Publications
2023
A 2.2Å cryoEM structure of a quinol-dependent NO Reductase shows close similarity to respiratory oxidases
Flynn, A. J., Antonyuk, S. V., Eady, R. R., Muench, S. P., & Hasnain, S. S. (2023). A 2.2Å cryoEM structure of a quinol-dependent NO Reductase shows close similarity to respiratory oxidases. NATURE COMMUNICATIONS, 14(1). doi:10.1038/s41467-023-39140-x
2022
Single crystal spectroscopy and multiple structures from one crystal (MSOX) define catalysis in copper nitrite reductases
Rose, S. L., Baba, S., Okumura, H., Antonyuk, S. V., Sasaki, D., Hedison, T. M., . . . Hasnain, S. S. (2022). Single crystal spectroscopy and multiple structures from one crystal (MSOX) define catalysis in copper nitrite reductases. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 119(30). doi:10.1073/pnas.2205664119
New horizons in structure-function studies of copper nitrite reductase
Eady, R. R., & Hasnain, S. S. (2022). New horizons in structure-function studies of copper nitrite reductase. COORDINATION CHEMISTRY REVIEWS, 460. doi:10.1016/j.ccr.2022.214463
Copper‐Containing Nitrite Reductase
Rose, S. L., Hough, M. A., Antonyuk, S. V., Eady, R. R., & Hasnain, S. S. (n.d.). Copper‐Containing Nitrite Reductase. Unknown Journal, 1-14. doi:10.1002/9781119951438.eibc2821
2021
An unprecedented insight into the catalytic mechanism of copper nitrite reductase from atomic-resolution and damage-free structures
Rose, S. L., Antonyuk, S. V., Sasaki, D., Yamashita, K., Hirata, K., Ueno, G., . . . Hasnain, S. S. (2021). An unprecedented insight into the catalytic mechanism of copper nitrite reductase from atomic-resolution and damage-free structures. SCIENCE ADVANCES, 7(1). doi:10.1126/sciadv.abd8523
Reverse protein engineering of a novel 4-domain copper nitrite reductase reveals functional regulation by protein-protein interaction
Sasaki, D., Watanabe, T. F., Eady, R. R., Garratt, R. C., Antonyuk, S. V., & Hasnain, S. S. (2021). Reverse protein engineering of a novel 4-domain copper nitrite reductase reveals functional regulation by protein-protein interaction. FEBS JOURNAL, 288(1), 262-280. doi:10.1111/febs.15324
2020
Nature of the copper-nitrosyl intermediates of copper nitrite reductases during catalysis
Hough, M. A., Conradie, J., Strange, R. W., Antonyuk, S. V., Eady, R. R., Ghosh, A., & Hasnain, S. S. (n.d.). Nature of the copper-nitrosyl intermediates of copper nitrite reductases during catalysis. Chemical Science. doi:10.1039/d0sc04797j
Structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes
Sasaki, D., Watanabe, T. F., Eady, R. R., Garratt, R. C., Antonyuk, S. V., & Hasnain, S. S. (2020). Structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes. IUCrJ, 7(3), 557-565. doi:10.1107/s2052252520005230
2019
Unexpected Roles of a Tether Harboring a Tyrosine Gatekeeper Residue in Modular Nitrite Reductase Catalysis
Hedison, T. M., Shenoy, R. T., Iorgu, A. I., Heyes, D. J., Fisher, K., Wright, G. S. A., . . . Scrutton, N. S. (2019). Unexpected Roles of a Tether Harboring a Tyrosine Gatekeeper Residue in Modular Nitrite Reductase Catalysis. ACS Catalysis, 9(7), 6087-6099. doi:10.1021/acscatal.9b01266
Catalytically important damage-free structures of a copper nitrite reductase obtained by femtosecond X-ray laser and room-temperature neutron crystallography
Halsted, T. P., Yamashita, K., Gopalasingam, C. C., Shenoy, R. T., Hirata, K., Ago, H., . . . Hasnain, S. S. (2019). Catalytically important damage-free structures of a copper nitrite reductase obtained by femtosecond X-ray laser and room-temperature neutron crystallography. IUCRJ, 6, 761-772. doi:10.1107/S2052252519008285
2018
