生物催化C—C成键反应及其应用

doi:10.11949/0438-1157.20201098

摘要/Abstract

摘要：

C—C成键反应是有机合成中构建有机分子碳骨架的关键反应。综述了近年来生物催化Aldol、Acyloin condensation、Stetter 、Pictet-Spengler 等C—C成键反应的关键酶制剂，以及这些酶制剂催化合成β-羟基-α-氨基、α-羟基酮、1，4-二酮、β-咔啉、四氢异喹啉等精细化学品的研究进展。此外，还对生物催化C—C成键反应的应用前景进行了展望，从而扩大生物催化在化学品生产中的应用范围。

关键词: C—C成键, 生物催化, 酶, 催化剂, 精细化学品, 应用前景

Abstract:

The C—C bond formation reaction is the key reaction to construct the carbon skeleton of organic molecules in organic synthesis. This review presents the key enzymes that catalyze C—C bond formation reactions such as Aldol, Acyloin condensation, Stetter, Pictet-Spengler, etc., and the application progress of those enzymes in the synthesis fine chemicals such as β-hydroxy-α-amino, α-hydroxyketone, 1,4-diketone, β-carboline and tetrahydroisoquinoline in recent years. In addition, this manuscript also describes the application prospects of biocatalysis C—C bond formation reactions to expand the application scope of biocatalysis in chemical production.

Key words: C—C bond, biocatalysis, enzyme, catalyst, fine chemicals, application prospects

中图分类号:

Q 814.9

齐娜, 宋伟, 刘立明, 吴静. 生物催化C—C成键反应及其应用[J]. 化工学报, 2021, 72(1): 216-228.

QI Na, SONG Wei, LIU Liming, WU Jing. Biocatalysis C—C bonding reaction and its application[J]. CIESC Journal, 2021, 72(1): 216-228.

图/表 10

表1 生物催化C—C成键反应及其在合成精细化学品中的应用

Table 1 Biocatalytic C—C bond formation reaction and fine chemicals generated at the C—C bond site

Reaction	Enzyme	Product	Ref.
oxidative C—C coupling	^Mtlaccase	benzo furan	[3]
oxidative C—C coupling	^EnBBE	berbenrine	[4]
cyclization reaction	^BmSHC	hopene	[5-6]
Suzuki-Miyaura	Suzukiase	Atropisomerci biaryls	[7]
Aldol	^RmFruA/ ^EcFucA/^EcTagA/ ^EcRhaD	polyhydroxy compounds	[8]
Aldol	^AvDTA/^AvLTA/^StSHMT_Sth	β-hydroxy-α-amino	[8]
Acyloin condensation	^ACDH/^PfBAL	PAC/2-HPP	[9]
Acyloin condensation	^PpYerE/^BsAAS	tert-α-hydroxy ketone	[9]
Stetter	^SmPigD/^HcHapD	1,4-dicarbonyls	[10]
Pictet-Spengler	^Rs/OpSTR	β-carbolines	[11]
Pictet-Spengler	^Tf/CjNCS	Tetrahydroisoquinolines	[11]

表2 依赖DHAP醛缩酶绿色合成稀有糖及其衍生物

Table 2 Green synthesis of rare sugars and their derivatives by DHAP aldolase

Aldolase	Yield	Diastereo ratio
FruA	35.7%	92∶8
FruA	23.4%	92∶8
FruA	2.8%	92∶8
FruA	4.7%	87∶13
FucA	35.6%	92∶8
RhaD	10.4%	49∶51
RhaD	10.6%	49∶51
RhaD	22.4%	89∶11

图1 FSA催化C—C键形成多羟基化合物

Fig.1 FSA catalyzes C—C bonds to form polyhydroxy compounds

图2 苏氨酸醛缩酶催化形成的β-羟基-α-氨基化合物

Fig.2 Synthesis of β - hydroxy - α - amino compounds catalyzed by threonine aldolase

图3 ThDP依赖的酶催化酮醇缩合反应合成仲-α-羟基酮化合物

Fig.3 ThDP-dependent enzymes catalyze the ketol condensation reaction to form secondary-α-hydroxyketone

