{"id":59,"date":"2020-07-17T15:22:37","date_gmt":"2020-07-17T19:22:37","guid":{"rendered":"http:\/\/chem.sites.mtu.edu\/christov\/?page_id=59"},"modified":"2026-01-12T15:55:32","modified_gmt":"2026-01-12T20:55:32","slug":"publications","status":"publish","type":"page","link":"https:\/\/chem.sites.mtu.edu\/christov\/publications\/","title":{"rendered":"Publications"},"content":{"rendered":"\n<p><strong>Cover Images<\/strong><\/p>\n\n\n\n<div class=\"wp-block-group is-nowrap is-layout-flex wp-container-core-group-is-layout-ad2f72ca wp-block-group-is-layout-flex\">\n<figure class=\"wp-block-image size-full is-resized\"><a href=\"https:\/\/doi.org\/10.1039\/D4SC08378D\"><img loading=\"lazy\" decoding=\"async\" width=\"1241\" height=\"1625\" src=\"https:\/\/chem.sites.mtu.edu\/christov\/wp-content\/uploads\/2025\/05\/d5sc90100f_page-0001.jpg\" alt=\"\" class=\"wp-image-387\" style=\"width:200px;height:auto\" srcset=\"https:\/\/chem.sites.mtu.edu\/christov\/wp-content\/uploads\/2025\/05\/d5sc90100f_page-0001.jpg 1241w, https:\/\/chem.sites.mtu.edu\/christov\/wp-content\/uploads\/2025\/05\/d5sc90100f_page-0001-229x300.jpg 229w, https:\/\/chem.sites.mtu.edu\/christov\/wp-content\/uploads\/2025\/05\/d5sc90100f_page-0001-782x1024.jpg 782w, https:\/\/chem.sites.mtu.edu\/christov\/wp-content\/uploads\/2025\/05\/d5sc90100f_page-0001-768x1006.jpg 768w, https:\/\/chem.sites.mtu.edu\/christov\/wp-content\/uploads\/2025\/05\/d5sc90100f_page-0001-1173x1536.jpg 1173w\" sizes=\"auto, (max-width: 1241px) 100vw, 1241px\" \/><\/a><\/figure>\n\n\n\n<figure class=\"wp-block-image size-large is-resized\"><a href=\"https:\/\/doi.org\/10.1002\/chem.202403989\"><img loading=\"lazy\" decoding=\"async\" width=\"772\" height=\"1024\" src=\"https:\/\/chem.sites.mtu.edu\/christov\/wp-content\/uploads\/2025\/05\/chem202580301-toc-0001-m-772x1024.jpg\" alt=\"\" class=\"wp-image-394\" style=\"width:203px;height:auto\" srcset=\"https:\/\/chem.sites.mtu.edu\/christov\/wp-content\/uploads\/2025\/05\/chem202580301-toc-0001-m-772x1024.jpg 772w, https:\/\/chem.sites.mtu.edu\/christov\/wp-content\/uploads\/2025\/05\/chem202580301-toc-0001-m-226x300.jpg 226w, https:\/\/chem.sites.mtu.edu\/christov\/wp-content\/uploads\/2025\/05\/chem202580301-toc-0001-m-768x1018.jpg 768w, https:\/\/chem.sites.mtu.edu\/christov\/wp-content\/uploads\/2025\/05\/chem202580301-toc-0001-m-1158x1536.jpg 1158w, https:\/\/chem.sites.mtu.edu\/christov\/wp-content\/uploads\/2025\/05\/chem202580301-toc-0001-m.jpg 1251w\" sizes=\"auto, (max-width: 772px) 100vw, 772px\" \/><\/a><\/figure>\n\n\n\n<figure class=\"wp-block-image size-large is-resized\"><img loading=\"lazy\" decoding=\"async\" width=\"772\" height=\"1024\" src=\"https:\/\/chem.sites.mtu.edu\/christov\/wp-content\/uploads\/2025\/05\/chem202302510-toc-0001-m-772x1024.jpg\" alt=\"\" class=\"wp-image-392\" style=\"width:202px;height:auto\" srcset=\"https:\/\/chem.sites.mtu.edu\/christov\/wp-content\/uploads\/2025\/05\/chem202302510-toc-0001-m-772x1024.jpg 772w, https:\/\/chem.sites.mtu.edu\/christov\/wp-content\/uploads\/2025\/05\/chem202302510-toc-0001-m-226x300.jpg 226w, https:\/\/chem.sites.mtu.edu\/christov\/wp-content\/uploads\/2025\/05\/chem202302510-toc-0001-m-768x1018.jpg 768w, https:\/\/chem.sites.mtu.edu\/christov\/wp-content\/uploads\/2025\/05\/chem202302510-toc-0001-m-1158x1536.jpg 1158w, https:\/\/chem.sites.mtu.edu\/christov\/wp-content\/uploads\/2025\/05\/chem202302510-toc-0001-m.jpg 1251w\" sizes=\"auto, (max-width: 772px) 100vw, 772px\" \/><\/figure>\n\n\n\n<figure class=\"wp-block-image size-large is-resized\"><a href=\"https:\/\/chemistry-europe.onlinelibrary.wiley.com\/doi\/10.1002\/chem.202300138\"><img loading=\"lazy\" decoding=\"async\" width=\"771\" height=\"1024\" src=\"https:\/\/chem.sites.mtu.edu\/christov\/wp-content\/uploads\/2023\/05\/DioxygenCover-1-771x1024.png\" alt=\"\" class=\"wp-image-345\" style=\"width:199px;height:265px\" srcset=\"https:\/\/chem.sites.mtu.edu\/christov\/wp-content\/uploads\/2023\/05\/DioxygenCover-1-771x1024.png 771w, https:\/\/chem.sites.mtu.edu\/christov\/wp-content\/uploads\/2023\/05\/DioxygenCover-1-226x300.png 226w, https:\/\/chem.sites.mtu.edu\/christov\/wp-content\/uploads\/2023\/05\/DioxygenCover-1-768x1020.png 