非血红素铁酶中动态配位变化对C‒H键选择性胺化反应的调控机制

doi:10.1016/S1872-2067(24)60064-1

催化学报 ›› 2024, Vol. 62: 131-144.DOI: 10.1016/S1872-2067(24)60064-1

非血红素铁酶中动态配位变化对C‒H键选择性胺化反应的调控机制

张璇^a^,^b, 刘佳^a, 廖浪星^a, 王子宽^c, 王斌举^a^,^*()

^a厦门大学化学化工学院, 固体表面物理化学国家重点实验室, 福建省理论与计算化学重点实验室, 福建厦门 361005, 中国
^b宁波大学新药技术研究院, 浙江宁波 315211, 中国
^c马克斯-普朗克煤炭研究所, 德国

收稿日期:2024-03-26 接受日期:2024-04-29 出版日期:2024-07-18 发布日期:2024-07-10
通讯作者: *电子邮箱: wangbinju2018@xmu.edu.cn (王斌举).
基金资助:
国家自然科学基金(22122305);国家自然科学基金(21907082);国家自然科学基金(22073077);国家自然科学基金(22303043);中国博士后科学基金(2023M742917);宁波市甬江人才工程项目

Coordination dynamics of iron enables the selective C-N coupling but bypasses unwanted C-H hydroxylation in Fe(II)/α-ketoglutarate- dependent non-heme enzymes

Xuan Zhang^a^,^b, Jia Liu^a, Langxing Liao^a, Zikuan Wang^c, Binju Wang^a^,^*()

^aState Key Laboratory of Physical Chemistry of Solid Surfaces and Fujian Provincial Key Laboratory of Theoretical and Computational Chemistry, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen 361005, Fujian, China
^bInstitute of Drug Discovery Technology, Ningbo University, Ningbo 315211, Zhejiang, China
^cMax-Planck-Institut für Kohlenforschung, Kaiser-Wilhelm-Platz 1, Mülheim an der Ruhr 45470, Germany

Received:2024-03-26 Accepted:2024-04-29 Online:2024-07-18 Published:2024-07-10
Contact: *E-mail: wangbinju2018@xmu.edu.cn (B. Wang).
Supported by:
National Natural Science Foundation of China(22122305);National Natural Science Foundation of China(21907082);National Natural Science Foundation of China(22073077);National Natural Science Foundation of China(22303043);China Postdoctoral Science Foundation(2023M742917);Ningbo Yongjiang Talent Programme

摘要/Abstract

摘要：

氮杂环丙烷结构广泛存在于天然生物碱中, 具有杀菌､抗癌等作用. 然而, 目前关于生物体系在合成氮杂环丙烷结构过程中如何克服氮杂环丙烷高环张力带来的热力学不利因素, 以及如何避免形成热力学更稳定的羟基化副产物的报道较少. TqaL_NC酶是目前非血红素酶家族中唯一一种能够依赖α-酮戊二酸活化C‒H键, 进而生成氮杂环丙烷结构的酶. 深入探究TqaL_NC酶选择性生成氮杂环丙烷结构并避免羟基化副产物的机制, 有助于深入理解非血红素铁酶家族在C‒H键活化及官能化过程中的选择性调控机理.

本文以TqaL_NC酶的晶体结构为基础, 采用分子动力学(MD)模拟以及量子力学-分子力学(QM/MM)等多尺度模拟方法对TqaL_NC酶与L-缬氨酸(L-Val)、TqaL_NC酶与L-异亮氨酸(L-Ile)和F345A-TqaL_NC酶与L-异亮氨酸(L-Ile)三个反应过程进行了详细的机理研究. 结果表明, TqaL_NC酶在反应过程中生成的直立式构象的Fe(IV)=O物种会通过构象异构化获得赤道面式构象, 为底物(L-Val､L-Ile､L-homoalaine)上NH₃⁺与Fe的配位提供结构基础. 在水和关键酸性残基的介导下, 底物NH₃⁺两次脱去质子与Fe(IV)=O物种配位, 生成HN-Fe(IV)=O结构. 随后, Fe(IV)=O物种攫取底物H原子, 生成HN-Fe(III)-OH中间体. 此时NH回弹反应比传统的OH回弹反应在动力学上更有优势, 因此选择性地生成了氮杂环丙烷产物. 在反应过程中, 底物侧链与周围氨基酸的位阻效应是影响NH回弹反应能垒的重要因素. 通过改变底物侧链大小(L-Val→L-Ile)以及附近氨基酸的突变(F345A)实验, 证实了该结论. 本文还通过理论计算预测了TqaL_NC酶与L-高丙氨酸的反应产物为羟基化产物, 并通过新的实验证据进一步支持了理论预测的机理. 此外, 在HN-Fe(III)-OH结构中, 通过前线轨道理论分析发现, dπ*_Fe-N, dπ*_Fe-OH轨道的能量差是影响NH/OH回弹反应能垒的另一重要因素. 当底物NH与Fe配位时, 其配位作用能够使得dπ*_Fe-N以及dπ*_Fe-OH轨道有效分裂, 这种分裂进而影响了反应路径的选择性, 确保氮杂环丙烷产物的生成.