图4 YerE催化C—C键的形成用于制备叔-α-羟基酮

Fig.4 YerE catalyzes the formation of C—C bonds for the preparation of tertiary-α-hydroxy ketones

图5 AO:DCPIP使用2,3-丁二酮作为乙酰阴离子供体催化生成叔醇

Fig.5 AO: DCPIP uses 2,3-butanedione as an acetyl anion donor to catalyze the formation of tertiary alcohols

图6 ThDP依赖的酶催化α, β-不饱和酮生成1,4-二羰基化合物

Fig.6 ThDP-dependent enzymes catalyze α, β-unsaturated ketones to produce 1,4-dicarbonyl compounds

图7 异胡豆苷合酶催化的Pictet-Spengler反应

Fig.7 Pictet-Spengler reaction catalyzed by strictosidine synthase

图8 NCS-Tf突变体催化合成1,1'-双取代的THIQ

Fig.8 NCS-Tf mutant catalyzed synthesis of 1,1'-disubstituted THIQ

参考文献 83

2	Sherwood J, Clark J H, Fairlamb I J S, et al. Solvent effects in palladium catalysed cross-coupling reactions [J]. Green Chem., 2019, 21(9): 2164-2213.
3	Sousa A C, Piedade M F M M, Martins L O, et al. An enzymatic route to a benzocarbazole framework using bacterial cotA laccase [J]. Green Chem., 2015, 17(3): 1429-1433.
4	Engelmann C, Illner S, Kragl U. Laccase initiated C—C couplings: various techniques for reaction monitoring [J]. Pro. Biochem., 2015, 50(10): 1591-1599.
5	Hammer S C, Marjanovic A, Dominicus J M, et al. Squalene hopene cyclases are protonases for stereoselective Brønsted acid catalysis [J]. Nat. Chem. Biol., 2015, 11(2): 121-130.
6	Hammer S C, Syren P O, Seitz M, et al. Squalene hopene cyclases: highly promiscuous and evolvable catalysts for stereoselective C—C and C—X bond formation [J]. Curr. Opin. Chem. Biol., 2013, 17(2): 293-300.
7	Chatterjee A, Mallin H, Klehr J, et al. An enantioselective artificial Suzukiase based on the biotin-streptavidin technology [J]. Chem. Sci., 2016, 7(1): 673-677.
8	Clapes P, Garrabou X. Current trends in asymmetric synthesis with aldolases [J]. Adv. Synth. Catal., 2011, 353(13): 2263-2283.
9	Xuan K, Yang G, Wu Z, et al. Efficient synthesis of (3R,5S) -6-chloro -2,4,6 - trideoxyhexapyranose by using new 2-deoxy-D-ribose-5-phosphate aldolase from Streptococcus suis with moderate activity and aldehyde tolerance [J]. Pro. Biochem., 2020, 92: 113-119.
10	Sudar M, Vasic-Racki D, Mueller M, et al. Mathematical model of the MenD-catalyzed 1,4-addition (Stetter reaction) of alpha-ketoglutaric acid to acrylonitrile [J]. J. Biotechnol., 2018, 268: 71-80.
11	Eger E, Schrittwieser J, Wetzl D, et al. Asymmetric biocatalytic synthesis of 1-aryltetrahydro-beta-carbolines enabled by “substrate walking” [J]. Chem.-Eur. J., 2020, 26(69): 16281-16285.
12	Ligibel M, Moore C, Bruccoleri R, et al. Identification and application of threonine aldolase for synthesis of valuable alpha-amino, beta-hydroxy-building blocks [J]. BBA Proteom., 2020, 1868(2): 140323.
13	Mueller M, Sprenger G A, Pohl M. C—C bond formation using ThDP-dependent lyases [J].Curr. Opin. Chem. Biol., 2013, 17(2): 261-270.
1	Al-Smadi D, Enugala T R, Kessler V, et al. Chemical and biochemical approaches for the synthesis of substituted dihydroxybutanones and di- and tri-hydroxypentanones [J]. J. Org. Chem., 2019, 84(11): 6982-6991.
14	Fessner W D, Schneider A, Held H, et al. The mechanism of classⅡ, metal-dependent aldolases [J]. Angew. Chem. Int. Ed., 1996, 35(19): 2219-2221.
15	Dean S M, Greenberg W A, Wong C H. Recent advances in aldolase-catalyzed asymmetric synthesis [J]. Adv. Synth. Catal., 2007, 349(8/9): 1308-1320.
16	Breuer M, Hauer B. Carbon-carbon coupling in biotransformation [J]. Curr. Opin. Chem. Biol., 2003, 14(6): 570-576.
