PUBLICATIONS
Snyder, N. S.; Mak, P. J. “Structure-function characterization of the mono- and diheme forms of MhuD, a noncanonical heme oxygenase from Mycobacterium tuberculosis”, J. Biol. Chem., 2022, 298, 101475-101790. DOI: 10.1016/j.jbc.2021.101475
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Chiura, T.; Mak, P. J. “Investigation of Cyanide Ligand as an Active Site Probe of Human Heme Oxygenase”, Inorg. Chem. 2021, 60, 4633-4645. DOI:10.1021/acs.inorgchem.0c03611
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Dybas, J.; Chiura, T.; Marzec, K. M.; Mak, P. J. “Probing Heme Active Sites of Hemoglobin in Functional Red Blood Cells Using Resonance Raman Spectroscopy”, J. Phys. Chem. B 2021, 125, 3556-3565. DOI: 10.1021/acs.jpcb.1c01199
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Traore, E. S.; Li, J.; Chiura, T.; Geng, J.; Sachla, A. J.; Yoshimoto, F.; Eichenbaum, Z.; Davis, I; Mak, P. J.; Liu, A. “Heme binding to HupZ with a C-​terminal tag from group A streptococcus”, Molecules 2021, 26, 549. DOI: 10.3390/molecules26030549
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Dybas, J.; Bokamper, M. J.; Marzec, K. M.; Mak, P. J.” Probing the structure-function relationship of hemoglobin in living human red blood cells”, Spectrochim. Acta, Part A: Mol. Biomol. Spectrosc. 2020, 239, 118530. DOI: 10.1016/j.saa.2020.118530
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Atifi, A.; Mak, P. J.; Ryan, M. D. “Ion Pairing versus Solvation of Dinitrobenzene Anions in Room-Temperature Ionic Liquids (RTILs): Vibrational Signatures of RTIL–Substrate Interactions”, J. Phys. Chem. A, 2020, 124, 10225-10238. DOI: 10.1021/acs.jpca.0c06267
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Usai, R.; Kaluka, D.; Mak, P. J.; Liu, Y.; Kincaid, J. R. “Resonance Raman spectroscopic studies of peroxo and hydroperoxo intermediates in lauric acid (LA)​-​bound cytochrome P450 119”, J. Inorg. Biochem. 2020, 208, 111084. DOI: 10.1016/j.jinorgbio.2020.111084
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Atifi, A.; Mak. P. J.; Ryan, M. D. “Proton-Coupled Reduction of an Iron Nitrosyl Porphyrin in the Protic Ionic Liquid Nanodomain”, Electrochim. Acta, 2019, 295, 735-741. ​
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Mak, P. J.; Duggal, R.; Denisov, I. G.; Gregory, M. C.; Sligar, S. G.; Kincaid, J. R. “Human Cytochrome CYP17A1: The Structural Basis for Compromised Lyase Activity with 17-Hydroxyprogesterone”, J. Am. Chem. Soc., 2018, 140, 7324–7331.
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Mak, P. J.; Denisov, I. G. “Spectroscopic studies of the cytochrome P450 reaction mechanisms”, Biochem. Biophys. Acta, Proteins and Proteomics, 2018, 1866, 178-204.
Gregory, M. C.; Mak, P. J.; Khatri, Y.; Kincaid, J. R.; Sligar, S. G. “Human P450 CYP17A1: Control of Substrate Preference by Asparagine 202”, Biochemistry, 2017, 57, 764-771.
Mak, P. J.; Kincaid, J. R. "Bioinorganic Applications of Resonance Raman Spectroscopy" in Reedijk, J. (Ed.) Elsevier Reference Module in Chemistry, Molecular Sciences and Chemical Engineering; Waltham, MA; Elsevier 2017, pp. 1-16.
Zhu, Q.; Mak, P. J.; Tuckey, R. C. ; Kincaid, J. R. "Active site structures of CYP11A1 in the presence of its physiological substrates and alterations upon binding of Adrenodoxin", Biochemistry, 2017, 56, 5786-5797.
Wang, Y.; Mak, P. J.; Zhu, Q.; Kincaid, J. R. “Application of resonance Raman spectroscopy for interrogation of cryoradiolytically reduced oxygenated heme proteins”, J. Raman Spectrosc., 2017, 48, 180-190.
Mak, P. J. "Resonance Raman spectroscopy as a structural probe of cytochrome P450 enzymatic cycle", Handbook of Porphyrin Science, Kadish, K. M.; Smith, K.; Guilard, R. Eds., World Scientific Publishing Co., Singapore, 2016, 42, 1-120.
Denisov, I.G.; Mak, P. J.; Grinkova, Y. V.; Sligar, S. G.; Kincaid, J. R. “The use of isomeric testostrone dimers to explore allosteric effects in substrate binding to cytochrome P450 CYP3A4”, J. Inorg. Biochem. 2016, 158, 77-85.
Mak, P. J.; Gregory, M. C.; Denisov, I. G.; Sligar, S. G.; Kincaid, J. R. “Unveiling the crucial intermediates in androgen production”, Proc. Natl. Acad. Sci. USA 2015, 112, 15856-15861.
Mak, P. J.; Thammawichai, W.; Wiedenhoeft, D.; Kincaid, J. R. “Resonance Raman spectroscopy reveals pH-dependent active site structural changes of Lactoperoxidase Compound 0 and its ferryl heme O-O bond cleavage products”, J. Am. Chem. Soc. 2015, 137, 349-361.