综上, 本文提出了依赖α-酮戊二酸酶催化合成氮杂环丙烷结构的新机理. 研究发现, Fe中心的动态配位效应在实现C‒H键选择性胺化反应并避免C‒H键羟基化反应中起到了关键作用. 该理论为非血红素Fe酶催化的非羟基化反应提供了新的见解, 并为探索包括C‒N/C‒S/C‒O等重要生物合成反应新机理的探究提供了新思路.

关键词: 联合量子力学-分子力学方法, C?H键活化, 非血红素酶, 胺化反应, 羟基化反应

Abstract:

Non-heme Fe(II)/α-ketoglutarate (αKG)-dependent enzymes catalyze numerous C-H activation and functionalization reactions. However, how αKG-dependent non-heme enzymes catalyzed C-H functionalization beyond the hydroxylation is largely unknown. Here, we addressed this issue in Fe(II)/ αKG-dependent oxygenase TqaL_Nc, which catalyzes the selective C-H amination but bypasses the thermodynamically favored C-H hydroxylation. Here, the extensive computational studies have shown that the aziridine formation involves the conformational change of the Fe(IV)=O species from the axial configuration to the equatorial one, the substrate deprotonation of NH₃⁺ group to form the NH-ligated intermediate, the C-H activation by the equatorial Fe(IV)=O species. Such mechanistic scenario has been cross-validated by oxidation of various substrates by TqaL_Nc and its variants, including the available experiments and our new experiments. While the presence of steric hindrance between the substrate and the second-sphere residues would inhibit the aziridination process, the intrinsic reactivity of aziridination vs. hydroxylation is dictated by the energy splitting between two key redox-active dπ* frontier molecular orbitals: dπ*_Fe-N and dπ*_Fe-OH. The present findings highlight the key roles of the coordination change and dynamics of iron cofactor in dictating the catalysis of non-heme enzymes and have far-reaching implications for the other non-heme Fe(II)/αKG-dependent enzymes catalyzed C-H functionalization beyond the hydroxylation.

Key words: Quantum mechanics/molecular, mechanics, C-H functionalization, Non-heme enzymes, Aziridination, Hydroxylation

张璇, 刘佳, 廖浪星, 王子宽, 王斌举. 非血红素铁酶中动态配位变化对C‒H键选择性胺化反应的调控机制[J]. 催化学报, 2024, 62: 131-144.

Xuan Zhang, Jia Liu, Langxing Liao, Zikuan Wang, Binju Wang. Coordination dynamics of iron enables the selective C-N coupling but bypasses unwanted C-H hydroxylation in Fe(II)/α-ketoglutarate- dependent non-heme enzymes[J]. Chinese Journal of Catalysis, 2024, 62: 131-144.

×
扫码分享

导出引用管理器 EndNote|Ris|BibTeX

链接本文: https://www.cjcatal.com/CN/10.1016/S1872-2067(24)60064-1

https://www.cjcatal.com/CN/Y2024/V62/I7/131

图/表 8

Fig. 1. Reactions, crystal structure and two possible mechanisms of TqaLNc. (a) Reactions catalyzed by TqaLNc with different substrates. L-Val is oxidated to aziridine product; L-Ile is oxidated to aziridine product and hydroxylation product. (b) Crystal structure of TqaLNc (PDB: 7EEH). Left part is the whole view of the protein. The right part is an enlarged view of the active site with the substrate docked into the active site and the loops ABC have been predicted by AlphaFold2. (c) Two possible catalytic mechanisms of TqaLNc for the formation of aziridine product.