17	Roldan R, Sanchez-Moreno I, Scheidt T, et al. Breaking the dogma of aldolase specificity: simple aliphatic ketones and aldehydes are nucleophiles for fructose-6-phosphate aldolase [J]. Chem.-Eur. J., 2017, 23(21): 5005-5009.
18	Iturrate L, Sanchez-Moreno I, Oroz-Guinea I, et al. Preparation and characterization of a bifunctional aldolase/kinase enzyme: a more efficient biocatalyst for C—C bond formation [J]. Chem.-Eur. J., 2010, 16(13): 4018-4030.
19	Li A, Cai L, Chen, Z, et al. Recent advances in the synthesis of rare sugars using DHAP-dependent aldolases [J]. Carbohydrate Res., 2017, 452: 108-115.
20	Iqbal M W, Riaz T, Hassanin H A M, et al. Characterization of a novel D-arabinose isomerase from Thermanaeromonas toyohensis and its application for the production of D-ribulose and L-fuculose [J]. Enzyme. Micro. Tech., 2019, 131: 109427.
21	Sugiyama M, Hong Z, Greenberg W A, et al. In vivo selection for the directed evolution of L-rhamnulose aldolase from L-rhamnulose-1-phosphate aldolase (Rhad) [J]. Bioorg. Med. Chem., 2007, 15(17): 5905-5911.
22	Sanchez-Moreno I, Garcia-Garcia J F, Bastida A, et al. Multienzyme system for dihydroxyacetone phosphate-dependent aldolase catalyzed C—C bond formation from dihydroxyacetone [J]. Chem. Comm., 2004,(14): 1634-1635.
23	Sugiyama M, Hong Z, Liang P H, et al. D-Fructose-6-phosphate aldolase - catalyzed one-pot synthesis of iminocyclitols [J]. J. Am. Chem. Soc., 2007, 129(47): 14811-14817.
24	Schurmann M, Schurmann M, Sprenger G A. Fructose 6-phosphate aldolase and 1-deoxy-D-xylulose 5-phosphate synthase from Escherichia coli as tools in enzymatic synthesis of 1-deoxysugars [J]. J. Mol. Cata. B-Enzym., 2002, 19: 247-252.
25	Garrabou X, Castillo J A, Guerard-Helaine C, et al. Asymmetric self- and cross-aldol reactions of glycolaldehyde catalyzed by D-fructose-6-phosphate aldolase [J]. Angew. Chem. Int. Ed., 2009, 48(30): 5521-5525.
26	Gueclue D, Szekrenyi A, Garrabou X, et al. Minimalist protein engineering of an aldolase provokes unprecedented substrate promiscuity [J]. ACS Catal., 2016, 6(3): 1848-1852.
27	Junker S, Roldan R, Joosten H J, et al. Complete switch of reaction specificity of an aldolase by directed evolution in vitro: synthesis of generic aliphatic aldol products [J]. Angew. Chem. Int. Ed., 2018, 57(32): 10153-10157.
28	Cesnik M, Sudar M, Roldan R, et al. Model-based optimization of the enzymatic aldol addition of propanal to formaldehyde: a first step towards enzymatic synthesis of 3-hydroxybutyric acid [J]. Chem. Eng. Res. Des., 2019, 150: 140-152.
29	Yang X, Wu L, Li A, et al. The engineering of decamericd-fructose-6-phosphate aldolase A by combinatorial modulation of inter- and intra-subunit interactions [J]. Chem. Commun., 2020, 56(55): 7561-7564.
30	Schmidt N G, Eger E, Kroutil W. Building bridges: biocatalytic C—C bond formation toward multifunctional products [J]. ACS Catal., 2016, 6(7): 4286-4311.
31	Ma H, Engel S, Enugala T R, et al., New stereoselective biocatalysts for carboligation and retro-aldol cleavage reactions derived from D-fructose 6-phosphate aldolase [J]. Biochemistry, 2018, 57(40): 5877-5885.
32	Liu J Q, Odani M, Yasuoka T, et al. Gene cloning and overproduction of low-specificity D-threonine aldolase from Alcaligenes xylosoxidans and its application for production of a key intermediate for parkinsonism drug [J]. Appl. Microbiol. Bioteth., 2000, 54(1): 44-51.