Identification of a tyrosine switch in copper-haem nitrite reductases
Dong, J., Sasaki, D., Eady, R. R., Antonyuk, S. V., & Hasnain, S. S. (2018). Identification of a tyrosine switch in copper-haem nitrite reductases. IUCrJ, 5(4), 510-518. doi:10.1107/S2052252518008242
Enzyme catalysis captured using multiple structures from one crystal at varying temperatures
Horrell, S., Kekilli, D., Sen, K., Owen, R. U., Dworkowski, F. S. N., Antonyuk, S. V., . . . Hough, M. A. (2018). Enzyme catalysis captured using multiple structures from one crystal at varying temperatures. IUCRJ, 5, 283-292. doi:10.1107/S205225251800386X
An unprecedented dioxygen species revealed by serial femtosecond rotation crystallography in copper nitrite reductase
Halsted, T. P., Yamashita, K., Hirata, K., Ago, H., Ueno, G., Tosha, T., . . . Hasnain, S. S. (2018). An unprecedented dioxygen species revealed by serial femtosecond rotation crystallography in copper nitrite reductase. IUCRJ, 5, 22-31. doi:10.1107/S2052252517016128
2016
Serial crystallography captures enzyme catalysis in copper nitrite reductase at atomic resolution from one crystal
Horrell, S., Antonyuk, S. V., Eady, R. R., Hasnain, S. S., Hough, M. A., & Strange, R. W. (2016). Serial crystallography captures enzyme catalysis in copper nitrite reductase at atomic resolution from one crystal. IUCrJ, 3(Part 4), 271-281. doi:10.1107/S205225251600823X
Fresh insight to functioning of selected enzymes of the nitrogen cycle
Eady, R. R., Antonyuk, S. V., & Hasnain, S. S. (2016). Fresh insight to functioning of selected enzymes of the nitrogen cycle. CURRENT OPINION IN CHEMICAL BIOLOGY, 31, 103-112. doi:10.1016/j.cbpa.2016.02.009
2014
Impact of residues remote from the catalytic centre on enzyme catalysis of copper nitrite reductase
Leferink, N. G. H., Antonyuk, S., Houwman, J. A., Scrutton, N., Eady, R. R., & Hasnain, S. S. (2014). Impact of residues remote from the catalytic centre on enzyme catalysis of copper nitrite reductase. Nature Communications, 5. doi:10.1038/ncomms5395
Fingerprinting redox and ligand states in haemprotein crystal structures using resonance Raman spectroscopy
Kekilli, D., Dworkowski, F. S. N., Pompidor, G., Fuchs, M. R., Andrew, C. R., Antonyuk, S., . . . Hough, M. A. (2014). Fingerprinting redox and ligand states in haemprotein crystal structures using resonance Raman spectroscopy. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 70, 1289-1296. doi:10.1107/S1399004714004039
2013
Structures of protein-protein complexes involved in electron transfer
Antonyuk, S. V., Han, C., Eady, R. R., & Hasnain, S. S. (2013). Structures of protein-protein complexes involved in electron transfer. NATURE, 496(7443), 123-127. doi:10.1038/nature11996
2012
Characterization of a novel copper-haem <i>c</i> dissimilatory nitrite reductase from <i>Ralstonia pickettii</i>
Han, C., Wright, G. S. A., Fisher, K., Rigby, S. E. J., Eady, R. R., & Hasnain, S. S. (2012). Characterization of a novel copper-haem <i>c</i> dissimilatory nitrite reductase from <i>Ralstonia pickettii</i>. BIOCHEMICAL JOURNAL, 444, 219-226. doi:10.1042/BJ20111623
Laser-flash photolysis indicates that internal electron transfer is triggered by proton uptake by Alcaligenes xylosoxidans copper-dependent nitrite reductase.
Leferink, N. G. H., Eady, R. R., Hasnain, S. S., & Scrutton, N. S. (2012). Laser-flash photolysis indicates that internal electron transfer is triggered by proton uptake by Alcaligenes xylosoxidans copper-dependent nitrite reductase.. The FEBS journal, 279(12), 2174-2181. doi:10.1111/j.1742-4658.2012.08601.x
A distal pocket Leu residue inhibits the binding of O2 and NO at the distal heme site of cytochrome c'.
