface. Biochemistry (2008) 0.91
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. J Am Chem Soc (2010) 0.91
Experimental evidence for a link among cupredoxins: red, blue, and purple copper transformations in nitrous oxide reductase. Proc Natl Acad Sci U S A (2008) 0.90
H135A controls the redox activity of the Sco copper center. Kinetic and spectroscopic studies of the His135Ala variant of Bacillus subtilis Sco. Biochemistry (2009) 0.90
The roles of Rhodobacter sphaeroides copper chaperones PCu(A)C and Sco (PrrC) in the assembly of the copper centers of the aa(3)-type and the cbb(3)-type cytochrome c oxidases. Biochim Biophys Acta (2012) 0.84
The essential role of the Cu(II) state of Sco in the maturation of the Cu(A) center of cytochrome oxidase: evidence from H135Met and H135SeM variants of the Bacillus subtilis Sco. J Biol Inorg Chem (2010) 0.84
Cu(A) centers and their biosynthetic models in azurin. J Biol Inorg Chem (2010) 0.83
Metal-binding properties of an engineered purple CuA center in azurin. J Biol Inorg Chem (2000) 0.82
Kinetics of copper incorporation into a biosynthetic purple Cu(A) azurin: characterization of red, blue, and a new intermediate species. J Am Chem Soc (2011) 0.81
Selenocysteine positional variants reveal contributions to copper binding from cysteine residues in domains 2 and 3 of human copper chaperone for superoxide dismutase. Biochemistry (2008) 0.80
Three-dimensional structure of the human copper transporter hCTR1. Proc Natl Acad Sci U S A (2009) 1.79
Unusual Cu(I)/Ag(I) coordination of Escherichia coli CusF as revealed by atomic resolution crystallography and X-ray absorption spectroscopy. Protein Sci (2007) 1.71
Direct metal transfer between periplasmic proteins identifies a bacterial copper chaperone. Biochemistry (2008) 1.44
Hydrogen tunneling in peptidylglycine alpha-hydroxylating monooxygenase. J Am Chem Soc (2002) 1.42
Substrate-linked conformational change in the periplasmic component of a Cu(I)/Ag(I) efflux system. J Biol Chem (2007) 1.41
Synthesis and X-ray absorption spectroscopy structural studies of Cu(I) complexes of histidylhistidine peptides: the predominance of linear 2-coordinate geometry. J Am Chem Soc (2007) 1.40
The N-terminal metal-binding site 2 of the Wilson's Disease Protein plays a key role in the transfer of copper from Atox1. J Biol Chem (2004) 1.38
X-ray absorption spectroscopy of the copper chaperone HAH1 reveals a linear two-coordinate Cu(I) center capable of adduct formation with exogenous thiols and phosphines. J Biol Chem (2003) 1.38
Structural studies of copper(I) complexes of amyloid-beta peptide fragments: formation of two-coordinate bis(histidine) complexes. Angew Chem Int Ed Engl (2008) 1.17
Spectroscopic studies of metal binding and metal selectivity in Bacillus subtilis BSco, a Homologue of the Yeast Mitochondrial Protein Sco1p. J Am Chem Soc (2005) 1.17
Probing the role of axial methionine in the blue copper center of azurin with unnatural amino acids. J Am Chem Soc (2003) 1.15
Oxygen and hydrogen isotope effects in an active site tyrosine to phenylalanine mutant of peptidylglycine alpha-hydroxylating monooxygenase: mechanistic implications. Biochemistry (2003) 1.13
The selenocysteine-substituted blue copper center: spectroscopic investigations of Cys112SeCys Pseudomonas aeruginosa azurin. J Am Chem Soc (2004) 1.09
The hydrogen peroxide reactivity of peptidylglycine monooxygenase supports a Cu(II)-superoxo catalytic intermediate. J Biol Chem (2005) 1.03
Anatomy of a red copper center: spectroscopic identification and reactivity of the copper centers of Bacillus subtilis Sco and its Cys-to-Ala variants. J Am Chem Soc (2010) 1.01
A multinuclear copper(I) cluster forms the dimerization interface in copper-loaded human copper chaperone for superoxide dismutase. Biochemistry (2007) 0.99
The catalytic copper of peptidylglycine alpha-hydroxylating monooxygenase also plays a critical structural role. Biophys J (2005) 0.97