Jones, E. M.; Monza, E.; Balakrishnan,G.; Blouin, G. C.; Mak, P. J.; Zhu, Q.; Kincaid,J. R.; Guallar, V.; Spiro, T. G. “Differential Control of Heme Reactivity in Alpha and Beta Subunits of Hemoglobin: A Combined Raman Spectroscopic and Computational Study”, J. Am. Chem. Soc. 2014, 136, 10325-10339.
Mak, P. J.; Luthra, A.; Sligar, S. G.; Kincaid; J. R. “Resonance Raman spectroscopy of the oxygenated intermediates of CYP19 implicates a Compound I intermediate in the final lyase step”, J. Am. Chem. Soc. 2014, 136, 4825-4828.
Rwere, F.; Mak, P. J.; Kincaid, J. R. “Resonance Raman determination of vinyl group orientations in different forms of myoglobins”, J. Raman Spectrosc., 2014, 45, 97-104.
Mak, P. J.; Gregory, M. C.; Sligar, S. G.; Kincaid, J. R. “Resonance Raman spectroscopy reveals that substrate structure selectively impacts the heme-bound diatomic ligands of CYP17”, Biochemistry, 2014, 53, 90-100 – highlighted on journal’s home page.
Mak, P. J.; Zhu, Q.; Kincaid, J. R. “Using resonance Raman cross-section data to estimate the spin state populations of Cytochromes P450”, J. Raman Spectrosc. 2013, 44, 1792-1794.
Gregory, M.; Mak, P. J.; Sligar, S. G.; Kincaid, J. R. “Differential Hydrogen Bonding in Human CYP17 Dictates Hydroxylation versus Lyase Chemistry”, Angew. Chem. Int. Ed., 2013, 52, 5342-5345.
Mak, P. J.; Yang, Y.; Im, S.-C.; Waskell, L. A.; Kincaid, J. R. “Experimental Documentation of the Structural Consequences of Hydrogen-Bonding Interactions to the Proximal Cysteine of a Cytochrome P450”, Angew. Chem. Int. Ed., 2012, 51, 10403-10407.
Mak, P. J.; Denisov, I.G.; Grinkova, Y. V.; Sligar, S. G.; Kincaid, J. R. “Defining CYP3A4 Structural Responses to Substrate Binding. Raman Spectroscopic Studies of a Nanodisc-Incorporated Mammalian Cytochrome P450”, J. Am. Chem. Soc., 2011, 133, 1357-1366.
Mak, P. J.; Zhang, H.; Hollenberg, P. F.; Kincaid, J. R. “Defining the Structural Consequences of Mechanism-Based Inactivation of Mammalian Cytochrome P450 2B4 Using Resonance Raman Spectroscopy”, J. Am. Chem. Soc. 2010, 132, 1494-1495.
Balakrishnan, G.; Ibrahim, M.; Mak, P. J.; Hata, J.; Kincaid, J. R.; Spiro, T. G. “Linking Conformation Change to Hemoglobin Activation Via Chain-Selective Time-resolved Resonance Raman Spectroscopy of Protoheme/Mesoheme Hybrids” J. Biol. Inorg. Chem., 2009, 14, 741-750.
Mak, P. J.; Kincaid, J. R. “Resonance Raman spectroscopic studies of hydroperoxo derivatives of cobalt-substituted myoglobin.” J. Inorg. Biochem., 2008, 102, 1952-1957.
8. Denisov, I. G.; Mak, P. J.; Makris, T. M.; Sligar, S. G.; Kincaid, J. R. “Resonance Raman Characterization of the Peroxo and Hydroperoxo Intermediates in Cytochrome P450.” J. Phys. Chem. A, 2008, 112, 13172-13179.
Mak P. J.; Kaluka D.; Manyumwa E. M.; Zhang H.; Deng T.; Kincaid J. R. “Defining Resonance Raman Spectral Response to Substrate Binding by Cytochrome P450.” Biopolymers, 2008, 89, 1045-1053.
Rwere, F.; Mak, P. J.; Kincaid, J. R. “Resonance Raman Interrogation of the Consequences of Heme Rotational Disorder in Myoglobin and Its Ligated Derivatives.” Biochemistry, 2008, 47, 12869-12877.
Mak, P. J.; Im, S.-C.; Zhang, H.; Waskell, L. A.; Kincaid, J. R. ”Resonance Raman Studies of Cytochrome P450 2B4 in Its Interactions with Substrates and Redox Partners.” Biochemistry, 2008, 47, 3950-3963 – “selected as hot article”.
Rwere F.; Mak P. J.; Kincaid J. R. “The impact of altered protein-heme interactions on the resonance Raman spectra of heme proteins. Studies of heme rotational disorder.” Biopolymers, 2008, 89, 179-186.
Mak, P. J.; Denisov, I. G.; Victoria, D.; Makris, T. M.; Deng, T.; Sligar, S. G.; Kincaid, J. R. “Resonance Raman Detection of the Hydroperoxo Intermediate in the Cytochrome P450 Enzymatic Cycle.” J. Am. Chem. Soc., 2007, 129, 6382-6383.
Podstawka, E.; Mak, P. J.; Kincaid, J. R.; Proniewicz, L. M. “Low frequency resonance Raman spectra of isolated α and β subunits of hemoglobin and their deuterated analogues.” Biopolymers, 2006, 83, 455-466.
Mak, P. J.; Podstawka, E.; Kincaid, J. R.; Proniewicz, L. M. “Effects of systematic peripheral group deuteration on the low-frequency resonance Raman spectra of myoglobin derivatives.” Biopolymers, 2004, 75, 217-228.