Fig. 2. The formation and conformation isomerization of Fe(IV)=O species. (a) QM(UB3LYP/B2)/MM relative energies (kcal mol?1) for the Fe(IV)=O species formation with substrate L-Val by TqaLNc. The dispersion corrections and ZPEs are included in the relative energies. (b) QM(UB3LYP/B1)/MM-optimized geometries of key TS1b species involved in the reaction. Key distances are given in ?. Geometries of TS1a and TS1b are shown in Fig. S1. (c) (UB3LYP/B2)/MM relative energies (kcal mol?1) for the conformation change between structures ax-FeO and eq-FeO. The dispersion corrections and ZPEs are included in the relative energies and QM(UB3LYP/B1)/MM-optimized geometries of key species involved in the reaction. Key distances are given in ?.

Fig. 3. Aziridine formation from the axial Fe(IV)=O species through mechanism A in Fig. 1(c). (a) Representation snapshot of MD simulation of axial Fe(IV)=O species (ax-FeO). (b) QM(UB3LYP/B1)/MM relative energies (kcal mol?1) for the aziridine formation with substrate L-Val by the axial Fe(IV)=O species (ax-FeO) in three proposed routes. The dispersion corrections are included in the relative energies.

Fig. 4. The second deprotonation process beginning from F1’ and aziridine formation through mechanism B in Fig. 1(c). (a) QM(UB3LYP/B2)/MM relative energies (kcal mol?1) for the conversion from structure F1’ to F2. The dispersion corrections and ZPEs are included in the relative energies. QM(UB3LYP/B1)/MM-optimized geometries of key species involved in the reaction. Key distances are given in ?. (b) QM(UB3LYP/B2)/MM relative energies (kcal mol?1) for the aziridine formation reaction with substrate L-Val by TqaLNc via mechanism B on quintet state. The dispersion corrections and ZPEs are included in the relative energies. (c) QM(UB3LYP/B1)/MM-optimized geometries of key species involved in the reaction. Key distances are given in ?.

Fig. 5. Barriers of aziridination vs. hydroxylation between various substrates and enzymes. QM(UB3LYP/B2)/MM relative energies (kcal mol?1) for the TS barriers of aziridination reaction and hydroxylation reaction and QM(UB3LYP/B1)/MM-optimized geometries of key species of the Fe(III)-OH species for (a) the oxidation of substrate L-Val by TqaLNc, also see Fig. 4 for the full energy profile. (b) The oxidation of substrate L-Ile by TqaLNc, also see Fig. S13 for the full energy profile. (c) The oxidation of substrate L-Ile by F345A-TqaLNc, also see Fig. S14 for the full energy profile. The dispersion corrections and ZPEs are included in the relative energies. Key distances are given in ?.

Fig. 6. Further validation of mechanism through oxidation of L-homoalanine by TqaLNc through computational and experimental methods. (a) QM(UB3LYP/B2)/MM relative energies (kcal mol?1) for the aziridine formation reaction with substrate L-homoalanine by TqaLNc via mechanism B on quintet state. The dispersion corrections and ZPEs are included in the relative energies. (b) QM(UB3LYP/B1)/MM-optimized geometries of key species involved in the reaction. Key distances are given in ?. (c) LC-MS EIC results on new substrate L-homoalanine (1) oxidized by TqaLNc. EIC of [M+H]+ signals from Dns-1 (m/z = 335.1077), Dns-2 (m/z = 351.1026), and the product of 1 catalyzed by TqaLNc (m/z = 351.1024).

Fig. 7. Frontier orbitals calculated for (a) the substrate radical intermediate F3 (see Fig. 4 for the full reaction process) and (b) Int5 (see Fig. S18 for the full reaction process). The FMOs, dπ*Fe-N, dπ*Fe-OH, dσ*Fe-N, and dπ*Fe-OH are operative in aziridination and hydroxylation, respectively. The arrows indicate the interaction of the substrate orbital with FMOs and energy barrier gaps are in kcal mol?1.

Fig. 8. Proposed catalytic cycle of the aziridine formation by TqaLNc in this study.

