Advancements and challenges in protein purification techniques for denitrifying enzymes: A path to effective nitrogen removal and reduced N₂O emissions

References

• Al-Attar, S., & de Vries, S. (2015). An electrogenic nitric oxide reductase. FEBS Letters, 589(16), 2050–2057. https://doi.org/10.1016/j.febslet.2015.06.033
   PubMed Web of Science ®Google Scholar
• Albertsson, I., Sjöholm, J., Beek, J., Watmough, N. J., Widengren, J., & Ädelroth, P. (2019). Functional interactions between nitrite reductase and nitric oxide reductase from Paracoccus denitrificans. Scientific Reports, 9(1), 17234. https://doi.org/10.1038/s41598-019-53553-z
   Google Scholar
• Almeida, S., Sousa, C., Abreu, V., Diniz, C., Dorneles, E. M. S., Lage, A. P., Barh, D., & Azevedo, V. (2017). Exploration of nitrate reductase metabolic pathway in Corynebacterium pseudotuberculosis. International Journal of Genomics, 2017, 9481756–9481712. https://doi.org/10.1155/2017/9481756
   PubMed Web of Science ®Google Scholar
• Arciszewska, K., Kowalska, E., Bartnicki, F., Bonarek, P., Banaś, A. K., & Strzałka, W. (2023). DNA aptamer-based affinity chromatography system for purification of recombinant proteins tagged with lysine tag. Journal of Chromatography. A, 1692, 463846. https://doi.org/10.1016/j.chroma.2023.463846
   PubMed Web of Science ®Google Scholar
• Argandoña, M., Martínez-Checa, F., Llamas, I., Arco, Y., Quesada, E., & del Moral, A. (2006). A membrane-bound nitrate reductase encoded by the narGHJI operon is responsible for anaerobic respiration in Halomonas maura. Extremophiles: Life under Extreme Conditions, 10(5), 411–419. https://doi.org/10.1007/s00792-006-0515-2
   PubMed Web of Science ®Google Scholar
• Arias-Cartin, R., Grimaldi, S., Pommier, J., Lanciano, P., Schaefer, C., Arnoux, P., Giordano, G., Guigliarelli, B., & Magalon, A. (2011). Cardiolipin-based respiratory complex activation in bacteria. Proceedings of the National Academy of Sciences of the United States of America, 108(19), 7781–7786. https://doi.org/10.1073/pnas.1010427108
   PubMed Web of Science ®Google Scholar
• Arnoux, P., Sabaty, M., Alric, J., Frangioni, B., Guigliarelli, B., Adriano, J.-M., & Pignol, D. (2003). Structural and redox plasticity in the heterodimeric periplasmic nitrate reductase. Nature Structural Biology, 10(11), 928–934. https://doi.org/10.1038/nsb994
   PubMedGoogle Scholar
• Bakken, L. R., Bergaust, L., Liu, B., & Frostegård, Å. (2012). Regulation of denitrification at the cellular level: A clue to the understanding of N2O emissions from soils. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences, 367(1593), 1226–1234. https://doi.org/10.1098/rstb.2011.0321
   PubMed Web of Science ®Google Scholar
• Benedini, L. J., Figueiredo, D., Cabrera-Crespo, J., Gonçalves, V. M., Silva, G. G., Campani, G., Zangirolami, T. C., & Furlan, F. F. (2020). Modeling and simulation of anion exchange chromatography for purification of proteins in complex mixtures. Journal of Chromatography. A, 1613, 460685. https://doi.org/10.1016/j.chroma.2019.460685
   PubMed Web of Science ®Google Scholar
• Bennett, S. P., Soriano-Laguna, M. J., Bradley, J. M., Svistunenko, D. A., Richardson, D. J., Gates, A. J., & Le Brun, N. E. (2019). NosL is a dedicated copper chaperone for assembly of the CuZ center of nitrous oxide reductase. Chemical Science, 10(19), 4985–4993. https://doi.org/10.1039/c9sc01053j
   PubMed Web of Science ®Google Scholar
• Bergaust, L., Shapleigh, J., Frostegård, Å., & Bakken, L. (2008). Transcription and activities of NOx reductases in Agrobacterium tumefaciens: The influence of nitrate, nitrite and oxygen availability. Environmental Microbiology, 10(11), 3070–3081. https://doi.org/10.1111/j.1462-2920.2007.01557.x
   PubMed Web of Science ®Google Scholar
• Berks, B. C., Richardson, D. J., Robinson, C., Reilly, A., Aplin, R. T., & Ferguson, S. J. (1994). Purification and characterization of the periplasmic nitrate reductase from Thiosphaera pantotropha. European Journal of Biochemistry, 220(1), 117–124. https://doi.org/10.1111/j.1432-1033.1994.tb18605.x
   PubMedGoogle Scholar
• Bertero, M. G., Rothery, R. A., Palak, M., Hou, C., Lim, D., Blasco, F., Weiner, J. H., & Strynadka, N. C. J. (2003). Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A. Nature Structural Biology, 10(9), 681–687. https://doi.org/10.1038/nsb969
   PubMedGoogle Scholar
• Bird, L. E. (2011). High throughput construction and small scale expression screening of multi-tag vectors in Escherichia coli. Methods (San Diego, Calif.), 55(1), 29–37. https://doi.org/10.1016/j.ymeth.2011.08.002
   PubMed Web of Science ®Google Scholar
• Blomberg, M. R. A., & Siegbahn, P. E. M. (2016). Improved free energy profile for reduction of NO in cytochrome c dependent nitric oxide reductase (cNOR). Journal of Computational Chemistry, 37(19), 1810–1818. https://doi.org/10.1002/jcc.24396
   PubMed Web of Science ®Google Scholar
• Campbell, W. H., & Kinghorn, K. R. (1990). Functional domains of assimilatory nitrate reductases and nitrite reductases. Trends in Biochemical Sciences, 15(8), 315–319. https://doi.org/10.1016/0968-0004(90)90021-3
   PubMed Web of Science ®Google Scholar