Garton, E. M., Pixton, D. A., Petersen, C. A., Eady, R. R., Hasnain, S. S., & Andrew, C. R. (2012). A distal pocket Leu residue inhibits the binding of O2 and NO at the distal heme site of cytochrome c'.. Journal of the American Chemical Society, 134(3), 1461-1463. doi:10.1021/ja209770p
Characterization of a novel copperheme c dissimilatory nitrite reductase from Ralstonia pickettii
Han, C., Wright, G. S. A., Fisher, K., Rigby, S. E. J., Eady, R. R., & Hasnain, S. S. (2012). Characterization of a novel copperheme c dissimilatory nitrite reductase from Ralstonia pickettii. Biochemical Journal, 444, 216-219.
2011
Carbon monoxide poisoning is prevented by the energy costs of conformational changes in gas-binding haemproteins
Antonyuk, S. V., Rustage, N., Petersen, C. A., Arnst, J. L., Heyes, D. J., Sharma, R., . . . Hasnain, S. S. (2011). Carbon monoxide poisoning is prevented by the energy costs of conformational changes in gas-binding haemproteins. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 108(38), 15780-15785. doi:10.1073/pnas.1109051108
Distal-to-Proximal NO Conversion in Hemoproteins: The Role of the Proximal Pocket
Hough, M. A., Antonyuk, S. V., Barbieri, S., Rustage, N., McKay, A. L., Servid, A. E., . . . Hasnain, S. S. (2011). Distal-to-Proximal NO Conversion in Hemoproteins: The Role of the Proximal Pocket. JOURNAL OF MOLECULAR BIOLOGY, 405(2), 395-409. doi:10.1016/j.jmb.2010.10.035
Electron Transfer and Half Reactivity in Nitrogenase.
Clark, T. A., Fairhurst, S., Lowe, D. J., Watmough, N. J., & Eady, R. R. (2011). Electron Transfer and Half Reactivity in Nitrogenase.. Biochemical Society Transactions, 39, 201-206.
Gating Mechanisms for Biological Electron Transfer: Integrating Structure with Biophysics Reveals the Nature of Redox Control in Cytochrome P450 reductase and Copper-Dependent Nitrite Reductase.
Leferink, N. G. H., Pudney, C. R., Brenner, S., Heys, D. J., Eady, R. R., Hasnain, S. S., . . . Scrutton, N. S. (2011). Gating Mechanisms for Biological Electron Transfer: Integrating Structure with Biophysics Reveals the Nature of Redox Control in Cytochrome P450 reductase and Copper-Dependent Nitrite Reductase.. FEBS Letters, 586, 578-584.
Mechanism of Proton-Coupled Electron Transfer in the Catalytic Cycle of Alcaligenes xylosoxidans Copper-Dependent Nitrite Reductase
Leferink, N. G. H., Han, C., Antonyuk, S. V., Heyes, D. J., Rigby, S. E. J., Hough, M. A., . . . Hasnain, S. S. (2011). Mechanism of Proton-Coupled Electron Transfer in the Catalytic Cycle of Alcaligenes xylosoxidans Copper-Dependent Nitrite Reductase. Biochemistry, 50, 4121-4131. doi:10.1021/bi
2010
Characterization of cycP gene expression in Achromobacter xylosoxidans NCIMB 11015 and high-level heterologous synthesis of cytochrome c' in Escherichia coli.
Harris, R. L., Barbieri, S., Paraskevopoulos, K., Murphy, L. M., Eady, R. R., Hasnain, S. S., & Sawers, R. G. (2010). Characterization of cycP gene expression in Achromobacter xylosoxidans NCIMB 11015 and high-level heterologous synthesis of cytochrome c' in Escherichia coli.. Journal of molecular microbiology and biotechnology, 18(2), 102-108. doi:10.1159/000287989
2009
Demonstration of proton-coupled electron transfer in the copper-containing nitrite reductases.
Brenner, S., Heyes, D. J., Hay, S., Hough, M. A., Eady, R. R., Hasnain, S. S., & Scrutton, N. S. (2009). Demonstration of proton-coupled electron transfer in the copper-containing nitrite reductases.. The Journal of biological chemistry, 284(38), 25973-25983. doi:10.1074/jbc.m109.012245
2008
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.