33	Fesko K. Threonine aldolases: perspectives in engineering and screening the enzymes with enhanced substrate and stereo specificities [J]. Appl. Microbiol. Biotech., 2016, 100(6): 2579-2590.
34	Kataoka M, Ikemi M, Morikawa T, et al. Isolation and characterization of D-threonine aldolase, a pyridoxal-5'-phosphate-dependent enzyme from Arthrobacter sp. DK-38 [J]. Eur. J. Biochem., 1997, 248(2): 385-393.
35	Kataoka M, Wada M, Nishi K, et al. Purification and characterization of L-threonine aldolase from Aeromonas jandaei DK-39 [J]. FEMS Microbiol. Lett., 1997, 151(2): 245-248.
36	Fesko K, Strohmeier G A, Breinbauer R. Expanding the threonine aldolase toolbox for the asymmetric synthesis of tertiary alpha-amino acids [J]. Appl. Microbiol. Biotech., 2015, 99(22): 9651-9661.
37	Gong L, Xu G, Cao X, et al. High-throughput screening method for directed evolution and characterization of aldol activity of D-threonine aldolase [J]. Appl. Biochem. Biotech.,2020, doi:10.1007/s12010-020-03447-y. DOI
38	Vidal L, Calveras J, Clapes P, et al. Recombinant production of serine hydroxymethyl transferase from Streptococcus thermophilus and its preliminary evaluation as a biocatalyst [J]. Appl. Microbiol. Biotech., 2005, 68(4): 489-497.
39	Florio R, Di Salvo M L,Vivoli M, et al. Serine hydroxymethyltransferase: a model enzyme for mechanistic, structural, and evolutionary studies [J]. BBA Proteom., 2011, 1814(11): 1489-1496.
40	Hernandez K, Zelen I, Petrillo G, et al. Engineered L-serine hydroxymethyl transferase from streptococcus thermophilus for the synthesis of alpha, alpha - dialkyl-alpha-amino acids [J]. Angew. Chem. Int. Ed., 2015, 54(10): 3013-3017.
41	Hoyos P,Sinisterra J V,Molinari F, et al. Biocatalytic strategies for the asymmetric synthesis of alpha-hydroxy ketones [J]. Accounts Chem. Res., 2010, 43(2): 288-299.
42	Fraas S, Steinbach A K, Tabbert A, et al. Cyclohexane-1,2-dione hydrolase: a new tool to degrade alicyclic compounds [J]. J. Mol. B-Enzym., 2009, 61(1/2): 47-49.
43	Steinbach A K, Fraas S, Harder J, et al. Cyclohexane-1,2-dione hydrolase from Denitrifying azoarcus sp strain 22lin, a novel member of the thiamine diphosphate enzyme family [J]. J. Bacteriol., 2011, 193(23): 6760-6769.
44	Loschonsky S, Waltzer S, Fraas S, et al. Catalytic scope of the thiamine-dependent multifunctional enzyme cyclohexane-1,2-dione hydrolase [J]. ChemBioChem, 2014, 15(3): 389-392.
45	Loschonsky S, Wacker T, Waltzer S, et al. Extended reaction scope of thiamine diphosphate dependent cyclohexane-1,2-dione hydrolase: from C—C bond cleavage to C—C bond ligation [J]. Angew. Chem. Int. Ed., 2014, 53(52): 14402-14406.
46	Loschonsky S, Waltzer S, Brecht V, et al. Elucidation of the enantioselective cyclohexane-1,2-dione hydrolase catalyzed formation of (S)- acetoin [J]. ChemCatChem, 2014, 6(4): 969-972.
47	Gonzalez B, Vicuna R. Benzaldehyde lyase, a novel thiamine PPi-requiring enzyme, from Pseudomonas fluorescens biovar I [J]. J. Bacteriol., 1989, 171(5): 2401-2405.
48	Mosbacher T G, Mueller M, Schulz G E. Structure and mechanism of the ThDP-dependent benzaldehyde lyase from Pseudomonas fluorescens [J]. FEBS J., 2005, 272(23): 6067-6076.
