Year |
Citation |
Score |
2021 |
Jacobs AB, Banerjee R, Deweese DE, Braun A, Babicz JT, Gee LB, Sutherlin KD, Böttger LH, Yoda Y, Saito M, Kitao S, Kobayashi Y, Seto M, Tamasaku K, Lipscomb JD, ... Park K, et al. Nuclear Resonance Vibrational Spectroscopic Definition of the Fe(IV) Intermediate Q in Methane Monooxygenase and Its Reactivity. Journal of the American Chemical Society. PMID 34570980 DOI: 10.1021/jacs.1c05436 |
0.433 |
|
2020 |
Srnec M, Iyer SR, Dassama LMK, Park K, Wong SD, Sutherlin KD, Yoda Y, Kobayashi Y, Kurokuzu M, Saito M, Seto M, Krebs C, Bollinger JM, Solomon EI. Nuclear Resonance Vibrational Spectroscopic Definition of the Facial Triad Fe═O Intermediate in Taurine Dioxygenase: Evaluation of Structural Contributions to Hydrogen Atom Abstraction. Journal of the American Chemical Society. PMID 33103886 DOI: 10.1021/jacs.0c08903 |
0.46 |
|
2020 |
Shin J, Gwon S, Kim S, Lee J, Park K. Correlation between the C-C Cross-coupling Activity and C-to-Ni Charge Transfer Transition of High-valent Ni Complexes. Journal of the American Chemical Society. PMID 32057242 DOI: 10.1021/Jacs.9B10405 |
0.367 |
|
2019 |
Seo B, Jung GY, Lee SJ, Baek DS, Sa YJ, Ban HW, Son JS, Park K, Kwak SK, Joo SH. Monomeric MoS42–-Derived Polymeric Chains with Active Molecular Units for Efficient Hydrogen Evolution Reaction Acs Catalysis. 10: 652-662. DOI: 10.1021/Acscatal.9B02700 |
0.321 |
|
2018 |
Sutherlin KD, Wasada-Tsutsui Y, Mbughuni MM, Rogers MS, Park K, Liu LV, Kwak Y, Srnec M, Böttger LH, Frenette M, Yoda Y, Kobayashi Y, Kurokuzu M, Saito M, Seto M, et al. NRVS definition of O intermediates in an extradiol dioxygenase: correlation to crystallography and reactivity. Journal of the American Chemical Society. PMID 30418018 DOI: 10.1021/Jacs.8B06517 |
0.531 |
|
2018 |
Sutherlin KD, Rivard BS, Böttger LH, Liu LV, Rogers MS, Srnec M, Park K, Yoda Y, Kitao S, Kobayashi Y, Saito M, Seto M, Hu M, Zhao J, Lipscomb JD, et al. NRVS studies of the peroxide shunt intermediate in a Rieske dioxygenase and its relation to the native FeOreaction. Journal of the American Chemical Society. PMID 29618204 DOI: 10.1021/Jacs.8B01822 |
0.534 |
|
2018 |
Gunasekar G, Park K, Jeong H, Jung K, Park K, Yoon S. Molecular Rh(III) and Ir(III) Catalysts Immobilized on Bipyridine-Based Covalent Triazine Frameworks for the Hydrogenation of CO2 to Formate Catalysts. 8: 295. DOI: 10.3390/Catal8070295 |
0.323 |
|
2017 |
Park K, Li N, Kwak Y, Srnec M, Bell CB, Liu LV, Wong SD, Yoda Y, Kitao S, Seto M, Hu M, Zhao J, Krebs C, Bollinger JM, Solomon EI. Peroxide Activation for Electrophilic Reactivity by the Binuclear Non-heme Iron Enzyme AurF. Journal of the American Chemical Society. 139: 7062-7070. PMID 28457126 DOI: 10.1021/Jacs.7B02997 |
0.565 |
|
2016 |
Park K, Mera PE, Escalante-Semerena JC, Brunold TC. Resonance Raman spectroscopic study of the interaction between Co(II)rrinoids and the ATP:corrinoid adenosyltransferase PduO from Lactobacillus reuteri. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. PMID 27383231 DOI: 10.1007/S00775-016-1371-X |
0.639 |
|
2016 |
Solomon EI, Park K. Structure/function correlations over binuclear non-heme iron active sites. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. PMID 27369780 DOI: 10.1007/S00775-016-1372-9 |
0.529 |
|
2015 |
Park K, Mera PE, Moore TC, Escalante-Semerena JC, Brunold TC. Unprecedented Mechanism Employed by the Salmonella enterica EutT ATP:Co(I) rrinoid Adenosyltransferase Precludes Adenosylation of Incomplete Co(II) rrinoids. Angewandte Chemie (International Ed. in English). 54: 7158-61. PMID 25914129 DOI: 10.1002/Anie.201501930 |
0.621 |
|
2014 |
