ArticleProceedings of the National Academy of Sciences of the United States of America2012
Flexibility of the metal-binding region in apo-cupredoxins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- A designed Copper Histidine-brace enzyme for oxidative depolymerization of polysaccharides as a model of lytic polysaccharide monooxygenase.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- In-cell kinetic stability is an essential trait in metallo-β-lactamase evolution.Nature chemical biology · 2023Article
- Design of a Flexible, Zn-Selective Protein Scaffold that Displays Anti-Irving-Williams Behavior.Journal of the American Chemical Society · 2022Article
- Orchestrating copper binding: structure and variations on the cupredoxin fold.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022Review
- Frustration Dynamics and Electron-Transfer Reorganization Energies in Wild-Type and Mutant Azurins.Journal of the American Chemical Society · 2022Article
- Biochemistry of Copper Site Assembly in Heme-Copper Oxidases: A Theme with Variations.International journal of molecular sciences · 2019Review
- DEPC modification of the CuJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019Article
- Characterization and effect of metal ions on the formation of the Thermus thermophilus Sco mixed disulfide intermediate.Protein science : a publication of the Protein Society · 2018Article
- Engineering a bifunctional copper site in the cupredoxin fold by loop-directed mutagenesis.Chemical science · 2018Article
- Mitochondrial cytochrome c oxidase biogenesis: Recent developments.Seminars in cell & developmental biology · 2018Review
- Walking the seven lines: binuclear copper A in cytochrome c oxidase and nitrous oxide reductase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Review
- Stabilization of protein structure through π-π interaction in the second coordination sphere of pseudoazurin.Protein science : a publication of the Protein Society · 2017Article
- The structural flexibility of the human copper chaperone Atox1: Insights from combined pulsed EPR studies and computations.Protein science : a publication of the Protein Society · 2017Article
- Loop recognition and copper-mediated disulfide reduction underpin metal site assembly of CuA in human cytochrome oxidase.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Electron Transfer Proteins as Electronic Conductors: Significance of the Metal and Its Binding Site in the Blue Cu Protein, Azurin.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2015Article
- Molecular dynamics simulations of apocupredoxins: insights into the formation and stabilization of copper sites under entatic control.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Article
- Modulating the Copper-Sulfur Interaction in Type 1 Blue Copper Azurin by Replacing Cys112 with Nonproteinogenic Homocysteine.Inorganic chemistry frontiers · 2014Article
- Redox state dependence of axial ligand dynamics in Nitrosomonas europaea cytochrome c552.The journal of physical chemistry. B · 2013Article
- Antimalarial activity of cupredoxins: the interaction of Plasmodium merozoite surface protein 119 (MSP119) and rusticyanin.The Journal of biological chemistry · 2013Article
- A new structural paradigm in copper resistance in Streptococcus pneumoniae.Nature chemical biology · 2013Article
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4 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Protein-mediated electron transfer is an essential event in many biochemical processes. Efficient electron transfer requires the reorganization energy of the redox event to be minimized, which is ensured by the presence of rigid donor and acceptor sites. Electron transfer copper sites are present in the ubiquitous cupredoxin fold, able to bind one or two copper ions. The low reorganization energy in these metal centers has been accounted for by assuming that the protein scaffold creates an entatic/rack-induced state, which gives rise to a rigid environment by means of a preformed metal chelating site. However, this notion is incompatible with the need for an exposed metal-binding site and protein-protein interactions enabling metallochaperone-mediated assembly of the copper site. Here we report an NMR study that reveals a high degree of structural heterogeneity in the metal-binding region of the nonmetallated Cu(A)-binding cupredoxin domain, arising from microsecond to second dynamics that are quenched upon metal binding. We also report similar dynamic features in apo-azurin, a paradigmatic blue copper protein, suggesting a general behavior. These findings reveal that the entatic/rack-induced state, governing the features of the metal center in the copper-loaded protein, does not require a preformed metal-binding site. Instead, metal binding is a major contributor to the rigidity of electron transfer copper centers. These results reconcile the seemingly contradictory requirements of a rigid, occluded center for electron transfer, and an accessible, dynamic site required for in vivo copper uptake.
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