参考文献

[1]	F. M. Ismail, D. O. Levitsky, V. M. Dembitsky, Eur. J. Med. Chem., 2009, 44, 3373-3387.
[2]	R. Yue, M. Li, Y. Wang, Y. Guan, J. Zhang, Z. Yan, F. Liu, F. Lu, H. Zhang, Eur. J. Med. Chem., 2020, 204, 112639.
[3]	S. Alcaro, R. S. Coleman, J. Med. Chemv., 2000, 43, 2783-2788.
[4]	S. E. Wolkenberg, D. L. Boger, Chem. Rev., 2002, 102, 2477-2495.
[5]	C. J. Thibodeaux, W. C. Chang, H. W. Liu, Chem. Rev., 2012, 112, 1681-1709.
[6]	R. Bunno, T. Awakawa, T. Mori, I. Abe, Angew. Chem. Int. Ed., 2021, 60, 15827-15831.
[7]	H. Tsutsumi, Y. Katsuyama, M. Izumikawa, M. Takagi, M. Fujie, N. Satoh, K. Shin-Ya, Y. Ohnishi, J. Am. Chem. Soc., 2018, 140, 6631-6639.
[8]	S. Kurosawa, F. Hasebe, H. Okamura, A. Yoshida, K. Matsuda, Y. Sone, T. Tomita, T. Shinada, H. Takikawa, T. Kuzuyama, S. Kosono, M. Nishiyama, J. Am. Chem. Soc., 2022, 144, 16164-16170.
[9]	S. Martinez, R. P. Hausinger, J. Biol. Chem., 2015, 290, 20702-20711.
[10]	L. F. Wu, S. Meng, G. L. Tang, Biochim. Biophys. Acta-Proteins Proteomics, 2016, 1864, 453-470.
[11]	S.-S. Gao, N. Naowarojna, R. Cheng, X. Liu, P. Liu, Nat. Prod. Rep., 2018, 35, 792-837.
[12]	C. R. Zwick, H. Renata, ACS Catal., 2023, 13, 4853-4865.
[13]	T. Awakawa, T. Mori, R. Ushimaru, I. Abe, Nat. Prod. Rep., 2023, 40, 46-61.
[14]	R. Ushimaru, M. W. Ruszczycky, W. C. Chang, F. Yan, Y. N. Liu, H. W. Liu, J. Am. Chem. Soc., 2018, 140, 7433-7436.
[15]	H. S. Ali, J. Warwicker, S. P. de Visser, ACS Catal., 2023, 13, 10705-10721.
[16]	Y. T. Lin, H. S. Ali, S. P. de Visser, Chem. Eur. J., 2022, 28, e202103982.
[17]	H. Tao, T. Mori, H. Chen, S. Lyu, A. Nonoyama, S. Lee, I. Abe, Nat. Commun., 2022, 13, 95.
[18]	X. Li, T. Awakawa, T. Mori, M. Ling, D. Hu, B. Wu, I. Abe, J. Am. Chem. Soc., 2021, 143, 21425-21432.
[19]	H. Tang, Y. Tang, I. V. Kurnikov, H. J. Liao, N. L. Chan, M. G. Kurnikova, Y. Guo, W. C. Chang, ACS Catal., 2021, 11, 7186-7192.
[20]	J. Li, H. J. Liao, Y. Tang, J. L. Huang, L. Cha, T. S. Lin, J. L. Lee, I. V. Kurnikov, M. G. Kurnikova, W. C. Chang, N. L. Chan, Y. Guo, J. Am. Chem. Soc., 2020, 142, 6268-6284.
[21]	R. Ushimaru, M. W. Ruszczycky, H. W. Liu, J. Am. Chem. Soc., 2019, 141, 1062-1066.
[22]	T. Y. Chen, W. C. Chang, Proc. Natl. Acad. Sci. U. S. A., 2021, 118, e2109992118
[23]	W. Singh, D. Quinn, T. S. Moody, M. Huang, J. Phys. Chem. B, 2019, 123, 7801-7811.
[24]	T.-Y. Chen, S. Xue, W.-C. Tsai, T.-C. Chien, Y. Guo, W.-C. Chang, ACS Catal., 2020, 11, 278-282.
[25]	T. Mori, Y. Nakashima, H. Chen, S. Hoshino, T. Mitsuhashi, I. Abe, Chem. Commun., 2022, 58, 5510-5513.
[26]	C. Y. Lai, I. W. Lo, R. T. Hewage, Y. C. Chen, C. T. Chen, C. F. Lee, S. Lin, M. C. Tang, H. C. Lin, Angew. Chem. Int Ed., 2017, 56, 9478-9482.