49	Mueller C R, Perez-Sanchez M, Maria P D. Benzaldehyde lyase-catalyzed diastereoselective C—C bond formation by simultaneous carboligation and kinetic resolution [J]. Org.Biomol.Chem., 2013, 11(12): 2000-2004.
50	Liang Y F, Jiao N. Highly efficient C—H hydroxylation of carbonyl compounds with oxygen under mild conditions [J]. Angew. Chem. Int. Ed., 2014, 53(2): 548-552.
51	Lehwald P, Richter M, Roehr C, et al. Enantioselective intermolecular aldehyde-ketone cross-coupling through an enzymatic carboligation reaction [J]. Angew. Chem. Int. Ed., 2010, 49(13): 2389-2392.
52	Bortolini O, Giovannini P P, Maietti S, et al. An enzymatic approach to the synthesis of optically pure (3R)- and (3S)-enantiomers of green tea flavor compound 3-hydroxy-3-methylnonane-2,4-dione [J]. J. Mol. B-Enzym., 2013, 85/86: 93-98.
53	Hampel S, Steitz J P, Baierl A, et al. Structural and mutagenesis studies of the thiamine-dependent, ketone-accepting yere from pseudomonas protegens [J]. ChemBioChem, 2018, 19(21): 2283-2292.
54	Giovannini P P, Pedrini P, Venturi V, et al. Bacillus stearothermophilus acetylacetoin synthase: a new catalyst for C—C bond formation [J]. J. Mol. B-Enzym., 2010, 64(1/2): 113-117.
55	Giovannini P P, Mantovani M, Grandini A, et al. New acetoin reductases from Bacillus stearothermophilus: meso- and 2R,3R-butanediol as fermentation products [J]. J. Mol. Catal. B-Enzym., 2011, 69(1/2): 15-20.
56	Giovannini P P, Fantin G, Massi A, et al. Enzymatic diastereo- and enantioselective synthesis of alpha-alkyl-alpha,beta-dihydroxyketones [J]. Org. Biomol. Chem., 2011, 9(23): 8038-8045.
57	Bernacchia G, Bortolini O, De Bastiani M, et al. Enzymatic chemoselective aldehyde-ketone cross-couplings through the polarity reversal of methylacetoin [J]. Angew. Chem. Int. Ed., 2015, 54(24): 7171-7175.
58	Di Carmine G, Bortolini O, Massi A, et al. Enzymatic cross-benzoin-type condensation of aliphatic aldehydes: enantioselective synthesis of 1-alkyl-1-hydroxypropan-2-ones and 1-alkyl-1-hydroxybutan-2-ones [J]. Adv. Synth. Catal., 2018, 360(21): 4132-4141.
59	Giovannini P P, Lerin L A, Mueller M, et al. (S)-Selectivity in phenylacetyl carbinol synthesis using the wild-type enzyme acetoin: dichlorophenolindophenol oxidoreductase from Bacillus licheniformis [J]. Adv. Synth. Catal.,2016, 358(17): 2767-2776.
60	Christmann M. New developments in the asymmetric Stetter reaction [J]. Angew. Chem. Int. Ed., 2005, 44(18): 2632-2634.
61	Williamson N R, Simonsen H T, Ahmed R A A, et al. Biosynthesis of the red antibiotic, prodigiosin, in serratia: identification of a novel 2-methyl -3-N-amyl-pyrrole (map) assembly pathway, definition of the terminal condensing enzyme, and implications for undecylprodigiosin biosynthesis in streptomyces [J]. Mol. Microbiol., 2005, 56(4): 971-989.
62	Dresen C, Richter M, Pohl M, et al. The enzymatic asymmetric conjugate umpolung reaction [J]. Angew. Chem. Int. Ed., 2010, 49(37): 6600-6603.
63	Beigi M, Waltzer S, Zarei M, et al. New Stetter reactions catalyzed by thiamine diphosphate dependent mend from E. coli [J]. J.Biotechnol., 2014, 191: 64-68.
64	Kasparyan E, Richter M, Dresen C, et al. Asymmetric Stetter reactions catalyzed by thiamine diphosphate-dependent enzymes[J]. Appl. Microbiol. Bioteth., 2014, 98(23): 9681-9690.
65	Kurutsch A, Richter M, Brecht V, et al. Mend as a versatile catalyst for asymmetric synthesis[J]. J. Mol. B-Enzym., 2009, 61(1/2): 56-66.
