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Bioresource Technology, 311. https://doi.org/10.1016/j.biortech.2020.123538 Zhang, L., Beatty, A., Lu, L., Abdalrahman, A., Makris, T. M., Wang, G., & Wang, Q. (2020). Microfluidic-assisted polymer-protein assembly to fabricate homogeneous functionalnanoparticles. Materials Science and Engineering C, 111. https://doi.org/10.1016/j.msec.2020.110768 Makris, T. M. (2019). CHAPTER 6: Cytochrome P450 Decarboxylases. In RSC Metallobiology: Vol. 2019-January (pp. 127–143). https://doi.org/10.1039/9781788012911-00127 Blahut, M., Wise, C. E., Bruno, M. R., Dong, G., Makris, T. M., Frantom, P. A., … Outten, F. W. (2019). Direct observation of intermediates in the SufS cysteine desulfurase reaction reveals functional roles of conserved active-site residues. Journal of Biological Chemistry, 294(33), 12444–12458. https://doi.org/10.1074/jbc.RA119.009471 Manley, O. M., Fan, R., Guo, Y., & Makris, T. M. (2019). Oxidative Decarboxylase UndA Utilizes a Dinuclear Iron Cofactor. Journal of the American Chemical Society, 141(22), 8684–8688. https://doi.org/10.1021/jacs.9b02545 Kader, S., Monavarian, M., Barati, D., Moeinzadeh, S., Makris, T. M., & Jabbari, E. (2019). Plasmin-Cleavable Nanoparticles for On-Demand Release of Morphogens in Vascularized Osteogenesis. Biomacromolecules, 20(8), 2973–2988. https://doi.org/10.1021/acs.biomac.9b00532 Schlachter, C. R., Daneshian, L., Amaya, J., Klapper, V., Wybouw, N., Borowski, T., … Chruszcz, M. (2019). Structural and functional characterization of an intradiol ring-cleavage dioxygenase from the polyphagous spider mite herbivore Tetranychus urticae Koch. Insect Biochemistry and Molecular Biology, 107, 19–30. https://doi.org/10.1016/j.ibmb.2018.12.001 Kaniusaite, M., Goode, R. J. A., Schittenhelm, R. B., Makris, T. M., & Cryle, M. J. (2019). The Diiron Monooxygenase CmlA from Chloramphenicol Biosynthesis Allows Reconstitution of β-Hydroxylation during Glycopeptide Antibiotic Biosynthesis. ACS Chemical Biology, 14(12), 2932–2941. https://doi.org/10.1021/acschembio.9b00862 Amaya, J. A., Rutland, C. D., Leschinsky, N., & Makris, T. M. (2018). A Distal Loop Controls Product Release and Chemo- and Regioselectivity in Cytochrome P450 Decarboxylases. Biochemistry, 57(3), 344–353. https://doi.org/10.1021/acs.biochem.7b01065 Khivantsev, K., Biancardi, A., Fathizadeh, M., Almalki, F., Grant, J. L., Tien, H. N., … Yu, M. (2018). Catalytic N−H Bond Activation and Breaking by a Well-Defined CoII1O4 Site of a Heterogeneous Catalyst. ChemCatChem, 10(4), 736–742. https://doi.org/10.1002/cctc.201701268 Wise, C. E., Hsieh, C. H., Poplin, N. L., & Makris, T. M. (2018). Dioxygen Activation by the Biofuel-Generating Cytochrome P450 OleT. ACS Catalysis, 8(10), 9342–9352. https://doi.org/10.1021/acscatal.8b02631 Zhang, L., Xu, Y., Makris, T. M., & Wang, Q. (2018). Enhanced Arylamine N -Oxygenase Activity of Polymer-Enzyme Assemblies by Facilitating Electron-Transferring Efficiency. Biomacromolecules, 19(3), 918–925. https://doi.org/10.1021/acs.biomac.7b01706 Mi?aczewska, A., Kot, E., Amaya, J. A., Makris, T. M., Zaj?c, M., Korecki, J., … Borowski, T. (2018). On the Structure and Reaction Mechanism of Human Acireductone Dioxygenase. Chemistry - A European Journal, 24(20), 5225–5237. https://doi.org/10.1002/chem.201704617 Munro, A. W., McLean, K. J., Grant, J. L., & Makris, T. M. (2018). Structure and function of the cytochrome P450 peroxygenase enzymes. Biochemical Society Transactions, 46(1), 183–196. https://doi.org/10.1042/BST20170218 Rahman, M. M., Smith, M. D., Amaya, J. A., Makris, T. M., & Peryshkov, D. V. (2017). Activation of C-H Bonds of Alkyl- and Arylnitriles by the TaCl5-PPh3 Lewis Pair. Inorganic Chemistry, 56(19), 11798–11803. https://doi.org/10.1021/acs.inorgchem.7b01800 