768w, https:\/\/chem.sites.mtu.edu\/christov\/wp-content\/uploads\/2023\/05\/DioxygenCover-1-1156x1536.png 1156w, https:\/\/chem.sites.mtu.edu\/christov\/wp-content\/uploads\/2023\/05\/DioxygenCover-1-1541x2048.png 1541w\" sizes=\"auto, (max-width: 771px) 100vw, 771px\" \/><\/a><\/figure>\n<\/div>\n\n\n\n<p><\/p>\n\n\n\n<div class=\"wp-block-group is-nowrap is-layout-flex wp-container-core-group-is-layout-ad2f72ca wp-block-group-is-layout-flex\">\n<figure class=\"wp-block-image size-full is-resized\"><a href=\"https:\/\/chemistry-europe.onlinelibrary.wiley.com\/doi\/10.1002\/chem.202101174\"><img loading=\"lazy\" decoding=\"async\" width=\"771\" height=\"1024\" src=\"https:\/\/chem.sites.mtu.edu\/christov\/wp-content\/uploads\/2023\/05\/chem.202102157-pages-1-1-771x1024-1.png\" alt=\"\" class=\"wp-image-344\" style=\"width:199px;height:265px\" srcset=\"https:\/\/chem.sites.mtu.edu\/christov\/wp-content\/uploads\/2023\/05\/chem.202102157-pages-1-1-771x1024-1.png 771w, https:\/\/chem.sites.mtu.edu\/christov\/wp-content\/uploads\/2023\/05\/chem.202102157-pages-1-1-771x1024-1-226x300.png 226w, https:\/\/chem.sites.mtu.edu\/christov\/wp-content\/uploads\/2023\/05\/chem.202102157-pages-1-1-771x1024-1-768x1020.png 768w\" sizes=\"auto, (max-width: 771px) 100vw, 771px\" \/><\/a><\/figure>\n\n\n\n<figure class=\"wp-block-image is-resized\"><a href=\"https:\/\/pubs.acs.org\/doi\/10.1021\/acscentsci.0c00312\"><img loading=\"lazy\" decoding=\"async\" width=\"770\" height=\"1024\" src=\"https:\/\/chem.sites.mtu.edu\/christov\/wp-content\/uploads\/2021\/07\/acscii_v006i005-4-2-770x1024.jpg\" alt=\"\" class=\"wp-image-282\" style=\"aspect-ratio:0.752895752895753;width:199px;height:auto\" srcset=\"https:\/\/chem.sites.mtu.edu\/christov\/wp-content\/uploads\/2021\/07\/acscii_v006i005-4-2-770x1024.jpg 770w, https:\/\/chem.sites.mtu.edu\/christov\/wp-content\/uploads\/2021\/07\/acscii_v006i005-4-2-226x300.jpg 226w, https:\/\/chem.sites.mtu.edu\/christov\/wp-content\/uploads\/2021\/07\/acscii_v006i005-4-2-768x1021.jpg 768w, https:\/\/chem.sites.mtu.edu\/christov\/wp-content\/uploads\/2021\/07\/acscii_v006i005-4-2-1155x1536.jpg 1155w, https:\/\/chem.sites.mtu.edu\/christov\/wp-content\/uploads\/2021\/07\/acscii_v006i005-4-2-1540x2048.jpg 1540w, https:\/\/chem.sites.mtu.edu\/christov\/wp-content\/uploads\/2021\/07\/acscii_v006i005-4-2-scaled.jpg 1925w\" sizes=\"auto, (max-width: 770px) 100vw, 770px\" \/><\/a><\/figure>\n<\/div>\n\n\n\n<p><strong>2025<\/strong><\/p>\n\n\n\n<ul class=\"wp-block-list\">\n<li>Palacios, P. M.; Li, X.;\u00a0Rifayee, S. B. J. S<strong>.<\/strong>; Tang, H.; Karabencheva-Christova, T.; Christov, C. Z.; Chang, W.-C.; Guo, Y. Regio- and Stereo-Selective Halogenation by an Iron(II)- and 2-Oxoglutarate-Dependent Halogenase in the Biosynthesis of Halogenated Nucleosides. J. Am. Chem. Soc. 2025, 147, 52, 48166\u201348179. <a href=\"https:\/\/doi.org\/10.1021\/jacs.5c16374\">https:\/\/doi.org\/10.1021\/jacs.5c16374<\/a>.<\/li>\n\n\n\n<li>Cherilakkudy, F. H.; Thomas, M. G.; Varghese, A.; Waheed, S. O.; Krishnan, A.; Venditti, V.; Schofield, C. J.; Li, D.; Christov, C. Z.; Karabencheva-Christova, T. G. Revealing the Catalytic Mechanism of the Fe(II)\/2-Oxoglutarate-Dependent Human Epigenetic Modifying Enzyme ALKBH5.\u00a0<em>Cell Rep. Phys. Sci.<\/em>\u00a0<strong>2025<\/strong>,\u00a0<em>6<\/em>\u00a0(8), 102779. <a href=\"https:\/\/doi.org\/10.1016\/j.xcrp.2025.102779\">https:\/\/doi.org\/10.1016\/j.xcrp.2025.102779<\/a>.<\/li>\n\n\n\n<li>Melayikandy, S.; Krishnan, A.; Varghese, A.; Jaber Sathik Rifayee, S. B.; Waheed, S. O.; Ramanan, R.; Li, D.; Christov, C. Z.; Karabencheva-Christova, T. G. Catalytic Mechanism of the Bacterial Non-Heme Fe(II) and 2-Oxoglutarate Dependent Enzyme AlkB with Single-Stranded DNA Containing Complex Guanine Adducts.\u00a0<em>Inorg. Chem.<\/em>\u00a0<strong>2025<\/strong>,\u00a0<em>64<\/em>\u00a0(30), 15650\u201315666. <a href=\"https:\/\/doi.org\/10.1021\/acs.inorgchem.5c02176\">https:\/\/doi.org\/10.1021\/acs.inorgchem.5c02176<\/a>.<\/li>\n\n\n\n<li>Chatterjee, S.; Rankin, J. A.; Farrugia, M. A.;\u00a0<strong>Rifayee, S. B. J. S.