• Cerqueira, N. M. F. S. A., Gonzalez, P. J., Fernandes, P. A., Moura, J. J. G., & Ramos, M. J. (2015). Periplasmic nitrate reductase and formate dehydrogenase: Similar molecular architectures with very different enzymatic activities. Accounts of Chemical Research, 48(11), 2875–2884. https://doi.org/10.1021/acs.accounts.5b00333
   PubMed Web of Science ®Google Scholar
• Cheng, J., Liu, T., You, X., Zhang, F., Sui, S.-F., Wan, X., & Zhang, X. (2023). Determining protein structures in cellular lamella at pseudo-atomic resolution by GisSPA. Nature Communications, 14(1), 1282. https://doi.org/10.1038/s41467-023-36175-y
   Web of Science ®Google Scholar
• Chu, S., Zhang, D., Wang, D., Zhi, Y., & Zhou, P. (2017). Heterologous expression and biochemical characterization of assimilatory nitrate and nitrite reductase reveals adaption and potential of Bacillus megaterium NCT-2 in secondary salinization soil. International Journal of Biological Macromolecules, 101, 1019–1028. https://doi.org/10.1016/j.ijbiomac.2017.04.009
   PubMed Web of Science ®Google Scholar
• Coelho, C., & Romão, M. J. (2015). Structural and mechanistic insights on nitrate reductases. Protein Science: A Publication of the Protein Society, 24(12), 1901–1911. https://doi.org/10.1002/pro.2801
   PubMedGoogle Scholar
• Coskun, O. (2016). Separation techniques: Chromatography. Northern Clinics of Istanbul, 3(2), 156–160. https://doi.org/10.14744/nci.2016.32757
   PubMed Web of Science ®Google Scholar
• Crowe, J., Döbeli, H., Gentz, R., Hochuli, E., Stüber, D., & Henco, K. (1994). 6xHis-Ni-NTA chromatography as a superior technique in recombinant protein expression/purification. Methods in Molecular Biology (Clifton, N.J.), 31, 371–387. https://doi.org/10.1385/0-89603-258-2:371
   PubMedGoogle Scholar
• Cummins, P. M., Rochfort, K. D., & O’Connor, B. F. (2017). Ion-exchange chromatography: Basic principles and application. Protein chromatography: methods and protocols, 209–223.
   Google Scholar
• Denisov, I. G., & Sligar, S. G. (2016). Nanodiscs for structural and functional studies of membrane proteins. Nature Structural & Molecular Biology, 23(6), 481–486. https://doi.org/10.1038/nsmb.3195
   PubMed Web of Science ®Google Scholar
• Dias, J. M., Than, M. E., Humm, A., Huber, R., Bourenkov, G. P., Bartunik, H. D., Bursakov, S., Calvete, J., Caldeira, J., Carneiro, C., Moura, J. J., Moura, I., & Romão, M. J. (1999). Crystal structure of the first dissimilatory nitrate reductase at 1.9 A solved by MAD methods. Structure (London, England: 1993), 7(1), 65–79. https://doi.org/10.1016/s0969-2126(99)80010-0
   PubMed Web of Science ®Google Scholar
• Dong, X., Liu, H., Long, S., Xu, S., & Lichtfouse, E. (2022). Weak electrical stimulation on biological denitrification: Insights from the denitrifying enzymes. The Science of the Total Environment, 806(Pt 4), 150926. https://doi.org/10.1016/j.scitotenv.2021.150926
   PubMedGoogle Scholar
• Dow, J. M., Grahl, S., Ward, R., Evans, R., Byron, O., Norman, D. G., Palmer, T., & Sargent, F. (2014). Characterization of a periplasmic nitrate reductase in complex with its biosynthetic chaperone. The FEBS Journal, 281(1), 246–260. https://doi.org/10.1111/febs.12592
   PubMed Web of Science ®Google Scholar
• Du, F., Liu, Y. Q., Xu, Y.-S., Li, Z. J., Wang, Y. Z., Zhang, Z. X., & Sun, X. M. (2021). Regulating the T7 RNA polymerase expression in E. coli BL21 (DE3) to provide more host options for recombinant protein production. Microbial Cell Factories, 20(1), 189. https://doi.org/10.1186/s12934-021-01680-6
   PubMed Web of Science ®Google Scholar
• Duré, A. B., Cristaldi, J. C., Guevara Cuasapud, L. A., Dalosto, S. D., Rivas, M. G., Ferroni, F. M., González, P. J., Montich, G. G., & Brondino, C. D. (2023). Molecular and kinetic properties of copper nitrite reductase from Sinorhizobium meliloti 2011 upon substituting the interfacial histidine ligand coordinated to the type 2 copper active site for glycine. Journal of Inorganic Biochemistry, 241, 112155. https://doi.org/10.1016/j.jinorgbio.2023.112155
   PubMed Web of Science ®Google Scholar
• Einsle, O., Messerschmidt, A., Stach, P., Bourenkov, G. P., Bartunik, H. D., Huber, R., & Kroneck, P. M. H. (1999). Structure of cytochrome c nitrite reductase. Nature, 400(6743), 476–480. https://doi.org/10.1038/22802
   PubMed Web of Science ®Google Scholar
• Farrar, J. A., Zumft, W. G., & Thomson, A. J. (1998). CuA and CuZ are variants of the electron transfer center in nitrous oxide reductase. Proceedings of the National Academy of Sciences of the United States of America, 95(17), 9891–9896. https://doi.org/10.1073/pnas.95.17.9891
   PubMed Web of Science ®Google Scholar
• Francis, D. M., & Page, R. (2010). Strategies to optimize protein expression in E. coli. Current Protocols in Protein Science, Chapter 5(1), 5.24.1–5.24.29. https://doi.org/10.1002/0471140864.ps0524s61
   PubMedGoogle Scholar
• Fukuda, M., Takeda, H., Kato, H. E., Doki, S., Ito, K., Maturana, A. D., Ishitani, R., & Nureki, O. (2015). Structural basis for dynamic mechanism of nitrate/nitrite antiport by NarK. Nature Communications, 6(1), 7097. https://doi.org/10.1038/ncomms8097
   PubMedGoogle Scholar
