Enzyme catalysis captured using multiple structures from one crystal at varying temperatures
暂无分享,去创建一个
Thomas W Keal | Michael A Hough | Robin L Owen | S. Antonyuk | R. Strange | S. Hasnain | R. Owen | S. Horrell | F. Dworkowski | T. Keal | Richard W Strange | Svetlana V Antonyuk | Robert R Eady | S Samar Hasnain | Kakali Sen | Sam Horrell | Demet Kekilli | Florian S N Dworkowski | Chin W Yong | R. Eady | M. Hough | K. Sen | D. Kekilli | C. Yong
[1] B. Shoichet,et al. One Crystal, Two Temperatures: Cryocooling Penalties Alter Ligand Binding to Transient Protein Sites , 2015, Chembiochem : a European journal of chemical biology.
[2] J. Colletier,et al. Temperature-dependent macromolecular X-ray crystallography , 2010, Acta crystallographica. Section D, Biological crystallography.
[3] S. Antonyuk,et al. Serial crystallography captures enzyme catalysis in copper nitrite reductase at atomic resolution from one crystal , 2016, IUCrJ.
[4] Philip R. Evans,et al. How good are my data and what is the resolution? , 2013, Acta crystallographica. Section D, Biological crystallography.
[5] S. Grimme,et al. A consistent and accurate ab initio parametrization of density functional dispersion correction (DFT-D) for the 94 elements H-Pu. , 2010, The Journal of chemical physics.
[6] R. Strange,et al. Recent structural insights into the function of copper nitrite reductases. , 2017, Metallomics : integrated biometal science.
[7] M. Murphy,et al. Conserved active site residues limit inhibition of a copper-containing nitrite reductase by small molecules. , 2008, Biochemistry.
[8] Abhishek Dey,et al. Spectroscopic and computational studies of nitrite reductase: proton induced electron transfer and backbonding contributions to reactivity. , 2009, Journal of the American Chemical Society.
[9] G. G. Stokes. "J." , 1890, The New Yale Book of Quotations.
[10] M. Murphy,et al. Stable copper-nitrosyl formation by nitrite reductase in either oxidation state. , 2007, Biochemistry.
[11] S. Hasnain,et al. Demonstration of Proton-coupled Electron Transfer in the Copper-containing Nitrite Reductases* , 2009, The Journal of Biological Chemistry.
[12] N. Scrutton,et al. Laser‐flash photolysis indicates that internal electron transfer is triggered by proton uptake by Alcaligenes xylosoxidans copper‐dependent nitrite reductase , 2012, The FEBS journal.
[13] Elspeth F. Garman,et al. RADDOSE-3D: time- and space-resolved modelling of dose in macromolecular crystallography , 2013 .
[14] Gwyndaf Evans,et al. Outrunning free radicals in room-temperature macromolecular crystallography , 2012, Acta crystallographica. Section D, Biological crystallography.
[15] Gwyndaf Evans,et al. DIALS: implementation and evaluation of a new integration package , 2018, Acta crystallographica. Section D, Structural biology.
[16] Georg Weidenspointner,et al. Femtosecond X-ray protein nanocrystallography , 2011, Nature.
[17] M. Murphy,et al. Directing the mode of nitrite binding to a copper‐containing nitrite reductase from Alcaligenes faecalis S‐6: Characterization of an active site isoleucine , 2003, Protein science : a publication of the Protein Society.
[18] F. E. Dodd,et al. Structural and kinetic evidence for an ordered mechanism of copper nitrite reductase. , 1999, Journal of molecular biology.
[19] Alexey A. Sokol,et al. ChemShell—a modular software package for QM/MM simulations , 2014 .
[20] J. Hajdu,et al. The catalytic pathway of horseradish peroxidase at high resolution , 2002, Nature.
[21] Cong Han,et al. Proton-coupled electron transfer in the catalytic cycle of Alcaligenes xylosoxidans copper-dependent nitrite reductase. , 2011, Biochemistry.
[22] C. Scholes,et al. EPR-ENDOR of the Cu(I)NO complex of nitrite reductase. , 2006, Journal of the American Chemical Society.
[23] J. Sussman,et al. Specific protein dynamics near the solvent glass transition assayed by radiation‐induced structural changes , 2001, Protein science : a publication of the Protein Society.
[24] S. Hasnain,et al. Identification of the proton channel to the active site type 2 Cu center of nitrite reductase: structural and enzymatic properties of the His254Phe and Asn90Ser mutants. , 2008, Biochemistry.
[25] Hein J. Wijma,et al. A Random-sequential Mechanism for Nitrite Binding and Active Site Reduction in Copper-containing Nitrite Reductase* , 2006, Journal of Biological Chemistry.