<\/strong>; Christov, C. Z.; Hu, J.; Hausinger, R. P. Biochemical, Structural, and Conformational Characterization of a Fungal Ethylene-Forming Enzyme. Biochemistry 2025, 64 (9), 2054\u20132067. <a href=\"https:\/\/doi.org\/10.1021\/acs.biochem.5c00038\">https:\/\/doi.org\/10.1021\/acs.biochem.5c00038<\/a>.<\/li>\n\n\n\n<li>Jaber Sathik Rifayee, S. B.; Thomas, M. G.; Christov, C. Z. Revealing the nature of the second branch point in the catalytic mechanism of the Fe(ii)\/2OG-dependent ethylene forming enzyme RSC <em>Chem. Sci.<\/em>, <strong>2025<\/strong>,16, 7667-7684. <a href=\"https:\/\/doi.org\/10.1039\/D4SC08378D\" data-type=\"link\" data-id=\"https:\/\/doi.org\/10.1039\/D4SC08378D\">https:\/\/doi.org\/10.1039\/D4SC08378D<\/a>. <\/li>\n<\/ul>\n\n\n\n<p><strong>2024<\/strong><\/p>\n\n\n\n<ul class=\"wp-block-list\">\n<li>Thomas, M. G.; Jaber Sathik Rifayee, S. B.; Christov, C. Z. How Do Variants of Residues in the First Coordination Sphere, Second Coordination Sphere, and Remote Areas Influence the Catalytic Mechanism of Non-Heme Fe(II)\/2-Oxoglutarate Dependent Ethylene-Forming Enzyme? ACS Catal. 2024, 14, 24, 18550\u201318569. <a href=\"https:\/\/doi.org\/10.1021\/acscatal.4c04010\">https:\/\/doi.org\/10.1021\/acscatal.4c04010<\/a>.<\/li>\n\n\n\n<li>Chatterjee, S.; Fellner, M.; Rankin, JoelA.;\u00a0<strong>Thomas, M. G.<\/strong>; J S Rifayee, S. B.; Christov, C. Z.; Hu, J.; Hausinger, R. P. Structural, Spectroscopic, and Computational Insights from Canavanine-Bound and Two Catalytically Compromised Variants of the Ethylene-Forming Enzyme. Biochemistry 2024, 63 (8), 1038\u20131050. <a href=\"https:\/\/doi.org\/10.1021\/acs.biochem.4c00031\">https:\/\/doi.org\/10.1021\/acs.biochem.4c00031<\/a>.<\/li>\n\n\n\n<li>Devadas, S.; Thomas, M. G.; Rifayee, S. B. J. S.; Varada, B.; White, W.; Sommer, E.; Campbell, K.; Schofield, C. J.; Christov, C. Origins of Catalysis in Non\u2010Heme Fe(II)\/2\u2010Oxoglutarate\u2010Dependent Histone Lysine Demethylase KDM4A with Differently Methylated Histone H3 Peptides.&nbsp;<em>Chem. \u2013 Eur. J.&nbsp;<\/em><strong>2024<\/strong>, e202403989.&nbsp;<a href=\"https:\/\/doi.org\/10.1002\/chem.202403989\" target=\"_blank\" rel=\"noreferrer noopener\">https:\/\/doi.org\/10.1002\/chem.202403989<\/a>.<\/li>\n\n\n\n<li>Thomas, M. G.; Jaber Sathik Rifayee, S. B.; Chaturvedi, S. S.; Gorantla, K. R.; White, W.; Wildey, J.; Schofield, C. J.; Christov, C. Z. The Unique Role of the Second Coordination Sphere to Unlock and Control Catalysis in Nonheme Fe(II)\/2-Oxoglutarate Histone Demethylase KDM2A. <em>Inorg. Chem.<\/em><strong>2024<\/strong>, <em>63<\/em> (23), 10737\u201310755. <a href=\"https:\/\/doi.org\/10.1021\/acs.inorgchem.4c01365\">https:\/\/doi.org\/10.1021\/acs.inorgchem.4c01365<\/a>.<\/li>\n<\/ul>\n\n\n\n<p><strong>2023<\/strong><\/p>\n\n\n\n<ul class=\"wp-block-list\">\n<li>Rifayee, S. B. J. S.; Chaturvedi, S. S.; Warner, C.; Wildey, J.; White, W.; Thompson, M.; Schofield, C. J.; Christov, C. Z. Catalysis by KDM6 Histone Demethylases \u2013 A Synergy between the Non-Heme Iron(II) Center, Second Coordination Sphere, and Long-Range Interactions. <em>Chemistry \u2013 A European Journal<\/em>, <strong>2023<\/strong>. <a href=\"https:\/\/doi.org\/10.1002\/chem.202301305\">https:\/\/doi.org\/10.1002\/chem.202301305<\/a>.<\/li>\n\n\n\n<li>Chaturvedi, S. S.; Rifayee, S. B. J. S.; Ramanan, R.; Rankin, J. A.; Hu, J.; Hausinger, R. P.; Christov, C. Can an External Electric Field Switch between Ethylene Formation and L-Arginine Hydroxylation in the Ethylene Forming Enzyme?&nbsp;<em>Phys. Chem. Chem. Phys.<\/em>&nbsp;<strong>2023<\/strong>.&nbsp;<a href=\"https:\/\/doi.org\/10.1039\/D3CP01899G\">https:\/\/doi.org\/10.1039\/D3CP01899G<\/a>.<\/li>\n\n\n\n<li>Hausinger, R. P.; Rifayee, S. B. J. S.;\u00a0<strong>Thomas, M. G.<\/strong>; Chatterjee, S.; Hu, J.; Christov, C. Z. Biological Formation of Ethylene. RSC Chem. Biol. 2023, 4 (9), 635\u2013646. <a href=\"https:\/\/doi.org\/10.1039\/D3CB00066D\">https:\/\/doi.org\/10.1039\/D3CB00066D<\/a>.