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X-ray Structure of the Cupredoxin Amicyanin, fromParacoccus denitrificans, Refined at 1.31 Å Resolution

https://doi.org/10.1107/s0907444996001072
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Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/cbf.290120313openalex-snapshot
Topics in molecular and structural biology
inferredcites →https://doi.org/10.5860/choice.37-0940openalex-snapshot
Advanced inorganic chemistry

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.2139/ssrn.4766630openalex-extracted
Examining the Impact of Water Molecules in Regulating Amicyanin Protein's Function: A Computational Study
inferred← citeshttps://doi.org/10.1002/chem.200701997openalex-snapshot
The Importance of the Long Type 1 Copper‐Binding Loop of Nitrite Reductase for Structure and Function
inferred← citeshttps://doi.org/10.1002/prot.22204openalex-snapshot
Molecular dynamics of amicyanin reveals a conserved dynamical core for blue copper proteins
inferred← citeshttps://doi.org/10.1007/0-306-46828-x_4openalex-snapshot
Methylamine Dehydrogenase Structure and Function of Electron Transfer Complexes
inferred← citeshttps://doi.org/10.1007/978-94-011-5133-7_10openalex-snapshot
Structural Research on the Methylamine Dehydrogenase Redox Chain of Paracoccus Denitrificans
inferred← citeshttps://doi.org/10.1016/b0-08-043748-6/08172-xopenalex-snapshot
Electron Transfer: Cupredoxins
inferred← citeshttps://doi.org/10.1016/b978-0-08-102688-5.08172-1openalex-snapshot
Classic Perspectives - Electron Transfer: Cupredoxins
inferred← citeshttps://doi.org/10.1016/j.abb.2014.03.010openalex-snapshot
The sole tryptophan of amicyanin enhances its thermal stability but does not influence the electronic properties of the type 1 copper site
inferred← citeshttps://doi.org/10.1016/j.ccr.2004.03.019openalex-snapshot
Atomic resolution crystallography and XAFS
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2011.08.002openalex-snapshot
Replacement of the axial copper ligand methionine with lysine in amicyanin converts it to a zinc-binding protein that no longer binds copper
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2012.05.002openalex-snapshot
Inner- and outer-sphere metal coordination in blue copper proteins
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2017.11.016openalex-snapshot
Relaxation of structural constraints during Amicyanin unfolding
inferred← citeshttps://doi.org/10.1016/j.sbi.2006.02.001openalex-snapshot
Conformer generation under restraints
inferred← citeshttps://doi.org/10.1016/j.str.2004.02.031openalex-snapshot
Heterogeneity and Inaccuracy in Protein Structures Solved by X-Ray Crystallography
inferred← citeshttps://doi.org/10.1016/s0022-2836(02)00443-6openalex-snapshot
Crystal Structures of the Met148Leu and Ser86Asp Mutants of Rusticyanin from Thiobacillus ferrooxidans: Insights into the Structural Relationship with the Cupredoxins and the Multi Copper Proteins
inferred← citeshttps://doi.org/10.1016/s0162-0134(02)00364-1openalex-snapshot
An outer-sphere hydrogen-bond network constrains copper coordination in blue proteins
inferred← citeshttps://doi.org/10.1016/s1381-1177(99)00065-xopenalex-snapshot
Coping with formaldehyde during C1 metabolism of Paracoccus denitrificans
inferred← citeshttps://doi.org/10.1021/acs.jpcb.8b07130openalex-snapshot
Geometrical Description of Protein Structural Motifs
inferred← citeshttps://doi.org/10.1021/bi001971uopenalex-snapshot
Electronic Characterization of the Oxidized State of the Blue Copper Protein Rusticyanin by 1H NMR: Is the Axial Methionine the Dominant Influence for the High Redox Potential?