Hough, M. A., Eady, R. R., & Hasnain, S. S. (2008). 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.. Biochemistry, 47(51), 13547-13553. doi:10.1021/bi801369y
Crystallography with online optical and X-ray absorption spectroscopies demonstrates an ordered mechanism in copper nitrite reductase
Hough, M. A., Antonyuk, S. V., Strange, R. W., Eady, R. R., & Hasnain, S. S. (2008). Crystallography with online optical and X-ray absorption spectroscopies demonstrates an ordered mechanism in copper nitrite reductase. JOURNAL OF MOLECULAR BIOLOGY, 378(2), 353-361. doi:10.1016/j.jmb.2008.01.097
2006
Insight into catalysis of nitrous oxide reductase from high-resolution structures of resting and inhibitor-bound enzyme from <i>Achromobacter cycloclastes</i>
Paraskevopoulos, K., Antonyuk, S. V., Sawers, R. G., Eady, R. R., & Hasnain, S. S. (2006). Insight into catalysis of nitrous oxide reductase from high-resolution structures of resting and inhibitor-bound enzyme from <i>Achromobacter cycloclastes</i>. JOURNAL OF MOLECULAR BIOLOGY, 362(1), 55-65. doi:10.1016/j.jmb.2006.06.064
2005
Atomic resolution structures of resting-state, substrate- and product-complexed Cu-nitrite reductase provide insight into catalytic mechanism
Antonyuk, S. V., Strange, R. W., Sawers, G., Eady, R. R., & Hasnain, S. S. (2005). Atomic resolution structures of resting-state, substrate- and product-complexed Cu-nitrite reductase provide insight into catalytic mechanism. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 102(34), 12041-12046. doi:10.1073/pnas.0504207102
High resolution structural studies of mutants provide insights into catalysis and electron transfer processes in copper nitrite reductase
Hough, M. A., Ellis, M. J., Antonyuk, S., Strange, R. W., Sawers, G., Eady, R. R., & Hasnain, S. S. (2005). High resolution structural studies of mutants provide insights into catalysis and electron transfer processes in copper nitrite reductase. JOURNAL OF MOLECULAR BIOLOGY, 350(2), 300-309. doi:10.1016/j.jmb.2005.04.006
Heterologous metalloprotein biosynthesis in Escherichia coli: conditions for the overproduction of functional copper-containing nitrite reductase and azurin from Alcaligenes xylosoxidans.
Harris, R. L., Prudêncio, M., Hasnain, S. S., Eady, R. R., & Sawers, R. G. (2005). Heterologous metalloprotein biosynthesis in Escherichia coli: conditions for the overproduction of functional copper-containing nitrite reductase and azurin from Alcaligenes xylosoxidans.. Journal of synchrotron radiation, 12(Pt 1), 13-18. doi:10.1107/s0909049504027852
2004
Insights into redox partner interactions and substrate binding in nitrite reductase from <i>Alcaligenes xylosoxidans</i>:: Crystal structures of the TrP138His and His313Gln mutants
Barrett, M. L., Harris, R. L., Antonyuk, S., Hough, M. A., Ellis, M. J., Sawers, G., . . . Hasnain, S. S. (2004). Insights into redox partner interactions and substrate binding in nitrite reductase from <i>Alcaligenes xylosoxidans</i>:: Crystal structures of the TrP138His and His313Gln mutants. BIOCHEMISTRY, 43(51), 16311-16319. doi:10.1021/bi048682g
Nitrous Oxide Reductase
Eady, R. R., Antonyuk, S. V., & Hasnain, S. S. (2004). Nitrous Oxide Reductase. Wiley. doi:10.1002/0470028637.met205
2003
The structure of glyceraldehyde 3-phosphate dehydrogenase from <i>Alcaligenes xylosoxidans</i> at 1.7 Å resolution
Antonyuk, S. V., Eady, R. R., Strange, R. W., & Hasnain, S. S. (2003). The structure of glyceraldehyde 3-phosphate dehydrogenase from <i>Alcaligenes xylosoxidans</i> at 1.7 Å resolution. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 59, 835-842. doi:10.1107/S0907444903041441