66	Westphal R, Waltzer S, Mackfeld U, et al. (S)-Selective menD variants from Escherichia coli provide access to new functionalized chiral alpha-hydroxy ketones [J]. Chem. Commun., 2013, 49(20): 2061-2063.
67	Chrzanowska M, Grajewska A, Rozwadowska M D. Asymmetric synthesis of isoquinoline alkaloids: 2004—2015[J]. Chem. Rev., 2016, 116(19): 12369-12465.
68	Schapfl M, Baier S, Fries A, et al. Extended substrate range of thiamine diphosphate-dependent mend enzyme by coupling of two C—C bonding reactions [J]. Appl. Microbio. Biot., 2018, 102(19): 8359-8372.
69	Patil M D, Grogan G, Yun H. Biocatalyzed C—C bond formation for the production of alkaloids[J]. ChemCatChem, 2018, 10(21): 4797-4818.
70	Cao R, Peng W, Wang Z, et al. Beta-carboline alkaloids: biochemical and pharmacological functions[J]. Curr. Med. Chem., 2007, 14(4): 479-500.
71	Brown R T, Leonard J, Sleigh S K. The role of strictosidine in monoterpenoid indole alkaloid biosynthesis[J]. Phytochem., 1978,17: 899-900
72	Pressnitz D, Fischereder E M, Pletz J, et al. Asymmetric synthesis of (R)-1-alkyl-substituted tetrahydro-beta-carbolines catalyzed by strictosidine synthases[J]. Angew. Chem. Int. Ed., 2018, 57(33): 10683-10687.
73	Eger E, Simon A, Sharma M, et al. Inverted binding of non-natural substrates in strictosidine synthase leads to a switch of stereochemical outcome in enzyme-catalyzed Pictet-Spengler reactions [J]. J. Am. Chem.Soc., 2020, 142(9): 4525-4526.
74	Fischereder E M, Pressnitz D, Kroutil W, et al. Stereoselective cascade to C3-methylated strictosidine derivatives employing transaminases and strictosidine synthases [J]. ACS Catal., 2016, 6(1): 23-30.
75	Fischereder E, Pressnitz D, Kroutil W, et al. Engineering strictosidine synthase: rational design of a small, focused circular permutation library of the beta-propeller fold enzyme [J]. Bioorg. Med. Chem., 2014, 22(20): 5633-5637.
76	Mori T, Hoshino S, Sahashi S, et al. Structural basis for beta-carboline alkaloid production by the microbial homodimeric enzyme McbB [J]. Chem. Biol., 2015, 22(7): 898-906.
77	Khan A Y, Suresh Kumar G. Natural isoquinoline alkaloids: binding aspects to functional proteins, serum albumins, hemoglobin, and lysozyme [J]. Biophy. Rev., 2015, 7(4): 407-420.
78	Samanani N, Facchini P J. Purification and characterization of norcoclaurine synthase - the first committed enzyme in benzylisoquinoline alkaloid biosynthesis in plants [J]. J. Biolog. Chem., 2002, 277(37): 33878-33883.
79	Bonamore A, Rovardi I, Gasparrini F, et al. An enzymatic, stereoselective synthesis of (S)-norcoclaurine [J]. Green Chem., 2010, 12(9): 1623-1627.
80	Lichman B R, Gershater M C, Lamming E D, et al. “Dopamine-first” mechanism enables the rational engineering of the norcoclaurine synthase aldehyde activity profile [J]. FEBS J., 2015, 282(6): 1137-1151.
81	Pesnot T, Gershater M C, Ward J M, et al. The catalytic potential of Coptis japonica NCS2 revealed — development and utilisation of a fluorescamine-based assay [J]. Adv. Synth. Catal., 2012, 354(16): 2997-3008.
82	Lichman B R, Zhao J, Hailes H C, et al. Enzyme catalysed pictet-spengler formation of chiral 1,1'-disubstituted- and spiro-tetrahydroisoquinolines [J]. Nat. Commun., 2017, 8: 1-9.
83	Fu B, Balskus E P. Discovery of C—C bond-forming and bond-breaking radical enzymes: enabling transformations for metabolic engineering [J]. Curr. Opin. Biotech., 2020, 65: 94-101.