[26] F. Weigend,et al. Balanced basis sets of split valence, triple zeta valence and quadruple zeta valence quality for H to Rn: Design and assessment of accuracy. , 2005, Physical chemistry chemical physics : PCCP.
[27] N. Pannu,et al. REFMAC5 for the refinement of macromolecular crystal structures , 2011, Acta crystallographica. Section D, Biological crystallography.
[28] E. Lattman,et al. Imaging enzyme kinetics at atomic resolution , 2016, IUCrJ.
[29] Christian Roth,et al. CCP4i2: the new graphical user interface to the CCP4 program suite , 2018, Acta crystallographica. Section D, Structural biology.
[30] M. Nishiyama,et al. Catalytic Roles for Two Water Bridged Residues (Asp-98 and His-255) in the Active Site of Copper-containing Nitrite Reductase* , 2000, The Journal of Biological Chemistry.
[31] M. Murphy,et al. Side-On Copper-Nitrosyl Coordination by Nitrite Reductase , 2004, Science.
[32] A. Brunger. Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. , 1992 .
[33] K. Yamaguchi,et al. Functional analysis of conserved aspartate and histidine residues located around the type 2 copper site of copper-containing nitrite reductase. , 2000, Journal of biochemistry.
[34] Matteo Levantino,et al. Using synchrotrons and XFELs for time-resolved X-ray crystallography and solution scattering experiments on biomolecules. , 2015, Current opinion in structural biology.
[35] Ezequiel Panepucci,et al. EIGER detector: application in macromolecular crystallography , 2016, Acta crystallographica. Section D, Structural biology.
[36] Frank Neese,et al. The ORCA program system , 2012 .
[37] B. Howes,et al. EPR and electron nuclear double resonance (ENDOR) studies show nitrite binding to the type 2 copper centers of the dissimilatory nitrite reductase of Alcaligenes xylosoxidans (NCIMB 11015). , 1994, Biochemistry.
[38] Randy J. Read,et al. Overview of the CCP4 suite and current developments , 2011, Acta crystallographica. Section D, Biological crystallography.
[39] Nathaniel Echols,et al. Accessing protein conformational ensembles using room-temperature X-ray crystallography , 2011, Proceedings of the National Academy of Sciences.
[40] Takashi Kameshima,et al. Redox-coupled proton transfer mechanism in nitrite reductase revealed by femtosecond crystallography , 2016, Proceedings of the National Academy of Sciences.
[41] G. Henkelman,et al. A climbing image nudged elastic band method for finding saddle points and minimum energy paths , 2000 .
[42] D. Kern,et al. Hidden alternate structures of proline isomerase essential for catalysis , 2010 .
[43] D. Stuart,et al. Exploiting fast detectors to enter a new dimension in room-temperature crystallography , 2014, Acta crystallographica. Section D, Biological crystallography.
[44] G. Schaftenaar,et al. Molden: a pre- and post-processing program for molecular and electronic structures* , 2000, J. Comput. Aided Mol. Des..
[45] S. Evans,et al. Spectroelectrochemical investigation of intramolecular and interfacial electron-transfer rates reveals differences between nitrite reductase at rest and during turnover. , 2011, Journal of the American Chemical Society.
[46] Graeme Winter,et al. Decision making in xia2 , 2013, Acta crystallographica. Section D, Biological crystallography.
[47] S. C. Rogers,et al. QUASI: A general purpose implementation of the QM/MM approach and its application to problems in catalysis , 2003 .
[48] P. Andrew Karplus,et al. Linking Crystallographic Model and Data Quality , 2012, Science.
[49] M. Murphy,et al. Alternate substrate binding modes to two mutant (D98N and H255N) forms of nitrite reductase from Alcaligenes faecalis S-6: structural model of a transient catalytic intermediate. , 2001, Biochemistry.
[50] P. Emsley,et al. Features and development of Coot , 2010, Acta crystallographica. Section D, Biological crystallography.
[51] G. Blaha,et al. Temperature-dependent radiation sensitivity and order of 70S ribosome crystals. , 2014, Acta crystallographica. Section D, Biological crystallography.
[52] G. Sawers,et al. Atomic resolution structures of resting-state, substrate- and product-complexed Cu-nitrite reductase provide insight into catalytic mechanism. , 2005, Proceedings of the National Academy of Sciences of the United States of America.
[53] K. Hirao,et al. Theoretical study on reaction mechanisms of nitrite reduction by copper nitrite complexes: toward understanding and controlling possible mechanisms of copper nitrite reductase. , 2015, The journal of physical chemistry. B.
[54] Walter Thiel,et al. DL-FIND: an open-source geometry optimizer for atomistic simulations. , 2009, The journal of physical chemistry. A.