[27]	W. Kim, T. Y. Chen, L. Cha, G. Zhou, K. Xing, N. K. Canty, Y. Zhang, W. C. Chang, Nat. Commun., 2022, 13, 5343.
[28]	X. Li, S. Xue, Y. Guo, W. C. Chang, J. Am. Chem. Soc., 2022, 144, 8257-8266.
[29]	E. I. Parkinson, H. G. Lakkis, A. A. Alwali, M. E. M. Metcalf, R. Modi, W. W. Metcalf, Angew. Chem. Int. Ed., 2022, 61, e202206173.
[30]	N. P. Dunham, W. C. Chang, A. J. Mitchell, R. J. Martinie, B. Zhang, J. A. Bergman, L. J. Rajakovich, B. Wang, A. Silakov, C. Krebs, A. K. Boal, J. M. Jr. Bollinger, J. Am. Chem. Soc., 2018, 140, 7116-7126.
[31]	Y. Nakashima, T. Mitsuhashi, Y. Matsuda, M. Senda, H. Sato, M. Yamazaki, M. Uchiyama, T. Senda, I. Abe, J. Am. Chem. Soc., 2018, 140, 9743-9750.
[32]	Y. Nakashima, T. Mori, H. Nakamura, T. Awakawa, S. Hoshino, M. Senda, T. Senda, I. Abe, Nat. Commun., 2018, 9, 104.
[33]	X. Li, R. Shimaya, T. Dairi, W.-C Chang, Y. Ogasawara, Angew. Chem. Int. Ed., 2022, 61, e202113189.
[34]	R. Ushimaru, L. Cha, S. Shimo, X. Li, J. C. Paris, T. Mori, K. Miyamoto, L. Coffer, M. Uchiyama, Y. Guo, W. C. Chang, I. Abe, J. Am. Chem. Soc., 2023, 145, 24210-24217.
[35]	Z. Zhang, T. J. Smart, H. Choi, F. Hardy, C. T. Lohans, M. I. Abboud, M. S. W. Richardson, R. S. Paton, M. A. McDonough, C. J. Schofield, Proc. Natl. Acad. Sci. U. S. A., 2017, 114, 4667-4672.
[36]	R. A. Copeland, S. Zhou, I. Schaperdoth, T. K. C. Shoda, J. M. Jr. Bollinger, C. Krebs, Science, 2021, 373, 1489-1494.
[37]	R. A. Copeland, K. M. Davis, T. K. C. Shoda, E. J. Blaesi, A. K. Boal, C. Krebs, J. M. Jr. Bollinger, J. Am. Chem. Soc., 2021, 143, 2293-2303.
[38]	C. C. G. Yeh, S. Ghafoor, J. K. Satpathy, T. Mokkawes, C. V. Sastri, S. P. de Visser, ACS Catal., 2022, 12, 3923-3937.
[39]	S. Shimo, R. Ushimaru, A. Engelbrecht, M. Harada, K. Miyamoto, A. Kulik, M. Uchiyama, L. Kaysser, I. Abe, J. Am. Chem. Soc., 2021, 143, 18413-18418.
[40]	J. W. Slater, C. Y. Lin, M. E. Neugebauer, M. J. McBride, D. Sil, M. A. Nair, B. J. Katch, A. K. Boal, M. C. Y. Chang, A. Silakov, C. Krebs, J. M. Jr. Bollinger, Biochemistry, 2023, 62, 2480-2491.
[41]	A. Timmins, S. P. D. Visser, Catalysts, 2018, 8, 314.
[42]	S. D. Wong, M. Srnec, M. L. Matthews, L. V. Liu, Y. Kwak, K. Park, C. B. III Bell, E. E. Alp, J. Zhao, Y. Yoda, S. Kitao, M. Seto, C. Krebs, J. M. Jr. Bollinger, E. I. Solomon, Nature, 2013, 499, 320-323.
[43]	M. L. Hillwig, X. Liu, Nat. Chem. Biol., 2014, 10, 921-923.
[44]	A. J. Mitchell, Q. Zhu, A. O. Maggiolo, N. R. Ananth, M. L. Hillwig, X. Liu, A. K. Boal, Nat. Chem. Biol., 2016, 12, 636-640.
[45]	L. C. Blasiak, F. H. Vaillancourt, C. T. Walsh, C. L. Drennan, Nature, 2006, 440, 368-371.