Wise, C. E., Grant, J. L., Amaya, J. A., Ratigan, S. C., Hsieh, C. H., Manley, O. M., & Makris, T. M. (2017). Divergent mechanisms of iron-containing enzymes for hydrocarbon biosynthesis. Journal of Biological Inorganic Chemistry, 22(2-3), 221–235. https://doi.org/10.1007/s00775-016-1425-0 DeHaven, B. A., Tokarski, J. T., III, Korous, A. A., Mentink‐Vigier, F., Makris, T. M., Brugh, A. M., … Shimizu, L. S. (2017). Persistent Radicals of Self-assembled Benzophenone bis-Urea Macrocycles: Characterization and Application as a Polarizing Agent for Solid-state DNP MAS Spectroscopy. Chemistry - A European Journal, 23(34), 8315–8319. https://doi.org/10.1002/chem.201701705 Wise, C. E., & Makris, T. M. (2017). Recruitment and Regulation of the Non-ribosomal Peptide Synthetase Modifying Cytochrome P450 Involved in Nikkomycin Biosynthesis. ACS Chemical Biology, 12(5), 1316–1326. https://doi.org/10.1021/acschembio.7b00081 Hsieh, C. H., Huang, X., Amaya, J. A., Rutland, C. D., Keys, C. L., Groves, J. T., … Makris, T. M. (2017). 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J., Rivard, B. S., Münck, E., … Lipscomb, J. D. (2015). An unusual peroxo intermediate of the arylamine oxygenase of the chloramphenicol biosynthetic pathway. Journal of the American Chemical Society, 137(4), 1608–1617. https://doi.org/10.1021/ja511649n Grant, J. L., Hsieh, C. H., & Makris, T. M. (2015). Decarboxylation of fatty acids to terminal alkenes by cytochrome P450 compound i. Journal of the American Chemical Society, 137(15), 4940–4943. https://doi.org/10.1021/jacs.5b01965 Abeysinghe, D., Gerke, B., Morrison, G., Hsieh, C. H., Smith, M. D., Pöttgen, R., … Loye, H.-C. (2015). Synthesis, characterization, and properties of reduced europium molybdates and tungstates. Journal of Solid State Chemistry, 229, 173–180. https://doi.org/10.1016/j.jssc.2015.05.014 Catalase (KatA) Plays a role in protection against anaerobic nitric oxide in Pseudomonas aeruginosa. (2014). PLoS ONE, 9(3). https://doi.org/10.1371/journal.pone.0091813 Aukema, K. G., Makris, T. M., Stoian, S. A., Richman, J. E., Münck, E., Lipscomb, J. D., & Wackett, L. P. (2013). Cyanobacterial aldehyde deformylase oxygenation of aldehydes yields n - 1 aldehydes and alcohols in addition to alkanes. ACS Catalysis, 3(10), 2228–2238. https://doi.org/10.1021/cs400484m Makris, T. M., Knoot, C. J., Wilmot, C. M., & Lipscomb, J. D. (2013). Structure of a dinuclear iron cluster-containing β-hydroxylase active in antibiotic biosynthesis. Biochemistry, 52(38), 6662–6671. https://doi.org/10.1021/bi400845b Thompson, J. W., Salahudeen, A. A., Chollangi, S., Ruiz, J. C., Brautigam, C. A., Makris, T. M., … Bruick, R. K. (2012). Structural and molecular characterization of iron-sensing hemerythrin-like domain within F-box and leucine-rich repeat protein 5 (FBXL5). Journal of Biological Chemistry, 287(10), 7357–7365. https://doi.org/10.1074/jbc.M111.308684 Active-site structure of a β-hydroxylase in antibiotic biosynthesis. (2011). Journal of the American Chemical Society, 133(18), 6938–6941. https://doi.org/10.1021/ja201822v Knoot, C. J., Makris, T. M., & Lipscomb, J. D. (2011). Dinuclear Iron Cluster-Containing Oxygenase CmlA. Encyclopedia of Inorganic and Bioinorganic Chemistry. https://doi.org/10.1002/9781119951438.eibc2329 Makris, T. M., Chakrabarti, M., Münck, E., & Lipscomb, J. D. (2010). A family of diiron monooxygenases catalyzing amino acid beta-hydroxylation in antibiotic biosynthesis. Proceedings of the National Academy of Sciences of the United States of America, 107(35), 15391–15396. https://doi.org/10.1073/pnas.1007953107 Denisov, I. G., Mak, P. J., Makris, T. M., Sligar, S. G., & Kincaid, J. R. (2008). Resonance Raman characterization of the peroxo and hydroperoxo intermediates in cytochrome P450. Journal of Physical Chemistry A, 112(50), 13172–13179. https://doi.org/10.1021/jp8017875 Makris, T. M., Von Koenig, K., Schlichting, I., & Sligar, S. G. (2007). 