• Fukuda, Y., Tse, K. M., Nakane, T., Nakatsu, T., Suzuki, M., Sugahara, M., Inoue, S., Masuda, T., Yumoto, F., Matsugaki, N., Nango, E., Tono, K., Joti, Y., Kameshima, T., Song, C., Hatsui, T., Yabashi, M., Nureki, O., Murphy, M. E. P., … Mizohata, E. (2016). Redox-coupled proton transfer mechanism in nitrite reductase revealed by femtosecond crystallography. Proceedings of the National Academy of Sciences of the United States of America, 113(11), 2928–2933. https://doi.org/10.1073/pnas.1517770113
   PubMed Web of Science ®Google Scholar
• Fülöp, V., Moir, J. W. B., Ferguson, S. J., & Hajdu, J. (1995). The anatomy of a bifunctional enzyme: Structural basis for reduction of oxygen to water and synthesis of nitric oxide by cytochrome cd1. Cell, 81(3), 369–377. https://doi.org/10.1016/0092-8674(95)90390-9
   PubMed Web of Science ®Google Scholar
• Gao, H., Li, C., Ramesh, B., & Hu, N. (2018). Cloning, purification and characterization of novel Cu-containing nitrite reductase from the Bacillus firmus GY-49. World Journal of Microbiology and Biotechnology, 34(1), 10. https://doi.org/10.1007/s11274-017-2383-6
   Web of Science ®Google Scholar
• García-Fruitós, E. (2010). Inclusion bodies: A new concept. Microbial Cell Factories, 9(1), 80. https://doi.org/10.1186/1475-2859-9-80
   PubMedGoogle Scholar
• Godden, J. W., Turley, S., Teller, D. C., Adman, E. T., Liu, M. Y., Payne, W. J., & LeGall, J. (1991). The 2.3 Angstrom X-ray structure of nitrite reductase from Achromobacter cycloclastes. Science (New York, N.Y.), 253(5018), 438–442. https://doi.org/10.1126/science.1862344
   PubMed Web of Science ®Google Scholar
• Gonska, N., Young, D., Yuki, R., Okamoto, T., Hisano, T., Antonyuk, S., Hasnain, S. S., Muramoto, K., Shiro, Y., Tosha, T., & Ädelroth, P. (2018). Characterization of the quinol-dependent nitric oxide reductase from the pathogen Neisseria meningitidis, an electrogenic enzyme. Scientific Reports, 8(1), 3637. https://doi.org/10.1038/s41598-018-21804-0
   Google Scholar
• Gopalasingam, C. C., Johnson, R. M., Chiduza, G. N., Tosha, T., Yamamoto, M., Shiro, Y., Antonyuk, S. V., Muench, S. P., & Hasnain, S. S. (2019). Dimeric structures of quinol-dependent nitric oxide reductases (qNORs) revealed by cryo–electron microscopy. Science Advances, 5(8), eaax1803. https://doi.org/10.1126/sciadv.aax1803
   PubMed Web of Science ®Google Scholar
• Graf, D. R. H., Jones, C. M., & Hallin, S. (2014). Intergenomic comparisons highlight modularity of the denitrification pathway and underpin the importance of community structure for N2O emissions. PloS One, 9(12), e114118. https://doi.org/10.1371/journal.pone.0114118
   PubMed Web of Science ®Google Scholar
• Guo, K., Feng, X., Sun, W., Han, S., Wu, S., & Gao, H. (2022). NapB restores cytochrome c biosynthesis in bacterial dsbD-deficient mutants. Communications Biology, 5(1), 87. https://doi.org/10.1038/s42003-022-03034-3
   Web of Science ®Google Scholar
• Hallin, S., Philippot, L., Löffler, F. E., Sanford, R. A., & Jones, C. M. (2018). Genomics and ecology of novel N2O-reducing microorganisms. Trends in Microbiology, 26(1), 43–55. https://doi.org/10.1016/j.tim.2017.07.003
   PubMed Web of Science ®Google Scholar
• Han, C., Wright, G. S. A., Fisher, K., Rigby, S. E. J., Eady, R. R., & Hasnain, S. S. (2012). Characterization of a novel copper-HAEM c dissimilatory nitrite reductase from Ralstonia pickettii. The Biochemical Journal, 444(2), 219–226. https://doi.org/10.1042/BJ20111623
   PubMedGoogle Scholar
• Hino, T., Matsumoto, Y., Nagano, S., Sugimoto, H., Fukumori, Y., Murata, T., Iwata, S., & Shiro, Y. (2010). Structural basis of biological N2O generation by bacterial nitric oxide reductase. Science (New York, N.Y.), 330(6011), 1666–1670. https://doi.org/10.1126/science.1195591
   PubMed Web of Science ®Google Scholar
• Hino, T., Nagano, S., Sugimoto, H., Tosha, T., & Shiro, Y. (2012). Molecular structure and function of bacterial nitric oxide reductase. Biochimica et Biophysica Acta, 1817(4), 680–687. https://doi.org/10.1016/j.bbabio.2011.09.021
   PubMed Web of Science ®Google Scholar
• Jamali, M. A. M., Gopalasingam, C. C., Johnson, R. M., Tosha, T., Muramoto, K., Muench, S. P., Antonyuk, S. V., Shiro, Y., & Hasnain, S. S. (2020). The active form of quinol-dependent nitric oxide reductase from Neisseria meningitidis is a dimer. IUCrJ, 7(Pt 3), 404–415. https://doi.org/10.1107/S2052252520003656
   PubMedGoogle Scholar
• Jepson, B. J. N., Mohan, S., Clarke, T. A., Gates, A. J., Cole, J. A., Butler, C. S., Butt, J. N., Hemmings, A. M., & Richardson, D. J. (2007). Spectropotentiometric and structural analysis of the periplasmic nitrate reductase from Escherichia coli. The Journal of Biological Chemistry, 282(9), 6425–6437. https://doi.org/10.1074/jbc.M607353200
   PubMed Web of Science ®Google Scholar
• Jormakka, M., Richardson, D., Byrne, B., & Iwata, S. (2004). Architecture of NarGH reveals a structural classification of Mo-bisMGD enzymes. Structure (London, England: 1993), 12(1), 95–104. https://doi.org/10.1016/j.str.2003.11.020
   PubMed Web of Science ®Google Scholar
• Jormakka, M., Törnroth, S., Abramson, J., Byrne, B., & Iwata, S. (2002). Purification and crystallization of the respiratory complex formate dehydrogenase-N from Escherichia coli. Acta Crystallographica. Section D, Biological Crystallography, 58(Pt 1), 160–162. https://doi.org/10.1107/s0907444901017723
   PubMedGoogle Scholar
• Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., Bridgland, A., Meyer, C., Kohl, S. A. A., Ballard, A. J., Cowie, A., Romera-Paredes, B., Nikolov, S., Jain, R., Adler, J., … Hassabis, D. (2021). Highly accurate protein structure prediction with AlphaFold. Nature, 596(7873), 583–589. https://doi.org/10.1038/s41586-021-03819-2
   PubMed Web of Science ®Google Scholar
• Jungbauer, A., Kaar, W., & Schlegl, R. (2004). Folding and refolding of proteins in chromatographic beds. Current Opinion in Biotechnology, 15(5), 487–494. https://doi.org/10.1016/j.copbio.2004.08.009
   PubMed Web of Science ®Google Scholar
• Kahle, M., Blomberg, M. R. A., Jareck, S., & Ädelroth, P. (2019). Insights into the mechanism of nitric oxide reductase from a FeB-depleted variant. FEBS Letters, 593(12), 1351–1359. https://doi.org/10.1002/1873-3468.13436
   PubMed Web of Science ®Google Scholar
• Kahle, M., Ter Beek, J., Hosler, J. P., & Ädelroth, P. (2018). The insertion of the non-heme FeB cofactor into nitric oxide reductase from P. denitrificans depends on NorQ and NorD accessory proteins. Biochimica et Biophysica Acta Bioenergetics, 1859(10), 1051–1058. https://doi.org/10.1016/j.bbabio.2018.05.020
   PubMed Web of Science ®Google Scholar
• Kameya, M., Kanbe, H., Igarashi, Y., Arai, H., & Ishii, M. (2017). Nitrate reductases in Hydrogenobacter thermophilus with evolutionarily ancient features: Distinctive localization and electron transfer. Molecular Microbiology, 106(1), 129–141. https://doi.org/10.1111/mmi.13756
   PubMed Web of Science ®Google Scholar
• Kilic, V., Kilic, G. A., Kutlu, H. M., & Martínez-Espinosa, R. M. (2017). Nitrate reduction in Haloferax alexandrinus: The case of assimilatory nitrate reductase. Extremophiles: Life under Extreme Conditions, 21(3), 551–561. https://doi.org/10.1007/s00792-017-0924-4
   PubMed Web of Science ®Google Scholar
• Koppenhöfer, A., Little, R. H., Lowe, D. J., Ferguson, S. J., & Watmough, N. J. (2000). Oxidase reaction of Cytochrome cd1 from Paracoccus pantotrophus. Biochemistry, 39(14), 4028–4036. https://doi.org/10.1021/bi991912k
   PubMed Web of Science ®Google Scholar
• Krishnarjuna, B., Marte, J., Ravula, T., & Ramamoorthy, A. (2023). Enhancing the stability and homogeneity of non-ionic polymer nanodiscs by tuning electrostatic interactions. Journal of Colloid and Interface Science, 634, 887–896. https://doi.org/10.1016/j.jcis.2022.12.112
   PubMed Web of Science ®Google Scholar
• Krishnarjuna, B., & Ramamoorthy, A. (2022). Detergent-free isolation of membrane proteins and strategies to study them in a near-native membrane environment. Biomolecules, 12(8), 1076. https://doi.org/10.3390/biom12081076
   PubMed Web of Science ®Google Scholar
• Kumita, H., Matsuura, K., Hino, T., Takahashi, S., Hori, H., Fukumori, Y., Morishima, I., & Shiro, Y. (2004). NO reduction by nitric-oxide reductase from denitrifying bacterium Pseudomonas aeruginosa. The Journal of Biological Chemistry, 279(53), 55247–55254. https://doi.org/10.1074/jbc.M409996200
   PubMed Web of Science ®Google Scholar
• Kuypers, M. M. M., Marchant, H. K., & Kartal, B. (2018). The microbial nitrogen-cycling network. Nature Reviews. Microbiology, 16(5), 263–276. https://doi.org/10.1038/nrmicro.2018.9
   PubMed Web of Science ®Google Scholar
• Lee, H. J., Lee, H. S., Youn, T., Byrne, B., & Chae, P. S. (2022). Impact of novel detergents on membrane protein studies. Chem, 8(4), 980–1013. https://doi.org/10.1016/j.chempr.2022.02.007
   Web of Science ®Google Scholar
• Leferink, N. G. H., Antonyuk, S. V., Houwman, J. A., Scrutton, N. S., Eady, R. R., & Hasnain, S. S. (2014). Impact of residues remote from the catalytic centre on enzyme catalysis of copper nitrite reductase. Nature Communications, 5(1), 4395. https://doi.org/10.1038/ncomms5395
   PubMedGoogle Scholar
• Lehnert, N., Dong, H. T., Harland, J. B., Hunt, A. P., & White, C. J. (2018). Reversing nitrogen fixation. Nature Reviews Chemistry, 2(10), 278–289. https://doi.org/10.1038/s41570-018-0041-7
   Web of Science ®Google Scholar
• Lv, S., Zheng, F., Wang, Z., Hayat, K., Veiga, M. C., Kennes, C., & Chen, J. (2024). Unveiling novel pathways and key contributors in the nitrogen cycle: Validation of enrichment and taxonomic characterization of oxygenic denitrifying microorganisms in environmental samples. The Science of the Total Environment, 908, 168339. https://doi.org/10.1016/j.scitotenv.2023.168339
   PubMed Web of Science ®Google Scholar
• Mahinthichaichan, P., Gennis, R. B., & Tajkhorshid, E. (2018). Bacterial denitrifying nitric oxide reductases and aerobic respiratory terminal oxidases use similar delivery pathways for their molecular substrates. Biochimica et Biophysica Acta Bioenergetics, 1859(9), 712–724. https://doi.org/10.1016/j.bbabio.2018.06.002
   PubMed Web of Science ®Google Scholar
• Martínez-Espinosa, R. M., Marhuenda-Egea, F. C., & Bonete, M. J. (2001). Assimilatory nitrate reductase from the haloarchaeon Haloferax mediterranei: Purification and characterisation. FEMS Microbiology Letters, 204(2), 381–385. https://doi.org/10.1111/j.1574-6968.2001.tb10914.x
   PubMed Web of Science ®Google Scholar
• Matsumoto, Y., Tosha, T., Pisliakov, A. V., Hino, T., Sugimoto, H., Nagano, S., Sugita, Y., & Shiro, Y. (2012). Crystal structure of quinol-dependent nitric oxide reductase from Geobacillus stearothermophilus. Nature Structural & Molecular Biology, 19(2), 238–245. https://doi.org/10.1038/nsmb.2213