[46]	N. P. Dunham, J. M. Del Rio Pantoja, B. Zhang, L. J. Rajakovich, B. D. Allen, C. Krebs, A. K. Boal, J. M. Jr. Bollinger, J. Am. Chem. Soc., 2019, 141, 9964-9979.
[47]	T. Mori, R. Zhai, R. Ushimaru, Y. Matsuda, I. Abe, Nat. Commun., 2021, 12, 4417.
[48]	H. Tao, R. Ushimaru, T. Awakawa, T. Mori, M. Uchiyama, I. Abe, J. Am. Chem. Soc., 2022, 144, 21512-21520.
[49]	M. Srnec, S. R. Iyer, L. M. K. Dassama, K. Park, S. D. Wong, K. D. Sutherlin, Y. Yoda, Y. Kobayashi, M. Kurokuzu, M. Saito, M. Seto, C. Krebs, J. M. Jr. Bollinger, E. I. Solomon, J. Am. Chem. Soc., 2020, 142, 18886-18896.
[50]	J. Pan, E. S. Wenger, M. L. Matthews, C. J. Pollock, M. Bhardwaj, A. J. Kim, B. D. Allen, R. B. Grossman, C. Krebs, J. M. Jr. Bollinger, J. Am. Chem. Soc., 2019, 141, 15153-15165.
[51]	J. M. Elkins, M. J. Ryle, I. J. Clifton, J. C. D. Hotopp, J. S. Lloyd, N. I. Burzlaff, J. E. Baldwin, R. P. Hausinger, P. L. Roach, Biochemistry, 2002, 41, 5185-5192.
[52]	K. M. Davis, M. Altmyer, R. J. Martinie, I. Schaperdoth, C. Krebs, J. M. Jr. Bollinger, A. K. Boal, Biochemistry, 2019, 58, 4218-4223.
[53]	Z. H. Zhang, J. S. Ren, D. K. Stammers, J. E. Baldwin, K. Harlos, C. J. Schofield, Nat. Struct. Biol., 2000, 7, 127-133.
[54]	W. Yan, H. Song, F. Song, Y. Guo, C. H. Wu, A. S. Her, Y. Pu, S. Wang, N. Naowarojna, A. Weitz, M. P. Hendrich, C. E. Costello, L. Zhang, P. Liu, Y. J. Zhang, Nature, 2015, 527, 539-543.
[55]	L. Wu, Z. Wang, Y. Cen, B. Wang, J. Zhou, Angew. Chem. Int. Ed., 2022, 61, e202112063.
[56]	C. Y. Lin, A. L. Munoz, T. N. Laremore, A. Silakov, C. Krebs, A. K. Boal, J. M. Jr. Bollinger, ACS Catal., 2022, 12, 6968-6979.
[57]	S. P. de Visser, D. Kumar, Iron-Containing Enzymes: Versatile Catalysts of Hydroxylation Reactions in Nature, The Royal Society of Chemistry, UK, 2011.
[58]	S. P. de Visser, Chem. Rec., 2018, 18, 1501-1516.
[59]	I. Abe, Chem. Pharm. Bull., 2020, 68, 823-831.
[60]	S. P. de Visser, Chem. Eur. J., 2020, 26, 5308-5327.
[61]	A. Wojcik, M. Radon, T. Borowski, J. Phys. Chem. A, 2016, 120, 1261-1274.
[62]	B. Yu, W. C. Edstrom, J. Benach, Y. Hamuro, P. C. Weber, B. R. Gibney, J. F. Hunt, Nature, 2006, 439, 879-884.
[63]	H. Liu, J. Llano, J. W. Gauld, J. Phys. Chem. B, 2009, 113, 4887-4898.
[64]	M. G. Quesne, R. Latifi, L. E. Gonzalez-Ovalle, D. Kumar, S. P. de Visser, Chem. Eur. J., 2014, 20, 435-446.
[65]	X. Song, J. Lu, W. Lai, Phys. Chem. Chem. Phys., 2017, 19, 20188-20197.
[66]	H. Su, X. Sheng, W. Zhu, G. Ma, Y. Liu, ACS Catal., 2017, 7, 5534-5543.
[67]	W. C. Chang, Y. Guo, C. Wang, S. E. Butch, A. C. Rosenzweig, A. K. Boal, C. Krebs, J. M. Jr. Bollinger, Science, 2014, 343, 1140-1144.
[68]	G. Ma, W. Zhu, H. Su, N. Cheng, Y. Liu, ACS Catal., 2015, 5, 5556-5566.