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M., Schuler, M. A., & Sligar, S. G. (2005). A retinoic acid binding cytochrome P450: CYP120A1 from Synechocystis sp. PCC 6803. Archives of Biochemistry and Biophysics, 436(1), 110–120. https://doi.org/10.1016/j.abb.2005.01.011 Makris, T. M., Denisov, I., Schlichting, I., & Sligar, S. G. (2005). Activation of molecular oxygen by cytochrome P450. In Cytochrome P450: Structure, Mechanism, and Biochemistry: Third edition (pp. 149–182). https://doi.org/10.1007/0-387-27447-2_5 Denisov, I. G., Makris, T. M., Sligar, S. G., & Schlichting, I. (2005). Structure and chemistry of cytochrome P450. Chemical Reviews, 105(6), 2253–2277. https://doi.org/10.1021/cr0307143 Sono, M., Perera, R., Jin, S., Makris, T. M., Sligar, S. G., Bryson, T. A., & Dawson, J. H. (2005). The influence of substrate on the spectral properties of oxyferrous wild-type and T252A cytochrome P450-CAM. Archives of Biochemistry and Biophysics, 436(1), 40–49. https://doi.org/10.1016/j.abb.2004.12.026 Sligar, S. G., Makris, T. M., & Denisov, I. G. (2005). Thirty years of microbial P450 monooxygenase research: Peroxo-heme intermediates - The central bus station in heme oxygenase catalysis. Biochemical and Biophysical Research Communications, 338(1), 346–354. https://doi.org/10.1016/j.bbrc.2005.08.094 Jin, S., Makris, T. M., Bryson, T. A., Sligar, S. G., & Dawson, J. H. (2003). Epoxidation of olefins by hydroperoxo-ferric cytochrome P450. Journal of the American Chemical Society, 125(12), 3406–3407. https://doi.org/10.1021/ja029272n Makris, T. M., Denisov, I. G., & Sligar, S. G. (2003). Haem-oxygen reactive intermediates: Catalysis by the two-step. Biochemical Society Transactions, 31(3), 516–519. https://doi.org/10.1042/BST0310516 Ibrahim, M., Denisov, I. G., Makris, T. M., Kincaid, J. R., & Sligar, S. G. (2003). Resonance Raman Spectroscopic Studies of Hydroperoxo-Myoglobin at Cryogenic Temperatures. Journal of the American Chemical Society, 125(45), 13714–13718. https://doi.org/10.1021/ja036949d Denisov, I. G., Makris, T. M., & Sugar, S. G. (2002). Cryoradiolysis for the study of P450 reaction intermediates. Cytochrome P450 Part C, Vol. 357, pp. 103–115. https://doi.org/10.1016/s0076-6879(02)57670-9 Denisov, I. G., Makris, T. M., & Sligar, S. G. (2002). Formation and decay of hydroperoxo-ferric heme complex in horseradish peroxidase studied by cryoradiolysis. Journal of Biological Chemistry, 277(45), 42706–42710. https://doi.org/10.1074/jbc.M207949200 Makris, T. M., Davydov, R., Denisov, I. G., Hoffman, B. M., & Sligar, S. G. (2002). Mechanistic enzymology of oxygen activation by the cytochromes P450. Drug Metabolism Reviews, 34(4), 691–708. https://doi.org/10.1081/DMR-120015691 Denisov, I. G., Makris, T. M., & Sligar, S. G. (2001). Cryotrapped Reaction Intermediates of Cytochrome P450 Studied by Radiolytic Reduction with Phosphorus-32. Journal of Biological Chemistry, 276(15), 11648–11652. https://doi.org/10.1074/jbc.M010219200 Davydov, R., Makris, T. M., Kofman, V., Werst, D. E., Sligar, S. G., & Hoffman, B. M. (2001). Hydroxylation of camphor by reduced oxy-cytochrome p450cam: Mechanistic implications of EPR and ENDOR studies of catalytic intermediates in native and mutant enzymes. Journal of the American Chemical Society, 123(7), 1403–1415. https://doi.org/10.1021/ja003583l Davydov, R., Macdonald, I. D. G., Makris, T. M., Sugar, S. G., & Hoffman, B. M. (1999). EPR and ENDOR of catalytic intermediates in cryoreduced native and mutant oxy-cytochromes P450cam: Mutation-induced changes in the proton delivery system [15]. Journal of the American Chemical Society, 121(45), 10654–10655. https://doi.org/10.1021/ja9918829