   PubMed Web of Science ®Google Scholar
• Mintmier, B., McGarry, J. M., Bain, D. J., & Basu, P. (2021). Kinetic consequences of the endogenous ligand to molybdenum in the DMSO reductase family: A case study with periplasmic nitrate reductase. Journal of Biological Inorganic Chemistry: JBIC: A Publication of the Society of Biological Inorganic Chemistry, 26(1), 13–28. https://doi.org/10.1007/s00775-020-01833-9
   PubMed Web of Science ®Google Scholar
• Mintmier, B., McGarry, J. M., Sparacino-Watkins, C. E., Sallmen, J., Fischer-Schrader, K., Magalon, A., McCormick, J. R., Stolz, J. F., Schwarz, G., Bain, D. J., & Basu, P. (2018). Molecular cloning, expression and biochemical characterization of periplasmic nitrate reductase from Campylobacter jejuni. FEMS Microbiology Letters, 365(16), fny151. https://doi.org/10.1093/femsle/fny151
   PubMed Web of Science ®Google Scholar
• Miralles-Robledillo, J. M., Bernabeu, E., Giani, M., Martínez-Serna, E., Martínez-Espinosa, R. M., & Pire, C. (2021). Distribution of denitrification among Haloarchaea: A comprehensive study. Microorganisms, 9(8), 1669. Article 8. https://doi.org/10.3390/microorganisms9081669
   PubMed Web of Science ®Google Scholar
• Moir, J. W. B., Baratta, D., Richardson, D. J., & Ferguson, S. J. (1993). The purification of a cd1-type nitrite reductase from, and the absence of a copper-type nitrite reductase from, the aerobic denitrifier Thiosphaera pantotropha; the role of pseudoazurin as an electron donor. European Journal of Biochemistry, 212(2), 377–385. https://doi.org/10.1111/j.1432-1033.1993.tb17672.x
   PubMedGoogle Scholar
• Moreno-Vivián, C., Cabello, P., Martínez-Luque, M., Blasco, R., & Castillo, F. (1999). Prokaryotic nitrate reduction: Molecular properties and functional distinction among bacterial nitrate reductases. Journal of Bacteriology, 181(21), 6573–6584. https://doi.org/10.1128/JB.181.21.6573-6584.1999
   PubMed Web of Science ®Google Scholar
• Morozkina, E. V., & Zvyagilskaya, R. A. (2007). Nitrate reductases: Structure, functions, and effect of stress factors. Biochemistry. Biokhimiia, 72(10), 1151–1160. https://doi.org/10.1134/s0006297907100124
   PubMed Web of Science ®Google Scholar
• Müller, C., Zhang, L., Zipfel, S., Topitsch, A., Lutz, M., Eckert, J., Prasser, B., Chami, M., Lü, W., Du, J., & Einsle, O. (2022). Molecular interplay of an assembly machinery for nitrous oxide reductase. Nature, 608(7923), 626–631. Article 7923. https://doi.org/10.1038/s41586-022-05015-2
   PubMed Web of Science ®Google Scholar
• Nojiri, M., Koteishi, H., Nakagami, T., Kobayashi, K., Inoue, T., Yamaguchi, K., & Suzuki, S. (2009). Structural basis of inter-protein electron transfer for nitrite reduction in denitrification. Nature, 462(7269), 117–120. https://doi.org/10.1038/nature08507
   PubMed Web of Science ®Google Scholar
• Nojiri, M., Xie, Y., Inoue, T., Yamamoto, T., Matsumura, H., Kataoka, K., Yamaguchi, K., Kai, Y., Suzuki, S., Deligeer. (2007). Structure and function of a hexameric copper-containing nitrite reductase. Proceedings of the National Academy of Sciences of the United States of America, 104(11), 4315–4320. https://doi.org/10.1073/pnas.0609195104
   PubMed Web of Science ®Google Scholar
• Oba, K., Suenaga, T., Kuroiwa, M., Riya, S., & Terada, A. (2022). Exploring the functions of efficient canonical denitrifying bacteria as N2O sinks: Implications from 15N tracer and transcriptome analyses. Environmental Science & Technology, 56(16), 11694–11706. https://doi.org/10.1021/acs.est.2c02119
   PubMed Web of Science ®Google Scholar
• Opperman, D. J., Murgida, D. H., Dalosto, S. D., Brondino, C. D., & Ferroni, F. M. (2019). A three-domain copper-nitrite reductase with a unique sensing loop. IUCrJ, 6(Pt 2), 248–258. https://doi.org/10.1107/S2052252519000241
   PubMedGoogle Scholar
• Pang, Y., & Wang, J. (2021). Various electron donors for biological nitrate removal: A review. The Science of the Total Environment, 794, 148699. https://doi.org/10.1016/j.scitotenv.2021.148699
   PubMed Web of Science ®Google Scholar
• Paraskevopoulou, V., & Falcone, F. (2018). Polyionic tags as enhancers of protein solubility in recombinant protein expression. Microorganisms, 6(2), 47. https://doi.org/10.3390/microorganisms6020047
   PubMed Web of Science ®Google Scholar
• Pauleta, S. R., Dell’Acqua, S., & Moura, I. (2013). Nitrous oxide reductase. Coordination Chemistry Reviews, 257(2), 332–349. https://doi.org/10.1016/j.ccr.2012.05.026
   Web of Science ®Google Scholar
• Peciak, K., Laurine, E., Tommasi, R., Choi, J., & Brocchini, S. (2019). Site-selective protein conjugation at histidine. Chemical Science, 10(2), 427–439. https://doi.org/10.1039/C8SC03355B
   PubMed Web of Science ®Google Scholar
• Pedroso, H. A., Silveira, C. M., Almeida, R. M., Almeida, A., Besson, S., Moura, I., Moura, J. J. G., & Almeida, M. G. (2016). Electron transfer and docking between cytochrome cd1 nitrite reductase and different redox partners—A comparative study. Biochimica et Biophysica Acta, 1857(9), 1412–1421. https://doi.org/10.1016/j.bbabio.2016.04.279
   PubMed Web of Science ®Google Scholar
• Perret, G., & Boschetti, E. (2020). Aptamer-based affinity chromatography for protein extraction and purification. Aptamers in Biotechnology, 93–193.
