De Novo Design of Four-Helix Bundle Metalloproteins: One Scaffold, Diverse Reactivities.
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Marco Chino | Ornella Maglio | Angela Lombardi | W. DeGrado | M. Chino | A. Lombardi | O. Maglio | Fabio Pirro | William F DeGrado | F. Pirro
[1] Paweł Dydio,et al. Abiological catalysis by artificial haem proteins containing noble metals in place of iron , 2016, Nature.
[2] M. Chino,et al. A De Novo Heterodimeric Due Ferri Protein Minimizes the Release of Reactive Intermediates in Dioxygen-Dependent Oxidation. , 2017, Angewandte Chemie.
[3] P. S. Kim,et al. High-resolution protein design with backbone freedom. , 1998, Science.
[4] Jeff Rawson,et al. De novo design of a hyperstable non-natural protein-ligand complex with sub-Å accuracy. , 2017, Nature chemistry.
[5] W. DeGrado,et al. Noncovalent self-assembly of a heterotetrameric diiron protein , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[6] W. Hagen,et al. De novo design, synthesis and characterisation of MP3, a new catalytic four-helix bundle hemeprotein. , 2012, Chemistry.
[7] W. DeGrado,et al. Response of a designed metalloprotein to changes in metal ion coordination, exogenous ligands, and active site volume determined by X-ray crystallography. , 2005, Journal of the American Chemical Society.
[8] A. Lombardi,et al. Miniaturized heme proteins: crystal structure of Co(III)-mimochrome IV , 2004, JBIC Journal of Biological Inorganic Chemistry.
[9] W. DeGrado,et al. Spectroscopic and metal binding properties of a de novo metalloprotein binding a tetrazinc cluster , 2018, Biopolymers.
[10] S. Lippard,et al. Coupling Oxygen Consumption with Hydrocarbon Oxidation in Bacterial Multicomponent Monooxygenases. , 2015, Accounts of chemical research.
[11] Vincenzo Pavone,et al. Preorganization of molecular binding sites in designed diiron proteins , 2003, Proceedings of the National Academy of Sciences of the United States of America.
[12] A. Jasniewski,et al. Dioxygen Activation by Nonheme Diiron Enzymes: Diverse Dioxygen Adducts, High-Valent Intermediates, and Related Model Complexes. , 2018, Chemical reviews.
[13] Bryan S. Der,et al. Evolution of a highly active and enantiospecific metalloenzyme from short peptides , 2018, Science.
[14] Marco Chino,et al. De Novo Design of Tetranuclear Transition Metal Clusters Stabilized by Hydrogen-Bonded Networks in Helical Bundles. , 2017, Journal of the American Chemical Society.
[15] Christopher C. Moser,et al. Design and synthesis of multi-haem proteins , 1994, Nature.
[16] C. M. Summa,et al. Computational de novo design, and characterization of an A(2)B(2) diiron protein. , 2002, Journal of molecular biology.
[17] P. Stenmark,et al. Membrane-bound diiron carboxylate proteins. , 2003, Annual review of plant biology.
[18] Christopher M. Summa,et al. De novo design and structural characterization of proteins and metalloproteins. , 1999, Annual review of biochemistry.
[19] Vincenzo Pavone,et al. Hemoprotein Models Based on a Covalent Helix–Heme–Helix Sandwich: 2. Structural Characterization of CoIII Mimochrome I δ and δ Isomers , 2006 .
[20] W. DeGrado,et al. Molecular-Level Insight into the Differential Oxidase and Oxygenase Reactivities of de Novo Due Ferri Proteins. , 2015, Journal of the American Chemical Society.
[21] B. Fox,et al. In-crystal reaction cycle of a toluene-bound diiron hydroxylase , 2017, Nature.
[22] M. Kennedy,et al. Metal-binding properties and structural characterization of a self-assembled coiled coil: formation of a polynuclear Cd-thiolate cluster. , 2013, Journal of inorganic biochemistry.
[23] M. Chino,et al. Designing Covalently Linked Heterodimeric Four-Helix Bundles. , 2016, Methods in enzymology.
[24] R. Vitale,et al. An artificial heme-enzyme with enhanced catalytic activity: evolution, functional screening and structural characterization. , 2015, Organic & biomolecular chemistry.
[25] D. Baker,et al. The coming of age of de novo protein design , 2016, Nature.
[26] W. DeGrado,et al. De novo design of catalytic proteins. , 2004, Proceedings of the National Academy of Sciences of the United States of America.
[27] E. Solomon,et al. Structure/function correlations over binuclear non-heme iron active sites , 2016, JBIC Journal of Biological Inorganic Chemistry.
[28] S L Mayo,et al. Coupling backbone flexibility and amino acid sequence selection in protein design , 1997, Protein science : a publication of the Protein Society.
[29] A. Lombardi,et al. Miniaturized metalloproteins: application to iron-sulfur proteins. , 2000, Proceedings of the National Academy of Sciences of the United States of America.
[30] Alessandro Senes,et al. De novo design and molecular assembly of a transmembrane diporphyrin-binding protein complex. , 2010, Journal of the American Chemical Society.