Park K, Solomon EI. Modeling nuclear resonance vibrational spectroscopic data of binuclear non-heme iron enzymes using density functional theory. Canadian Journal of Chemistry. 92: 975-978. PMID 28943644 DOI: 10.1139/Cjc-2014-0067 |
0.539 |
|
2014 |
Park K, Solomon EI. Modeling nuclear resonance vibrational spectroscopic data of binuclear nonheme iron enzymes using density functional theory Canadian Journal of Chemistry. 92: 975-978. DOI: 10.1139/cjc-2014-0067 |
0.435 |
|
2013 |
Kwak Y, Jiang W, Dassama LM, Park K, Bell CB, Liu LV, Wong SD, Saito M, Kobayashi Y, Kitao S, Seto M, Yoda Y, Alp EE, Zhao J, Bollinger JM, et al. Geometric and electronic structure of the Mn(IV)Fe(III) cofactor in class Ic ribonucleotide reductase: correlation to the class Ia binuclear non-heme iron enzyme. Journal of the American Chemical Society. 135: 17573-84. PMID 24131208 DOI: 10.1021/Ja409510D |
0.529 |
|
2013 |
Wong SD, Srnec M, Matthews ML, Liu LV, Kwak Y, Park K, Bell CB, Alp EE, Zhao J, Yoda Y, Kitao S, Seto M, Krebs C, Bollinger JM, Solomon EI. Elucidation of the Fe(IV)=O intermediate in the catalytic cycle of the halogenase SyrB2. Nature. 499: 320-3. PMID 23868262 DOI: 10.1038/Nature12304 |
0.565 |
|
2013 |
Park K, Bell CB, Liu LV, Wang D, Xue G, Kwak Y, Wong SD, Light KM, Zhao J, Alp EE, Yoda Y, Saito M, Kobayashi Y, Ohta T, Seto M, et al. Nuclear resonance vibrational spectroscopic and computational study of high-valent diiron complexes relevant to enzyme intermediates. Proceedings of the National Academy of Sciences of the United States of America. 110: 6275-80. PMID 23576760 DOI: 10.1073/Pnas.1304238110 |
0.556 |
|
2013 |
Park K, Brunold TC. Combined spectroscopic and computational analysis of the vibrational properties of vitamin B12 in its Co3+, Co2+, and Co1+ oxidation states. The Journal of Physical Chemistry. B. 117: 5397-410. PMID 23477417 DOI: 10.1021/Jp309392U |
0.588 |
|
2013 |
Park K, Tsugawa T, Furutachi H, Kwak Y, Liu LV, Wong SD, Yoda Y, Kobayashi Y, Saito M, Kurokuzu M, Seto M, Suzuki M, Solomon EI. Nuclear resonance vibrational spectroscopy and DFT study of peroxo-bridged biferric complexes: Structural insight into peroxo intermediates of binuclear non-heme iron enzymes Angewandte Chemie - International Edition. 52: 1294-1298. PMID 23225363 DOI: 10.1002/Anie.201208240 |
0.531 |
|
2012 |
Park K, Mera PE, Escalante-Semerena JC, Brunold TC. Spectroscopic characterization of active-site variants of the PduO-type ATP:corrinoid adenosyltransferase from Lactobacillus reuteri: insights into the mechanism of four-coordinate Co(II)corrinoid formation. Inorganic Chemistry. 51: 4482-94. PMID 22480351 DOI: 10.1021/Ic202096X |
0.621 |
|
2009 |
Brunold TC, Conrad KS, Liptak MD, Park K. Spectroscopically validated density functional theory studies of the B12 cofactors and their interactions with enzyme active sites Coordination Chemistry Reviews. 253: 779-794. DOI: 10.1016/J.Ccr.2008.09.013 |
0.644 |
|
2008 |
Park K, Mera PE, Escalante-Semerena JC, Brunold TC. Kinetic and spectroscopic studies of the ATP:corrinoid adenosyltransferase PduO from Lactobacillus reuteri: substrate specificity and insights into the mechanism of Co(II)corrinoid reduction. Biochemistry. 47: 9007-15. PMID 18672897 DOI: 10.1021/Bi800419E |
0.654 |
|
2008 |
St Maurice M, Mera P, Park K, Brunold TC, Escalante-Semerena JC, Rayment I. Structural characterization of a human-type corrinoid adenosyltransferase confirms that coenzyme B12 is synthesized through a four-coordinate intermediate. Biochemistry. 47: 5755-66. PMID 18452306 DOI: 10.1021/Bi800132D |
0.649 |
|
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