   Google Scholar
• Philippot, L., & Højberg, O. (1999). Dissimilatory nitrate reductases in bacteria. Biochimica et Biophysica Acta, 1446(1-2), 1–23. https://doi.org/10.1016/s0167-4781(99)00072-x
   PubMedGoogle Scholar
• Pignol, D., Adriano, J. M., Fontecilla-Camps, J. C., & Sabaty, M. (2001). Crystallization and preliminary X-ray analysis of the periplasmic nitrate reductase (NapA-NapB complex) from Rhodobacter sphaeroides f. Sp. Denitrificans. Acta Crystallographica. Section D, Biological Crystallography, 57(Pt 12), 1900–1902. https://doi.org/10.1107/s0907444901015852
   PubMedGoogle Scholar
• Pinho, D., Besson, S., Silva, P. J., de Castro, B., & Moura, I. (2005). Isolation and spectroscopic characterization of the membrane-bound nitrate reductase from Pseudomonas chlororaphis DSM 50135. Biochimica et Biophysica Acta, 1723(1-3), 151–162. https://doi.org/10.1016/j.bbagen.2005.02.008
   PubMed Web of Science ®Google Scholar
• Pisliakov, A. V., Hino, T., Shiro, Y., & Sugita, Y. (2012). Molecular dynamics simulations reveal proton transfer pathways in cytochrome C-dependent nitric oxide reductase. PLoS Computational Biology, 8(8), e1002674. https://doi.org/10.1371/journal.pcbi.1002674
   PubMed Web of Science ®Google Scholar
• Pomowski, A., Zumft, W. G., Kroneck, P. M. H., & Einsle, O. (2011). N2O binding at a [4Cu:2S] copper–sulphur cluster in nitrous oxide reductase. Nature, 477(7363), 234–237. https://doi.org/10.1038/nature10332
   PubMed Web of Science ®Google Scholar
• Porath, J., Carlsson, J., Olsson, I., & Belfrage, G. (1975). Metal chelate affinity chromatography, a new approach to protein fractionation. Nature, 258(5536), 598–599. https://doi.org/10.1038/258598a0
   PubMed Web of Science ®Google Scholar
• Prasser, B., Schöner, L., Zhang, L., & Einsle, O. (2021). The copper chaperone NosL forms a heterometal site for Cu delivery to nitrous oxide reductase. Angewandte Chemie (International ed. in English), 60(34), 18810–18814. https://doi.org/10.1002/anie.202106348
   PubMed Web of Science ®Google Scholar
• Privé, G. G. (2007). Detergents for the stabilization and crystallization of membrane proteins. Methods (San Diego, Calif.), 41(4), 388–397. https://doi.org/10.1016/j.ymeth.2007.01.007
   PubMed Web of Science ®Google Scholar
• Prudêncio, M., Pereira, A. S., Tavares, P., Besson, S., Cabrito, I., Brown, K., Samyn, B., Devreese, B., Van Beeumen, J., Rusnak, F., Fauque, G., Moura, J. J., Tegoni, M., Cambillau, C., & Moura, I. (2000). Purification, characterization, and preliminary crystallographic study of copper-containing nitrous oxide reductase from Pseudomonas nautica 617. Biochemistry, 39(14), 3899–3907. https://doi.org/10.1021/bi9926328
   PubMed Web of Science ®Google Scholar
• Qi, C., Zhou, Y., Suenaga, T., Oba, K., Lu, J., Wang, G., Zhang, L., Yoon, S., & Terada, A. (2022). Organic carbon determines nitrous oxide consumption activity of clade I and II nosZ bacteria: Genomic and biokinetic insights. Water Research, 209, 117910. https://doi.org/10.1016/j.watres.2021.117910
   PubMed Web of Science ®Google Scholar
• Qin, X., Deng, L., Hu, C., Li, L., & Chen, X. (2017). Copper-containing nitrite reductase employing proton-coupled spin-exchanged electron-transfer and multiproton synchronized transfer to reduce nitrite. Chemistry (Weinheim an Der Bergstrasse, Germany), 23(59), 14900–14910. https://doi.org/10.1002/chem.201703221
   PubMed Web of Science ®Google Scholar
• Ravishankara, A. R., Daniel, J. S., & Portmann, R. W. (2009). Nitrous oxide (N2O): The dominant ozone-depleting substance emitted in the 21st century. Science (New York, N.Y.), 326(5949), 123–125. https://doi.org/10.1126/science.1176985
   PubMed Web of Science ®Google Scholar
• Rendon, J., Pilet, E., Fahs, Z., Seduk, F., Sylvi, L., Hajj Chehade, M., Pierrel, F., Guigliarelli, B., Magalon, A., & Grimaldi, S. (2015). Demethylmenaquinol is a substrate of Escherichia coli nitrate reductase A (NarGHI) and forms a stable semiquinone intermediate at the NarGHI quinol oxidation site. Biochimica et Biophysica Acta, 1847(8), 739–747. https://doi.org/10.1016/j.bbabio.2015.05.001
   PubMed Web of Science ®Google Scholar
• Richardson, D. J., Berks, B. C., Russell, D. A., Spiro, S., & Taylor, C. J. (2001). Functional, biochemical and genetic diversity of prokaryotic nitrate reductases. Cellular and Molecular Life Sciences: CMLS, 58(2), 165–178. https://doi.org/10.1007/PL00000845
   PubMed Web of Science ®Google Scholar
• Richter, C. D., Allen, J. W. A., Higham, C. W., Koppenhofer, A., Zajicek, R. S., Watmough, N. J., & Ferguson, S. J. (2002). Cytochrome cd1, reductive activation and kinetic analysis of a multifunctional respiratory enzyme. The Journal of Biological Chemistry, 277(5), 3093–3100. https://doi.org/10.1074/jbc.M108944200
   PubMed Web of Science ®Google Scholar
• Rinaldo, S., Giardina, G., Castiglione, N., Stelitano, V., & Cutruzzolà, F. (2011). The catalytic mechanism of Pseudomonas aeruginosa cd 1 nitrite reductase. Biochemical Society Transactions, 39(1), 195–200. https://doi.org/10.1042/BST0390195
   PubMedGoogle Scholar