[1]	李艺彤, 郭航, 陈浩, 叶芳. 催化剂非均匀分布的质子交换膜燃料电池操作条件研究[J]. 化工学报, 2023, 74(9): 3831-3840.
[2]	程业品, 胡达清, 徐奕莎, 刘华彦, 卢晗锋, 崔国凯. 离子液体基低共熔溶剂在转化CO₂中的应用[J]. 化工学报, 2023, 74(9): 3640-3653.
[3]	陈杰, 林永胜, 肖恺, 杨臣, 邱挺. 胆碱基碱性离子液体催化合成仲丁醇性能研究[J]. 化工学报, 2023, 74(9): 3716-3730.
[4]	杨学金, 杨金涛, 宁平, 王访, 宋晓双, 贾丽娟, 冯嘉予. 剧毒气体PH₃的干法净化技术研究进展[J]. 化工学报, 2023, 74(9): 3742-3755.
[5]	孟令玎, 崇汝青, 孙菲雪, 孟子晖, 刘文芳. 改性聚乙烯膜和氧化硅固定化碳酸酐酶[J]. 化工学报, 2023, 74(8): 3472-3484.
[6]	杨欣, 彭啸, 薛凯茹, 苏梦威, 吴燕. 分子印迹-TiO₂光电催化降解增溶PHE废水性能研究[J]. 化工学报, 2023, 74(8): 3564-3571.
[7]	杨菲菲, 赵世熙, 周维, 倪中海. Sn掺杂的In₂O₃催化CO₂选择性加氢制甲醇[J]. 化工学报, 2023, 74(8): 3366-3374.
[8]	李凯旋, 谭伟, 张曼玉, 徐志豪, 王旭裕, 纪红兵. 富含零价钴活性位点的钴氮碳/活性炭设计及甲醛催化氧化应用研究[J]. 化工学报, 2023, 74(8): 3342-3352.
[9]	陈雅鑫, 袁航, 刘冠章, 毛磊, 杨纯, 张瑞芳, 张光亚. 蛋白质纳米笼介导的酶自固定化研究进展[J]. 化工学报, 2023, 74(7): 2773-2782.
[10]	汤晓玲, 王嘉瑞, 朱玄烨, 郑仁朝. 基于Pickering乳液的卤醇脱卤酶催化合成手性环氧氯丙烷[J]. 化工学报, 2023, 74(7): 2926-2934.
[11]	余娅洁, 李静茹, 周树锋, 李清彪, 詹国武. 基于天然生物模板构建纳米材料及集成催化剂研究进展[J]. 化工学报, 2023, 74(7): 2735-2752.
[12]	涂玉明, 邵高燕, 陈健杰, 刘凤, 田世超, 周智勇, 任钟旗. 钙基催化剂的设计合成及应用研究进展[J]. 化工学报, 2023, 74(7): 2717-2734.
[13]	张琦钰, 高利军, 苏宇航, 马晓博, 王翊丞, 张亚婷, 胡超. 碳基催化材料在电化学还原二氧化碳中的研究进展[J]. 化工学报, 2023, 74(7): 2753-2772.
[14]	李盼, 马俊洋, 陈志豪, 王丽, 郭耘. Ru/α-MnO₂催化剂形貌对NH₃-SCO反应性能的影响[J]. 化工学报, 2023, 74(7): 2908-2918.
[15]	张谭, 刘光, 李晋平, 孙予罕. Ru基氮还原电催化剂性能调控策略[J]. 化工学报, 2023, 74(6): 2264-2280.