inferred← citeshttps://doi.org/10.1021/bi101794yopenalex-snapshot
Proline 96 of the Copper Ligand Loop of Amicyanin Regulates Electron Transfer from Methylamine Dehydrogenase by Positioning Other Residues at the Protein−Protein Interface
inferred← citeshttps://doi.org/10.1021/bi700303eopenalex-snapshot
Correlation of Rhombic Distortion of the Type 1 Copper Site of M98Q Amicyanin with Increased Electron Transfer Reorganization Energy
inferred← citeshttps://doi.org/10.1021/cr400479bopenalex-snapshot
Metalloproteins Containing Cytochrome, Iron–Sulfur, or Copper Redox Centers
inferred← citeshttps://doi.org/10.1021/ja0267019openalex-snapshot
Metal−Ligand Interplay in Blue Copper Proteins Studied by 1H NMR Spectroscopy: Cu(II)−Pseudoazurin and Cu(II)−Rusticyanin
inferred← citeshttps://doi.org/10.1021/ja0661562openalex-snapshot
Engineering Copper Sites in Proteins: Loops Confer Native Structures and Properties to Chimeric Cupredoxins
inferred← citeshttps://doi.org/10.1021/ja075978bopenalex-snapshot
NMR Hyperfine Shifts in Blue Copper Proteins: A Quantum Chemical Investigation
inferred← citeshttps://doi.org/10.1021/ja8038135openalex-snapshot
π-Interaction Tuning of the Active Site Properties of Metalloproteins
inferred← citeshttps://doi.org/10.1021/jacs.5c07009openalex-snapshot
Beyond Blue: Systematic Modulation of Electronic Structure and Redox Properties of Type 1 Copper in Azurin
inferred← citeshttps://doi.org/10.1039/b707987gopenalex-snapshot
The role of ligand-containing loops at copper sites in proteins
inferred← citeshttps://doi.org/10.1039/c8sc01444bopenalex-snapshot
Engineering a bifunctional copper site in the cupredoxin fold by loop-directed mutagenesis
inferred← citeshttps://doi.org/10.1039/d0sc01620aopenalex-snapshot
Cu A -based chimeric T1 copper sites allow for independent modulation of reorganization energy and reduction potential
inferred← citeshttps://doi.org/10.1039/d1dt04387kopenalex-snapshot
On the roles of methionine and the importance of its microenvironments in redox metalloproteins
inferred← citeshttps://doi.org/10.1039/d3dt03372dopenalex-snapshot
Beyond the coupled distortion model: structural analysis of the single domain cupredoxin AcoP, a green mononuclear copper centre with original features
inferred← citeshttps://doi.org/10.1073/pnas.0600774103openalex-snapshot
Basic requirements for a metal-binding site in a protein: The influence of loop shortening on the cupredoxin azurin
inferred← citeshttps://doi.org/10.1073/pnas.0811324106openalex-snapshot
Metal-binding loop length and not sequence dictates structure
inferred← citeshttps://doi.org/10.1073/pnas.0912672107openalex-snapshot
A joint x-ray and neutron study on amicyanin reveals the role of protein dynamics in electron transfer
inferred← citeshttps://doi.org/10.1074/jbc.m308863200openalex-snapshot
An Engineered CuA Amicyanin Capable of Intermolecular Electron Transfer Reactions
inferred← citeshttps://doi.org/10.1080/08927022.2026.2660823openalex-snapshot
Exploring the influence of water molecules on modulating the functional dynamics of amicyanin: a computational investigation
inferred← citeshttps://doi.org/10.1093/jb/mvm136openalex-snapshot
Identification of a Blue Copper Protein from Hyphomicrobium denitrificans and its Functions in the Periplasm
inferred← citeshttps://doi.org/10.1139/w2012-020openalex-snapshot
Purification and characterization of azurin from the methylamine-utilizing obligate methylotrophMethylobacillus flagellatusKT
inferred← citeshttps://doi.org/10.1371/journal.pcbi.1006547openalex-snapshot
Motif-Aware PRALINE: Improving the alignment of motif regions
inferred← citeshttps://doi.org/10.5796/electrochemistry.21-00030openalex-snapshot
Electrochemical Consideration of Electrostatic Interaction of Charged Molecules with Partially Overlapped Electric Field: Zwitterions and Proteins
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