<\/li>\n\n\n\n<li>Chaturvedi, S. S.; Thomas, M. G.; Rifayee, S. B. J. S.; White, W.; Wildey, J.; Warner, C.; Schofield, C. J.; Hu, J.; Hausinger, R. P.; Karabencheva\u2010Christova, T. G.; Christov, C. Z. Dioxygen Binding Is Controlled by the Protein Environment in Non\u2010heme Fe&nbsp;<sup>II<\/sup>&nbsp;and 2\u2010Oxoglutarate Oxygenases: A Study on Histone Demethylase PHF8 and an Ethylene\u2010Forming Enzyme.&nbsp;<em>Chemistry A European J<\/em>&nbsp;<strong>2023<\/strong>.&nbsp;<a href=\"https:\/\/doi.org\/10.1002\/chem.202300138\">https:\/\/doi.org\/10.1002\/chem.202300138<\/a>.<\/li>\n<\/ul>\n\n\n\n<p><strong>2022<\/strong><\/p>\n\n\n\n<ul class=\"wp-block-list\">\n<li>Sosa Alfaro, V.; Waheed, S. O.; Palomino, H.; Knorrscheidt, A.; Weissenborn, M.; Christov, C. Z.; Lehnert, N. YfeX &#8211; A New Platform for Carbene Transferase Development with High Intrinsic Reactivity.&nbsp;<em>Chemistry<\/em>&nbsp;<strong>2022<\/strong>,&nbsp;<em>28<\/em>&nbsp;(65), e202201474.&nbsp;<a href=\"https:\/\/doi.org\/10.1002\/chem.202201474\">https:\/\/doi.org\/10.1002\/chem.202201474<\/a>.<\/li>\n\n\n\n<li>Chaturvedi, S. S.; Jaber Sathik Rifayee, S. B.; Waheed, S. O.; Wildey, J.; Warner, C.; Schofield, C. J.; Karabencheva-Christova, T. G.; Christov, C. Z. Can Second Coordination Sphere and Long-Range Interactions Modulate Hydrogen Atom Transfer in a Non-Heme Fe(II)-Dependent Histone Demethylase?&nbsp;<em>JACS Au<\/em>&nbsp;<strong>2022<\/strong>,&nbsp;<em>2<\/em>&nbsp;(9), 2169\u20132186.&nbsp;<a href=\"https:\/\/doi.org\/10.1021\/jacsau.2c00345\">https:\/\/doi.org\/10.1021\/jacsau.2c00345<\/a>.<\/li>\n\n\n\n<li>Waheed SO, Varghese A, Chaturvedi SS, Karabencheva-Christova TG, Christov CZ. <a href=\"https:\/\/pubs.acs.org\/doi\/10.1021\/acscatal.2c00024?utm_source=SendGrid_ealert&amp;utm_medium=ealert&amp;utm_campaign=CIT_10.1021\/acscatal.0c05034&amp;ref=SendGrid_ealert_CIT_10.1021\/acscatal.0c05034_\">How Human TET2 Enzyme Catalyzes the Oxidation of Unnatural Cytosine Modifications in Double-Stranded DNA<\/a>. ACS Catal. 2022 April 19;12:5327-5344. doi: 10.1021\/acscatal.2c00024.<\/li>\n<\/ul>\n\n\n\n<p><strong>2021<\/strong><\/p>\n\n\n\n<ul class=\"wp-block-list\">\n<li>Ramanan R, Waheed SO, Schofield CJ, Christov CZ. <a href=\"https:\/\/chemistry-europe.onlinelibrary.wiley.com\/doi\/full\/10.1002\/chem.202101174\">What is the Catalytic Mechanism of Enzymatic Histone N-Methyl Arginine Demethylation and Can It be Influenced by an External Electric Field? <\/a>Chem. Eur. J. May 14. doi: 10.1002\/chem.202101174.      <\/li>\n\n\n\n<li>Waheed SO, Chaturvedi SS, Karabencheva-Christova TG, Christov CZ. <a href=\"https:\/\/pubs.acs.org\/doi\/full\/10.1021\/acscatal.0c05034\" data-type=\"URL\" data-id=\"https:\/\/pubs.acs.org\/doi\/full\/10.1021\/acscatal.0c05034\">Catalytic Mechanism of Human Ten-Eleven Translocation-2 (TET2) Enzyme: Effects of Conformational Changes, Electric Field, and Mutations.<\/a> ACS Catal. 2020 Mar 14;11(7):3877-3890. doi: 10.1021\/acscatal.0c05034.<\/li>\n\n\n\n<li>Chaturvedi SS, Ramanan R, Hu J, Hausinger RP, Christov CZ. <a href=\"https:\/\/doi.org\/10.1021\/acscatal.0c03349\" data-type=\"URL\" data-id=\"https:\/\/doi.org\/10.1021\/acscatal.0c03349\" target=\"_blank\" rel=\"noreferrer noopener\">Atomic and Electronic Structure Determinants Distinguish between Ethylene Formation and l-Arginine Hydroxylation Reaction Mechanisms in the Ethylene-Forming Enzyme<\/a>. ACS Catal. 2021 Jan 19;11:1578\u20131592. doi: 10.1021\/acscatal.0c03349.<\/li>\n<\/ul>\n\n\n\n<p><strong>2020<\/strong><\/p>\n\n\n\n<ul class=\"wp-block-list\">\n<li>Ramanan R, Chaturvedi SS, Lehnert N, Schofield CJ, Karabencheva-Christova TG, Christov CZ. <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1039\/D0SC03713C\" target=\"_blank\">Catalysis by the JmjC histone demethylase KDM4A integrates substrate dynamics, correlated motions and molecular orbital control<\/a>. Chem. Sci. 2020 Sept 4;11:9950-9961. doi: 10.1039\/D0SC03713C<\/li>\n\n\n\n<li>Waheed SO, Ramanan R, Chaturvedi SS, Lehnert N, Schofield CJ, Christov CZ, Karabencheva-Christova TG. <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1021\/acscentsci.0c00312\" target=\"_blank\">Role of Structural Dynamics in Selectivity and Mechanism of Non-heme Fe(II) and 2-Oxoglutarate-Dependent Oxygenases Involved in DNA Repair<\/a>. ACS Cent Sci. 2020 May 27;6(5):795-814. doi: 10.1021\/acscentsci.0c00312. <\/li>\n\n\n\n<li>Chaturvedi SS, Ramanan R, Lehnert N, Schofield CJ, Karabencheva-Christova TG, Christov CZ. <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1021\/acscatal.9b04907\" target=\"_blank\">Catalysis by the Non-Heme Iron(II) Histone Demethylase PHF8 Involves Iron Center Rearrangement and Conformational Modulation of Substrate Orientation<\/a>. ACS Catal. 