• Rinaldo, S., Sam, K. A., Castiglione, N., Stelitano, V., Arcovito, A., Brunori, M., Allen, J. W. A., Ferguson, S. J., & Cutruzzolà, F. (2011). Observation of fast release of NO from ferrous d 1 haem allows formulation of a unified reaction mechanism for cytochrome cd 1 nitrite reductases. The Biochemical Journal, 435(1), 217–225. https://doi.org/10.1042/BJ20101615
   PubMedGoogle Scholar
• Rockström, J., Steffen, W., Noone, K., Persson, Å., Chapin, F. S. I., Lambin, E., Lenton, T. M., Scheffer, M., Folke, C., Schellnhuber, H. J., Nykvist, B., de Wit, C. A., Hughes, T., van der Leeuw, S., Rodhe, H., Sörlin, S., Snyder, P. K., Costanza, R., Svedin, U., … Foley, J. (2009). Planetary boundaries: Exploring the safe operating space for humanity. Ecology and Society, 14(2), 32. https://doi.org/10.5751/ES-03180-140232
   Web of Science ®Google Scholar
• Sadeghi, S., Deshpande, S., Vallerinteavide Mavelli, G., Aksoyoglu, A., Bafna, J., Winterhalter, M., Kini, R. M., Lane, D. P., & Drum, C. L. (2021). A general approach to protein folding using thermostable exoshells. Nature Communications, 12(1), 5720. https://doi.org/10.1038/s41467-021-25996-4
   PubMed Web of Science ®Google Scholar
• Salomonsson, L., Reimann, J., Tosha, T., Krause, N., Gonska, N., Shiro, Y., & Adelroth, P. (2012). Proton transfer in the quinol-dependent nitric oxide reductase from Geobacillus stearothermophilus during reduction of oxygen. Biochimica et Biophysica Acta, 1817(10), 1914–1920. https://doi.org/10.1016/j.bbabio.2012.04.007
   PubMed Web of Science ®Google Scholar
• Schneider, L. K., & Einsle, O. (2016). Role of calcium in secondary structure stabilization during maturation of nitrous oxide reductase. Biochemistry, 55(10), 1433–1440. https://doi.org/10.1021/acs.biochem.5b01278
   PubMed Web of Science ®Google Scholar
• Schuster, L. A., & Reisch, C. R. (2022). Plasmids for controlled and tunable high-level expression in E. coli. Applied and Environmental Microbiology, 88(22), e00939-22. https://doi.org/10.1128/aem.00939-22
   PubMed Web of Science ®Google Scholar
• Sengupta, S., Shaila, M. S., & Rao, G. R. (1996). Purification and characterization of assimilatory nitrite reductase from Candida utilis. The Biochemical Journal, 317(Pt 1), 147–155. https://doi.org/10.1042/bj3170147
   PubMedGoogle Scholar
• Singh, B. K., Bardgett, R. D., Smith, P., & Reay, D. S. (2010). Microorganisms and climate change: Terrestrial feedbacks and mitigation options. Nature Reviews. Microbiology, 8(11), 779–790. https://doi.org/10.1038/nrmicro2439
   PubMed Web of Science ®Google Scholar
• Singh, A., Upadhyay, V., Upadhyay, A. K., Singh, S. M., & Panda, A. K. (2015). Protein recovery from inclusion bodies of Escherichia coli using mild solubilization process. Microbial Cell Factories, 14(1), 41. https://doi.org/10.1186/s12934-015-0222-8
   PubMed Web of Science ®Google Scholar
• Structural Genomics Consortium, Architecture et Fonction des Macromolécules Biologiques, Berkeley Structural Genomics Center, China Structural Genomics Consortium, Integrated Center for Structure and Function Innovation, Israel Structural Proteomics Center, Joint Center for Structural Genomics, Midwest Center for Structural Genomics, New York Structural GenomiX Research Center for Structural Genomics, Northeast Structural Genomics Consortium, Oxford Protein Production Facility, Protein Sample Production Facility, Max Delbrück Center for Molecular Medicine, RIKEN Structural Genomics/Proteomics Initiative, & SPINE2-Complexes. (2008). Protein production and purification. Nature Methods, 5(2), 135–146. https://doi.org/10.1038/nmeth.f.202
   PubMed Web of Science ®Google Scholar
• Suharti, S. (2019). The phenomenon of UV-Vis spectroscopic changing due the binding of CO to the nitric oxide reductase from Bacillus Azotoformans. IOP Conference Series: Materials Science and Engineering, 509, 012141. https://doi.org/10.1088/1757-899X/509/1/012141
   Google Scholar
• Suharti, Heering, H. A., de Vries, S. (2004). NO reductase from Bacillus azotoformans is a bifunctional enzyme accepting electrons from menaquinol and a specific endogenous membrane-bound cytochrome c551. Biochemistry, 43(42), 13487–13495. https://doi.org/10.1021/bi0488101
   PubMed Web of Science ®Google Scholar
• Suharti, Strampraad, M. J., Schröder, I., de Vries, S. (2001). A novel copper A containing menaquinol NO reductase from Bacillus azotoformans. Biochemistry, 40(8), 2632–2639. https://doi.org/10.1021/bi0020067
   PubMed Web of Science ®Google Scholar
• Sun, Y., Xu, J., Zhou, H., Zhang, H., Wu, J., & Yang, L. (2023). Recombinant protein expression Chassis library of Vibrio natriegens by fine-tuning the expression of T7 RNA polymerase. ACS Synthetic Biology, 12(2), 555–564. https://doi.org/10.1021/acssynbio.2c00562
   PubMedGoogle Scholar
• Suzuki, S., Kataoka, K., & Yamaguchi, K. (2000). Metal coordination and mechanism of multicopper nitrite reductase. Accounts of Chemical Research, 33(10), 728–735. https://doi.org/10.1021/ar9900257
   PubMed Web of Science ®Google Scholar
• Tan, W., Liao, T. H., Wang, J., Ye, Y., Wei, Y. C., Zhou, H. K., Xiao, Y., Zhi, X. Y., Shao, Z. H., Lyu, L. D., & Zhao, G. P. (2020). A recently evolved diflavin-containing monomeric nitrate reductase is responsible for highly efficient bacterial nitrate assimilation. The Journal of Biological Chemistry, 295(15), 5051–5066. https://doi.org/10.1074/jbc.RA120.012859