[69]	J. Xue, J. Lu, W. Lai, Phys. Chem. Chem. Phys., 2019, 21, 9957-9968.
[70]	S. S. Chaturvedi, R. Ramanan, J. Hu, R. P. Hausinger, C. Z. Christov, ACS Catal., 2021, 11, 1578-1592.
[71]	D. W. Kastner, A. Nandy, R. Mehmood, H. J. Kulik, ACS Catal., 2023, 13, 2489-2501.
[72]	T. Borowski, H. Noack, M. Radon, K. Zych, P. E. M. Siegbahn, J. Am. Chem. Soc., 2010, 132, 12887-12898.
[73]	X. Zhang, Z. Wang, J. Gao, W. Liu, Phys. Chem. Chem. Phys., 2020, 22, 8699-8712.
[74]	R.-N. Li, S.-L. Chen, Chem. Asian J., 2022, 17, e202200438.
[75]	M. E. Neugebauer, K. H. Sumida, J. G. Pelton, J. L. McMurry, J. A. Marchand, M. C. Y. Chang, Nat. Chem. Biol., 2019, 15, 1009-1016.
[76]	J. Zhang, Y. Li, W. Yuan, X. Zhang, Y. Si, B. Wang, ChemRxiv, 2024, doi: 10.26434/chemrxiv-2024-4ps0h.
[77]	R. Ushimaru, I. Abe, ACS Catal., 2022, 13, 1045-1076.
[78]	A. W. Senior, R. Evans, J. Jumper, J. Kirkpatrick, L. Sifre, T. Green, C. Qin, A. Zidek, A. W. R. Nelson, A. Bridgland, H. Penedones, S. Petersen, K. Simonyan, S. Crossan, P. Kohli, D. T. Jones, D. Silver, K. Kavukcuoglu, D. Hassabis, Nature, 2020, 577, 706-710.
[79]	O. Trott, A. J. Olson, J. Comput. Chem., 2010, 31, 455-461.
[80]	H. Li, A. D. Robertson, J. H. Jensen, Proteins-Struct. Funct. Bioinformat., 2005, 61, 704-721.
[81]	D. A. I. Y,. B.-S. I. Y. Case, S. R. Brozell, D. S. Cerutti, T. E. Cheatham, III V,. W. D. Cruzeiro, T. A. Darden, R. E. Duke, D. Ghoreishi, M. K. Gilson, H. Gohlke, A. W. Goetz, D. Greene, R. Harris, N. Homeyer, S. Izadi, A. Kovalenko, T. Kurtzman, T. S. Lee, S. LeGrand, P. Li, C. Lin, J. Liu, T. Luchko, R. Luo, D. J. Mermelstein, K. M. Merz, Y. Miao, G. Monard, C. Nguyen, H. Nguyen, I. Omelyan, A. Onufriev, F. Pan, R. Qi, D. R. Roe, A. Roitberg, C. Sagui, S. Schott-Verdugo, J. Shen, C. L. Simmerling, J. Smith, R. Salomon-Ferrer, J. Swails, R. C. Walker, J. Wang, H. Wei, R. M. Wolf, X. Wu, L. Xiao, D. M. York P., A. Kollman, AMBER 2018; University of California, San Francisco, 2018.
[82]	J. M. Wang, R. M. Wolf, J. W. Caldwell, P. A. Kollman, D. A. Case, J. Comput. Chem., 2004, 25, 1157-1174.
[83]	C. I. Bayly, P. Cieplak, W. D. Cornell, P. A. Kollman, J. Phys. Chem., 1993, 97, 10269-10280.
[84]	P. Li, K. M. Jr. Merz, J. Chem. Inf. Model., 2016, 56, 599-604.
[85]	W. L. Jorgensen, J. Chandrasekhar, J. D. Madura, R. W. Impey, M. L. Klein, J. Chem. Phys., 1983, 79, 926-935.
[86]	J. A. Maier, C. Martinez, K. Kasavajhala, L. Wickstrom, K. E. Hauser, C. Simmerling, J. Chem. Theory Comput., 2015, 11, 3696-3713.
[87]	J. P. Ryckaert, G. Ciccotti, H. J. C. Berendsen, J. Comput. Phys., 1977, 23, 327-341.