2020 Jan 17;10(2):1195-1209. doi: 10.1021\/acscatal.9b04907. <\/li>\n<\/ul>\n\n\n\n<p><strong>2019<\/strong><\/p>\n\n\n\n<ul class=\"wp-block-list\">\n<li>Chaturvedi SS, Ramanan R, Waheed SO, Ainsley J, Evison M, Ames JM, Schofield CJ, Karabencheva-Christova TG, Christov CZ. <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1002\/chem.201900492\" target=\"_blank\">Conformational Dynamics Underlies Different Functions of Human KDM7 Histone Demethylases<\/a>. Chemistry. 2019 Apr 11;25(21):5422-5426. doi: 10.1002\/chem.201900492. <\/li>\n\n\n\n<li>Waheed SO , Ramanan R , Chaturvedi SS , Ainsley J , Evison M , Ames JM , Schofield CJ , Christov CZ , Karabencheva-Christova TG . <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1039\/C9OB00162J\" target=\"_blank\">Conformational flexibility influences structure-function relationships in nucleic acid N-methyl demethylases<\/a>. Org Biomol Chem. 2019 Feb 20;17(8):2223-2231. doi: 10.1039\/c9ob00162j. <\/li>\n\n\n\n<li>Chaturvedi SS, Ramanan R, Waheed SO, Karabencheva-Christova TG, Christov CZ. <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1016\/bs.apcsb.2019.08.005\" target=\"_blank\">Structure-function relationships in KDM7 histone demethylases<\/a>. Adv Protein Chem Struct Biol. 2019;117:113-125. doi: 10.1016\/bs.apcsb.2019.08.005. <\/li>\n<\/ul>\n\n\n\n<p><strong>2018<\/strong><\/p>\n\n\n\n<ul class=\"wp-block-list\">\n<li>Ainsley J , Chaturvedi SS , Karabencheva-Christova TG , Tanasova M , Christov CZ . <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1039\/C8CC04843F\" target=\"_blank\">Integrating molecular probes and molecular dynamics to reveal binding modes of GLUT5 activatory and inhibitory ligands<\/a>. Chem Commun (Camb). 2018 Aug 30;54(71):9917-9920. doi: 10.1039\/c8cc04843f.<\/li>\n\n\n\n<li>Ainsley J, Mulholland AJ, Black GW, Sparagano O, Christov CZ, Karabencheva-Christova TG. <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1021\/acsomega.8b00385\" target=\"_blank\">Structural Insights from Molecular Dynamics Simulations of Tryptophan 7-Halogenase and Tryptophan 5-Halogenase<\/a>. ACS Omega. 2018 May 2;3(5):4847-4859. doi: 10.1021\/acsomega.8b00385. <\/li>\n\n\n\n<li>Karabencheva-Christova TG, Christov CZ. <a href=\"https:\/\/doi.org\/10.1016\/S1876-1623(18)30054-3\">Preface<\/a>. Adv Protein Chem Struct Biol. 2018;113:ix. doi: 10.1016\/S1876-1623(18)30054-3.<\/li>\n\n\n\n<li>Ainsley J, Lodola A, Mulholland AJ, Christov CZ, Karabencheva-Christova TG. <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1016\/bs.apcsb.2018.07.001\" target=\"_blank\">Combined Quantum Mechanics and Molecular Mechanics Studies of Enzymatic Reaction Mechanisms<\/a>. Adv Protein Chem Struct Biol. 2018;113:1-32. doi: 10.1016\/bs.apcsb.2018.07.001.<\/li>\n<\/ul>\n\n\n\n<p><strong>2017<\/strong><\/p>\n\n\n\n<ul class=\"wp-block-list\">\n<li>Karabencheva-Christova TG, Torras J, Mulholland AJ, Lodola A, Christov CZ. <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1038\/s41598-017-17789-x\" target=\"_blank\">Mechanistic Insights into the Reaction of Chlorination of Tryptophan Catalyzed by Tryptophan 7-Halogenase<\/a>. Sci Rep. 2017 Dec 12;7(1):17395. doi: 10.1038\/s41598-017-17789-x. <\/li>\n\n\n\n<li>Karabencheva-Christova TG, Christov CZ, Fields GB. <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1021\/acs.jpcb.7b09771\" target=\"_blank\">Conformational Dynamics of Matrix Metalloproteinase-1\u00b7Triple-Helical Peptide Complexes<\/a>. J Phys Chem B. 2018 May 31;122(21):5316-5326. doi: 10.1021\/acs.jpcb.7b09771. <\/li>\n\n\n\n<li>Rodriguez MC, Yongye AB, Cudic M, Martinez Mayorga K, Liu E, Mueller BM, Ainsley J, Karabencheva-Christova T, Christov CZ, Cudic M, Cudic P. <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1007\/s00726-017-2485-3\" target=\"_blank\">Targeting cancer-specific glycans by cyclic peptide lectinomimics<\/a>. Amino Acids. 