[31] Hidetoshi Kono,et al. Computational design and characterization of a monomeric helical dinuclear metalloprotein. , 2003, Journal of molecular biology.
[32] W. DeGrado,et al. The structure of a designed diiron(III) protein: implications for cofactor stabilization and catalysis. , 2006, Angewandte Chemie.
[33] B K Shoichet,et al. A relationship between protein stability and protein function. , 1995, Proceedings of the National Academy of Sciences of the United States of America.
[34] G. Ghirlanda,et al. Copper Environment in Artificial Metalloproteins Probed by Electron Paramagnetic Resonance Spectroscopy. , 2015, The journal of physical chemistry. B.
[35] Angela Lombardi,et al. Design and engineering of artificial oxygen-activating metalloenzymes. , 2016, Chemical Society reviews.
[36] Tillmann Heinisch,et al. Artificial Metalloenzymes: Reaction Scope and Optimization Strategies. , 2018, Chemical reviews.
[37] Daniel W. Kulp,et al. Altering the O2-Dependent Reactivity of de novo Due Ferri Proteins , 2012, Nature chemistry.
[38] L. Regan,et al. Characterization of a helical protein designed from first principles. , 1988, Science.
[39] Design of a Synthetic Receptor for the Calmodulin-Binding Domain of Calcineurin , 1997 .
[40] Gevorg Grigoryan,et al. De novo design of a transmembrane Zn2+-transporting four-helix bundle , 2014, Science.
[41] C. M. Summa,et al. INAUGURAL ARTICLE by a Recently Elected Academy Member:Retrostructural analysis of metalloproteins: Application to the design of a minimal model for diiron proteins , 2000 .
[42] J R Desjarlais,et al. From coiled coils to small globular proteins: Design of a native‐like three‐helix bundle , 1998, Protein science : a publication of the Protein Society.
[43] M. Chino,et al. Enhancement of Peroxidase Activity in Artificial Mimochrome VI Catalysts through Rational Design , 2018, Chembiochem : a European journal of chemical biology.
[44] Barbara Ciani,et al. pH dependent binding in de novo hetero bimetallic coiled coils. , 2018, Dalton transactions.
[45] W. DeGrado,et al. Systematic Perturbations of Binuclear Non-heme Iron Sites: Structure and Dioxygen Reactivity of de Novo Due Ferri Proteins. , 2015, Biochemistry.
[46] W. DeGrado,et al. An artificial di-iron oxo-protein with phenol oxidase activity. , 2009, Nature chemical biology.
[47] B. R. Gibney,et al. X-ray structure of a maquette scaffold. , 2003, Journal of molecular biology.
[48] D. Baker,et al. Design of a Novel Globular Protein Fold with Atomic-Level Accuracy , 2003, Science.
[49] A. Lombardi,et al. Spectroscopic and metal-binding properties of DF3: an artificial protein able to accommodate different metal ions , 2010, JBIC Journal of Biological Inorganic Chemistry.
[50] Sliding helix and change of coordination geometry in a model di-MnII protein. , 2003, Angewandte Chemie.
[51] K. Hodgson,et al. Spectroscopic definition of the biferrous and biferric sites in de novo designed four-helix bundle DFsc peptides: implications for O2 reactivity of binuclear non-heme iron enzymes. , 2009, Biochemistry.
[52] W. DeGrado,et al. Analysis and design of turns in alpha-helical hairpins. , 2005, Journal of molecular biology.
[53] Christopher M. Summa,et al. Tertiary templates for the design of diiron proteins. , 1999 .
[54] W. DeGrado,et al. Designed metalloprotein stabilizes a semiquinone radical. , 2016, Nature chemistry.
[55] W. DeGrado,et al. From synthetic coiled coils to functional proteins: automated design of a receptor for the calmodulin-binding domain of calcineurin. , 1998, Journal of molecular biology.
[56] W. DeGrado,et al. Toward the de novo design of a catalytically active helix bundle: a substrate-accessible carboxylate-bridged dinuclear metal center. , 2001, Journal of the American Chemical Society.
[57] Vikas Nanda,et al. De novo design of a redox-active minimal rubredoxin mimic. , 2005, Journal of the American Chemical Society.
[58] William Sheffler,et al. De novo design of a fluorescence-activating β-barrel , 2018, Nature.
[59] J R Desjarlais,et al. De novo design of the hydrophobic cores of proteins , 1995, Protein science : a publication of the Protein Society.
[60] W. DeGrado,et al. Design of a 4-helix bundle protein: synthesis of peptides which self-associate into a helical protein , 1987 .
[61] P. Leslie Dutton,et al. Design of a heme-binding four-helix bundle , 1994 .
[62] W. DeGrado,et al. Solution structure and dynamics of a de novo designed three-helix bundle protein. , 1999, Proceedings of the National Academy of Sciences of the United States of America.
[63] E. Marsh,et al. Aldehyde Decarbonylases: Enigmatic Enzymes of Hydrocarbon Biosynthesis. , 2013, ACS catalysis.
[64] Gevorg Grigoryan,et al. Design of protein-interaction specificity affords selective bZIP-binding peptides , 2009, Nature.