[88]	P. Sherwood, A. H. de Vries, M. F. Guest, G. Schreckenbach, C. R. A. Catlow, S. A. French, A. A.Sokol, S. T. Bromley, W. Thiel, A. J. Turner, S. Billeter, F. Terstegen, S. Thiel, J. Kendrick, S. C. Rogers, J. Casci, M. Watson, F. King, E. Karlsen, M. Sjøvoll, A. Fahmi, A. Schäfer, C. Lennartz, J. Mol. Struc., 2003, 632, 1-28.
[89]	R. Ahlrichs, M. Bar, M. Haser, H. Horn, C. Kolmel, Chem. Phys. Lett., 1989, 162, 165-169.
[90]	W. Smith, T. R. Forester, J. Mol. Graphics., 1996, 14, 136-141.
[91]	D. Bakowies, W. Thiel, J. Phys. Chem., 1996, 100, 10580-10594.
[92]	A. H. de Vries, P. Sherwood, S. J. Collins, A. M. Rigby, M. Rigutto, G. J. Kramer, J. Phys. Chem. B, 1999, 103, 6133-6141.
[93]	P. Sherwood, A. H. de Vries, S. J. Collins, S. P. Greatbanks, N. A. Burton, M. A. Vincent, I. H. Hillier, Faraday Discuss., 1997, 106, 79-92.
[94]	C. Lee, W. Yang, R. G. Parr, Phys. Rev. B, 1988, 37, 785-789.
[95]	M. Srnec, E. I. Solomon, J. Am. Chem. Soc., 2017, 139, 2396-2407.
[96]	T.-Y. Chen, Z. Zheng, X. Zhang, J. Chen, L. Cha, Y. Tang, Y. Guo, J. Zhou, B. Wang, H.-W. Liu, W.-C. Chang, ACS Catal., 2022, 12, 2270-2279.
[97]	M. R. A. Blomberg, T. Borowski, F. Himo, R.-Z. Liao, P. E. M. Siegbahn, Chem. Rev., 2014, 114, 3601-3658.
[98]	W. J. Wei, H. X. Qian, W. J. Wang, R. Z. Liao, Front. Chem., 2018, 6, 638.
[99]	S. Grimme, J. Comput. Chem., 2004, 25, 1463-1473.
[100]	J. Huang, C. Li, B. Wang, D. A. Sharon, W. Wu, S. Shaik, ACS Catal., 2016, 6, 2694-2704.
[101]	H. Li, Y. Liu, ACS Catal., 2020, 10, 2942-2957.
[102]	J. Kaestner, J. M. Carr, T. W. Keal, W. Thiel, A. Wander, P. Sherwood, J. Phys. Chem. A, 2009, 113, 11856-11865.
[103]	A. Bassan, T. Borowski, C. J. Schofield, P. E. Siegbahn, Chem. Eur. J., 2006, 12, 8835-8846.
[104]	H. Li, J. W. Huang, L. Dai, H. Zheng, S. Dai, Q. Zhang, L. Yao, Y. Yang, Y. Yang, J. Min, R. T. Guo, C. C. Chen, Nat. Commun., 2023, 14, 7425.
[105]	J. Pan, E. Wenger, C.-Y. Lin, B. Zhang, D. Sil, I. Schaperdoth, S. Saryazdi, R. Grossman, C. Krebs, J. M. Jr. Bollinger, ChemRxiv, 2024, DOI 10.26434/chemrxiv-2024-6qggj.
[106]	L. Cha, J. C. Paris, B. Zanella, M. Spletzer, A. Yao, Y. Guo, W. C. Chang, J. Am. Chem. Soc., 2023, 145, 6240-6246.

非血红素铁酶中动态配位变化对C‒H键选择性胺化反应的调控机制

Coordination dynamics of iron enables the selective C-N coupling but bypasses unwanted C-H hydroxylation in Fe(II)/α-ketoglutarate- dependent non-heme enzymes

RichHTML

PDF

Supporting Information

可视化

摘要/Abstract

引用本文

使用本文

扫码分享

图/表 8

参考文献

相关文章 3

编辑推荐

Metrics

[1]	马雷, 严丽, 陆安慧, 丁云杰. Ni-Re/SiO₂催化剂中Ni颗粒尺寸对乙醇胺催化胺化反应的影响[J]. 催化学报, 2019, 40(4): 567-579.
[2]	张涛. 糖类化学催化转化为氨基酸[J]. 催化学报, 2018, 39(6): 1013-1016.
[3]	刘文欢;郭鹏;苏际;胡佳;王艳梅;刘娜;郭洪臣. 钛硅分子筛TS-1的酸性表征及酸催化性能[J]. 催化学报, 2009, 30(6): 482-484.