2017 Nov;49(11):1867-1883. doi: 10.1007\/s00726-017-2485-3.<\/li>\n\n\n\n<li>Karabencheva-Christova TG, Christov CZ, Fields GB. <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1016\/bs.apcsb.2017.04.001\" target=\"_blank\">Collagenolytic Matrix Metalloproteinase Structure-Function Relationships: Insights From Molecular Dynamics Studies<\/a>. Adv Protein Chem Struct Biol. 2017;109:1-24. doi: 10.1016\/bs.apcsb.2017.04.001.<\/li>\n<\/ul>\n\n\n\n<p><strong>2016<\/strong><\/p>\n\n\n\n<ul class=\"wp-block-list\">\n<li>Drummen GP, Christov CZ. Editorial: <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.3390\/ijms17111914\" target=\"_blank\">Analysis of the Interaction of Dp44mT with Human Serum Albumin and Calf Thymus DNA Using Molecular Docking and Spectroscopic Techniques<\/a>. Int J Mol Sci. 2016 Nov 16;17(11):1914. doi: 10.3390\/ijms17111914. <\/li>\n\n\n\n<li>Singh W, Fields GB, Christov CZ, Karabencheva-Christova TG. <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.3390\/ijms17101727\" target=\"_blank\">Effects of Mutations on Structure-Function Relationships of Matrix Metalloproteinase-1<\/a>. Int J Mol Sci. 2016 Oct 14;17(10):1727. doi: 10.3390\/ijms17101727. <\/li>\n\n\n\n<li>Singh W, Karabencheva-Christova TG, Black GW, Ainsley J, Dover L, Christov CZ. <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1038\/srep20107\" target=\"_blank\">Conformational Dynamics, Ligand Binding and Effects of Mutations in NirE an S-Adenosyl-L-Methionine Dependent Methyltransferase<\/a>. Sci Rep. 2016 Jan 29;6:20107. doi: 10.1038\/srep20107. <\/li>\n\n\n\n<li>Christov CZ. <a rel=\"noreferrer noopener\" href=\"http:\/\/doi.org\/10.1016\/s1876-1623(16)30040-2\" data-type=\"URL\" data-id=\"http:\/\/doi.org\/10.1016\/s1876-1623(16)30040-2\" target=\"_blank\">Preface<\/a>. Adv Protein Chem Struct Biol. 2016;105:ix. doi: 10.1016\/S1876-1623(16)30040-2.<\/li>\n\n\n\n<li>Singh W, Fields GB, Christov CZ, Karabencheva-Christova TG. <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1039\/C6RA03033E\" data-type=\"URL\" data-id=\"https:\/\/doi.org\/10.1039\/C6RA03033E\" target=\"_blank\">Importance of the Linker Region in Matrix Metalloproteinase-1 Domain Interactions<\/a>. RSC Adv. 2016 Jan 1;6(28):23223-23232. doi: 10.1039\/C6RA03033E. <\/li>\n<\/ul>\n\n\n\n<p><strong>2014<\/strong><\/p>\n\n\n\n<ul class=\"wp-block-list\">\n<li>Karabencheva TG, Lee CC, Black GW, Donev R, Christov CZ. <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1039\/C4MB00141A\" data-type=\"URL\" data-id=\"https:\/\/doi.org\/10.1039\/C4MB00141A\" target=\"_blank\">How does conformational flexibility influence key structural features involved in activation of anaplastic lymphoma kinase?<\/a> Mol Biosyst. 2014 Jun;10(6):1490-5. doi: 10.1039\/c4mb00141a. <\/li>\n\n\n\n<li>Christov CZ. Metal-containing enzymes. <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1016\/s1876-1623(14)00055-8\" data-type=\"URL\" data-id=\"https:\/\/doi.org\/10.1016\/s1876-1623(14)00055-8\" target=\"_blank\">Preface<\/a>. Adv Protein Chem Struct Biol. 2014;97:ix. doi: 10.1016\/S1876-1623(14)00055-8. <\/li>\n<\/ul>\n\n\n\n<p><strong>2013<\/strong><\/p>\n\n\n\n<ul class=\"wp-block-list\">\n<li>Christov CZ, Lodola A, Karabencheva-Christova TG, Wan S, Coveney PV, Mulholland AJ. <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1016\/j.bpj.2013.01.040\" data-type=\"URL\" data-id=\"https:\/\/doi.org\/10.1016\/j.bpj.2013.01.040\" target=\"_blank\">Conformational effects on the pro-S hydrogen abstraction reaction in cyclooxygenase-1: an integrated QM\/MM and MD study<\/a>. Biophys J. 2013 Mar 5;104(5):L5-7. doi: 10.1016\/j.bpj.2013.01.040.