The catalytic role of the copper ligand H172 of peptidylglycine alpha-hydroxylating monooxygenase: a kinetic study of the H172A mutant. Biochemistry (2006) 0.95
The copper centers of tyramine β-monooxygenase and its catalytic-site methionine variants: an X-ray absorption study. J Biol Inorg Chem (2010) 0.93
Interactions between copper-binding sites determine the redox status and conformation of the regulatory N-terminal domain of ATP7B. J Biol Chem (2009) 0.92
A copper-methionine interaction controls the pH-dependent activation of peptidylglycine monooxygenase. Biochemistry (2011) 0.91
A selenocysteine variant of the human copper chaperone for superoxide dismutase. A Se-XAS probe of cluster composition at the domain 3-domain 3 dimer interface. Biochemistry (2008) 0.91
The catalytic role of the copper ligand H172 of peptidylglycine alpha-hydroxylating monooxygenase (PHM): a spectroscopic study of the H172A mutant. Biochemistry (2002) 0.91
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. J Am Chem Soc (2010) 0.91
pH Dependence of peptidylglycine monooxygenase. Mechanistic implications of Cu-methionine binding dynamics. Biochemistry (2006) 0.91
The lumenal loop Met672-Pro707 of copper-transporting ATPase ATP7A binds metals and facilitates copper release from the intramembrane sites. J Biol Chem (2011) 0.90
H135A controls the redox activity of the Sco copper center. Kinetic and spectroscopic studies of the His135Ala variant of Bacillus subtilis Sco. Biochemistry (2009) 0.90
Tryptophan Cu(I)-pi interaction fine-tunes the metal binding properties of the bacterial metallochaperone CusF. J Biol Inorg Chem (2009) 0.89
N-terminal region of CusB is sufficient for metal binding and metal transfer with the metallochaperone CusF. Biochemistry (2012) 0.87
Metal export by CusCFBA, the periplasmic Cu(I)/Ag(I) transport system of Escherichia coli. Curr Top Membr (2012) 0.87
Large scale production of the copper enzyme peptidylglycine monooxygenase using an automated bioreactor. Protein Expr Purif (2006) 0.86
Lumenal loop M672-P707 of the Menkes protein (ATP7A) transfers copper to peptidylglycine monooxygenase. J Am Chem Soc (2012) 0.85
Heme-copper/dioxygen adduct formation relevant to cytochrome c oxidase: spectroscopic characterization of [(6L)FeIII-(O2(2-))-CuII]+. J Biol Inorg Chem (2004) 0.85
Cysteine-to-serine mutants of the human copper chaperone for superoxide dismutase reveal a copper cluster at a domain III dimer interface. Biochemistry (2005) 0.85
Role for an essential tyrosine in peptide amidation. J Biol Chem (2006) 0.84
The essential role of the Cu(II) state of Sco in the maturation of the Cu(A) center of cytochrome oxidase: evidence from H135Met and H135SeM variants of the Bacillus subtilis Sco. J Biol Inorg Chem (2010) 0.84
HHM motif at the CuH-site of peptidylglycine monooxygenase is a pH-dependent conformational switch. Biochemistry (2013) 0.84
Copper transfer to the N-terminal domain of the Wilson disease protein (ATP7B): X-ray absorption spectroscopy of reconstituted and chaperone-loaded metal binding domains and their interaction with exogenous ligands. J Inorg Biochem (2004) 0.84
Interdomain long-range electron transfer becomes rate-limiting in the Y216A variant of tyramine β-monooxygenase. Biochemistry (2013) 0.84
Binding of copper and silver to single-site variants of peptidylglycine monooxygenase reveals the structure and chemistry of the individual metal centers. Biochemistry (2014) 0.83
Selenocysteine positional variants reveal contributions to copper binding from cysteine residues in domains 2 and 3 of human copper chaperone for superoxide dismutase. Biochemistry (2008) 0.80
Alternative ground states enable pathway switching in biological electron transfer. Proc Natl Acad Sci U S A (2012) 0.79
Copper-peptide complex structure and reactivity when found in conserved His-X(aa)-His sequences. J Am Chem Soc (2014) 0.78
Structure and coordination of CuB in the Acidianus ambivalens aa3 quinol oxidase heme-copper center. J Biol Inorg Chem (2005) 0.75