<\/li>\n\n\n\n<li>Christov CZ. <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1016\/b978-0-12-416596-0.09986-3\" target=\"_blank\">Introduction: Biomolecular spectroscopy: advances from integrating experiments and theory<\/a>. Adv Protein Chem Struct Biol. 2013;93:xi-xii. doi: 10.1016\/B978-0-12-416596-0.09986-3. <\/li>\n\n\n\n<li>Karabencheva-Christova TG, Carlsson U, Balali-Mood K, Black GW, Christov CZ. <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1371\/journal.pone.0056874\" data-type=\"URL\" data-id=\"https:\/\/doi.org\/10.1371\/journal.pone.0056874\" target=\"_blank\">Conformational effects on the circular dichroism of Human Carbonic Anhydrase II: a multilevel computational study<\/a>. PLoS One. 2013;8(2):e56874. doi: 10.1371\/journal.pone.0056874. <\/li>\n<\/ul>\n\n\n\n<p><strong>2011<\/strong><\/p>\n\n\n\n<ul class=\"wp-block-list\">\n<li>C. Christov, P. Gonz\u00e1lez-Bulnes, F. Malhaire, T. Karabencheva, C. Goudet, J.-P. Pin, A. Llebaria, and J. Giraldo. <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1002\/cmdc.201000378\" data-type=\"URL\" data-id=\"https:\/\/doi.org\/10.1002\/cmdc.201000378\" target=\"_blank\">Integrated Synthetic, Pharmacological and Computational Investigation of Cis-2-(3,5-dichlorophenylcarbamoyl) Cyclohexane Carboxylic Acid Enantiomers as Positive Allosteric Modulators of Metabotropic Glutamate Receptor Subtype 4<\/a>. ChemMedChem. 2011;6(1):131-140. doi: 10.1002\/cmdc.201000378.<\/li>\n<\/ul>\n\n\n\n<p><strong>2010<\/strong><\/p>\n\n\n\n<ul class=\"wp-block-list\">\n<li>T. Karabencheva, R. Donev, Kia Balali-Mood, and C. Christov. <a href=\"https:\/\/doi.org\/10.1016\/j.bpc.2010.05.003\" data-type=\"URL\" data-id=\"https:\/\/doi.org\/10.1016\/j.bpc.2010.05.003\" target=\"_blank\" rel=\"noreferrer noopener\">Individual Contributions of the Aromatic Chromophores to the Near-UV Circular Dichroism in Class A \u03b2-lactamases: A Comparative Computational Analysis<\/a>. Biophysical Chemistry, 2010;151(1-2):39-45. doi: 10.1016\/j.bpc.2010.05.003.<\/li>\n\n\n\n<li>C. Christov and T. Karabencheva. <a href=\"https:\/\/doi.org\/10.1007\/s00214-010-0744-4\" data-type=\"URL\" data-id=\"https:\/\/doi.org\/10.1007\/s00214-010-0744-4\" target=\"_blank\" rel=\"noreferrer noopener\">Computational Insight in Protein Circular Dichroism: Detailed Analysis of Contributions of Individual Chromophores in TEM-1 \u00df-Lactamase<\/a>. Theoretical Chemistry Accounts, 2010;128:25-37. doi: 10.1007\/s00214-010-0744-4.<\/li>\n<\/ul>\n\n\n\n<p><strong>2008<\/strong><\/p>\n\n\n\n<ul class=\"wp-block-list\">\n<li>C. Christov, T. Karabencheva, and A. Lodola. <a href=\"https:\/\/doi.org\/10.1016\/j.cplett.2008.03.012\" data-type=\"URL\" data-id=\"https:\/\/doi.org\/10.1016\/j.cplett.2008.03.012\" target=\"_blank\" rel=\"noreferrer noopener\">Aromatic Interactions and Rotational Strengths within Protein Environment: An Electronic Structural Study on \u03b2-lactamases From Class A<\/a>. Chemical Physics Letters, 2008;456:89-95. doi: 10.1016\/j.cplett.2008.03.012. <\/li>\n\n\n\n<li>Christov CZ, Karabencheva TG, Lodola A. <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1016\/j.compbiolchem.2008.02.003\" data-type=\"URL\" data-id=\"https:\/\/doi.org\/10.1016\/j.compbiolchem.2008.02.003\" target=\"_blank\">Relationship between chiroptical properties, structural changes and interactions in enzymes: a computational study on beta-lactamases from class A<\/a>. Comput Biol Chem. 2008 Jun;32(3):167-75. doi: 10.1016\/j.compbiolchem.2008.02.003.<\/li>\n\n\n\n<li>A. Lodola, M. Mol, S. Rivara, C. Christov, G. Tarzia, D. Piomelli and A. Mulholland (2008) <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1039\/b714136j\" data-type=\"URL\" data-id=\"https:\/\/doi.org\/10.1039\/b714136j\" target=\"_blank\">Identification of productive inhibitor binding orientation in fatty acid amide hydrolase (FAAH) by QM\/MM mechanistic modelling<\/a>. <em>Chemical Communications, <\/em>214 \u2013 216; DOI: 10.1039\/b714136j.<\/li>\n<\/ul>\n\n\n\n<p><strong>2006<\/strong><\/p>\n\n\n\n<ul class=\"wp-block-list\">\n<li>A Soriano, R. Castillo, C. Christov, J. Andres, V. Moliner and I. Tunon (2006) <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1021\/bi061319k\" data-type=\"URL\" data-id=\"https:\/\/doi.org\/10.1021\/bi061319k\" target=\"_blank\">Catalysis in Glycine N-Methyltransferase: Testing Electrostatic Stabilization and Compression Hypothesis<\/a>, <em>Biochemistry, <\/em>45, 14917 -14925. doi: 10.1021\/bi061319k.<\/li>\n<\/ul>\n\n\n\n<p><strong>2005<\/strong><\/p>\n\n\n\n<ul class=\"wp-block-list\">\n<li>C. Christov, F Tielens and M. Mirazchiiski (2005) <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1007\/s00894-005-0061-3\" data-type=\"URL\" data-id=\"https:\/\/doi.org\/10.1007\/s00894-005-0061-3\" target=\"_blank\">Modeling study of the influences of the aromatic transitions and the electrostatic environment on the far-UV rotational strengths in TEM-1 \u03b2- lactamase<\/a><em>. J. Molecular Modeling, <\/em>12, 411-416. doi: 10.1007\/s00894-005-0061-3.<\/li>\n<\/ul>\n\n\n\n<p><strong>2004<\/strong><\/p>\n\n\n\n<ul class=\"wp-block-list\">\n<li>C. Christov and T. Karabencheva (2004) <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1016\/j.cplett.2004.08.035\" data-type=\"URL\" data-id=\"https:\/\/doi.org\/10.1016\/j.cplett.2004.08.035\" target=\"_blank\">Mechanisms of generation of rotational strengths of Class-A \u03b2-lactamase from Escherichia coli (TEM-1) part I: theoretical analysis of the influence of conformational changes in the near UV<\/a>, <em>Chemical Physics Letters, <\/em>396, 282-287. doi: 10.1016\/j.cplett.2004.08.035.<\/li>\n\n\n\n<li>C<strong>. <\/strong>Christov, A. Kantardjev, T. Karabencheva, and F. Tielens (2004) <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1016\/j.cplett.2004.11.008\" target=\"_blank\">Mechanisms of generation of rotational strengths of Class-A \u03b2-lactamase from Escherichia coli (TEM-1) part II: theoretical study of the effects of the electrostatic interactions in the near-UV<\/a>, <em>Chemical Physics Letters, <\/em>400, 524-530. doi: 10.1016\/j.cplett.2004.11.008.<\/li>\n\n\n\n<li>T. Karabencheva and C. Christov (2004) <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1016\/j.cplett.2004.09.099\" data-type=\"URL\" data-id=\"https:\/\/doi.org\/10.1016\/j.cplett.2004.09.099\" target=\"_blank\">Comparative Theoretical Study of the Mechanisms of Generation of Rotational Strengths in the Near-UV in \u03b2-Lactamases from class A<\/a> <em>Chemical Physics Letters,<\/em>398, 511-516. doi: 10.1016\/j.cplett.2004.09.099.<\/li>\n\n\n\n<li>C<strong>. C<\/strong>hristov, D. Yanev, A. Shosheva and B. Atanasov (2004) <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1515\/znc-2004-11-1210\" data-type=\"URL\" data-id=\"https:\/\/doi.org\/10.1515\/znc-2004-11-1210\" target=\"_blank\">pH-dependent quenching of the fluorescence of tryptophan residues of TEM-1 \u03b2-lactamase: combined computational and experimental study<\/a>. <em>Zeitschrift fur Naturforschung, <\/em>59c, 11\/12, 824-827. doi: 10.1515\/znc-2004-11-1210.<\/li>\n<\/ul>\n\n\n\n<p><strong>2001<\/strong><\/p>\n\n\n\n<ul class=\"wp-block-list\">\n<li>C. Christov, S. Gabriel, B Atanasov, and J. Fleischhauer (2001) <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1515\/zna-2001-1111\" data-type=\"URL\" data-id=\"https:\/\/doi.org\/10.1515\/zna-2001-1111\" target=\"_blank\">Calculation of CD spectrum of Class-A \u03b2-lactamase from <em>Escherichia coli <\/em>(TEM-1)<\/a>. <em>Zeitschrift fur Naturforschung, <\/em>56a, 757-760. doi: 10.1515\/zna-2001-1111.<\/li>\n<\/ul>\n","protected":false},"excerpt":{"rendered":"<p>Cover Images 2025 2024 2023 2022 2021 2020 2019 2018 2017 2016 2014 2013 2011 2010 2008 2006 2005 2004 2001<\/p>\n","protected":false},"author":8,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"footnotes":""},"class_list":["post-59","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"https:\/\/chem.sites.mtu.edu\/christov\/wp-json\/wp\/v2\/pages\/59","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/chem.sites.mtu.edu\/christov\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/chem.sites.mtu.edu\/christov\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/chem.sites.mtu.edu\/christov\/wp-json\/wp\/v2\/users\/8"}],"replies":[{"embeddable":true,"href":"https:\/\/chem.sites.mtu.edu\/christov\/wp-json\/wp\/v2\/comments?post=59"}],"version-history":[{"count":59,"href":"https:\/\/chem.sites.mtu.edu\/christov\/wp-json\/wp\/v2\/pages\/59\/revisions"}],"predecessor-version":[{"id":407,"href":"https:\/\/chem.sites.mtu.edu\/christov\/wp-json\/wp\/v2\/pages\/59\/revisions\/407"}],"wp:attachment":[{"href":"https:\/\/chem.sites.mtu.edu\/christov\/wp-json\/wp\/v2\/media?parent=59"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}