   PubMed Web of Science ®Google Scholar
• ter Beek, J., Krause, N., Reimann, J., Lachmann, P., & Ädelroth, P. (2013). The nitric-oxide reductase from Paracoccus denitrificans uses a single specific proton pathway. The Journal of Biological Chemistry, 288(42), 30626–30635. https://doi.org/10.1074/jbc.M113.497347
   PubMed Web of Science ®Google Scholar
• Terasaka, E., Okada, N., Sato, N., Sako, Y., Shiro, Y., & Tosha, T. (2014). Characterization of quinol-dependent nitric oxide reductase from Geobacillus stearothermophilus: Enzymatic activity and active site structure. Biochimica et Biophysica Acta, 1837(7), 1019–1026. https://doi.org/10.1016/j.bbabio.2014.02.017
   PubMed Web of Science ®Google Scholar
• Tian, H., Lu, C., Ciais, P., Michalak, A. M., Canadell, J. G., Saikawa, E., Huntzinger, D. N., Gurney, K. R., Sitch, S., Zhang, B., Yang, J., Bousquet, P., Bruhwiler, L., Chen, G., Dlugokencky, E., Friedlingstein, P., Melillo, J., Pan, S., Poulter, B., … Wofsy, S. C. (2016). The terrestrial biosphere as a net source of greenhouse gases to the atmosphere. Nature, 531(7593), 225–228. https://doi.org/10.1038/nature16946
   PubMed Web of Science ®Google Scholar
• Tian, H., Xu, R., Canadell, J. G., Thompson, R. L., Winiwarter, W., Suntharalingam, P., Davidson, E. A., Ciais, P., Jackson, R. B., Janssens-Maenhout, G., Prather, M. J., Regnier, P., Pan, N., Pan, S., Peters, G. P., Shi, H., Tubiello, F. N., Zaehle, S., Zhou, F., … Yao, Y. (2020). A comprehensive quantification of global nitrous oxide sources and sinks. Nature, 586(7828), 248–256. https://doi.org/10.1038/s41586-020-2780-0
   PubMed Web of Science ®Google Scholar
• Torregrosa-Crespo, J., González-Torres, P., Bautista, V., Esclapez, J. M., Pire, C., Camacho, M., Bonete, M. J., Richardson, D. J., Watmough, N. J., & Martínez-Espinosa, R. M. (2017). Analysis of multiple haloarchaeal genomes suggests that the quinone-dependent respiratory nitric oxide reductase is an important source of nitrous oxide in hypersaline environments. Environmental Microbiology Reports, 9(6), 788–796. https://doi.org/10.1111/1758-2229.12596
   PubMed Web of Science ®Google Scholar
• Varadi, M., Anyango, S., Deshpande, M., Nair, S., Natassia, C., Yordanova, G., Yuan, D., Stroe, O., Wood, G., Laydon, A., Žídek, A., Green, T., Tunyasuvunakool, K., Petersen, S., Jumper, J., Clancy, E., Green, R., Vora, A., Lutfi, M., … Velankar, S. (2022). AlphaFold protein structure database: Massively expanding the structural coverage of protein-sequence space with high-accuracy models. Nucleic Acids Research, 50(D1), D439–D444. https://doi.org/10.1093/nar/gkab1061
   PubMed Web of Science ®Google Scholar
• Wg, Z. (1997). Cell biology and molecular basis of denitrification. Microbiology and Molecular Biology Reviews: MMBR, 61(4), 533–616. https://doi.org/10.1128/mmbr.61.4.533-616.1997
   Web of Science ®Google Scholar
• Williams, P. A., Fülöp, V., Garman, E. F., Saunders, N. F. W., Ferguson, S. J., & Hajdu, J. (1997). Haem-ligand switching during catalysis in crystals of a nitrogen-cycle enzyme. Nature, 389(6649), 406–412. https://doi.org/10.1038/38775
   PubMed Web of Science ®Google Scholar
• Yamagiwa, R., Kurahashi, T., Takeda, M., Adachi, M., Nakamura, H., Arai, H., Shiro, Y., Sawai, H., & Tosha, T. (2018). Pseudomonas aeruginosa overexpression system of nitric oxide reductase for in vivo and in vitro mutational analyses. Biochimica et Biophysica Acta. Bioenergetics, 1859(5), 333–341. https://doi.org/10.1016/j.bbabio.2018.02.009
   PubMed Web of Science ®Google Scholar
• Zhang, L., Bill, E., Kroneck, P. M. H., & Einsle, O. (2021a). A [3Cu:2S] cluster provides insight into the assembly and function of the CuZ site of nitrous oxide reductase. Chemical Science, 12(9), 3239–3244. https://doi.org/10.1039/d0sc05204c
   PubMed Web of Science ®Google Scholar
• Zhang, L., Bill, E., Kroneck, P. M. H., & Einsle, O. (2021b). Histidine-gated proton-coupled electron transfer to the CuA site of nitrous oxide reductase. Journal of the American Chemical Society, 143(2), 830–838. https://doi.org/10.1021/jacs.0c10057
   PubMed Web of Science ®Google Scholar
• Zhang, Z. X., Nong, F. T., Wang, Y. Z., Yan, C. X., Gu, Y., Song, P., & Sun, X. M. (2022). Strategies for efficient production of recombinant proteins in Escherichia coli: Alleviating the host burden and enhancing protein activity. Microbial Cell Factories, 21(1), 191. https://doi.org/10.1186/s12934-022-01917-y
   PubMed Web of Science ®Google Scholar
• Zhang, Z. X., Wang, Y. Z., Nong, F. T., Xu, Y., Ye, C., Gu, Y., Sun, X. M., & Huang, H. (2022). Developing a dynamic equilibrium system in Escherichia coli to improve the production of recombinant proteins. Applied Microbiology and Biotechnology, 106(18), 6125–6137. https://doi.org/10.1007/s00253-022-12145-0
   PubMed Web of Science ®Google Scholar
• Zhang, L., Wüst, A., Prasser, B., Müller, C., & Einsle, O. (2019). Functional assembly of nitrous oxide reductase provides insights into copper site maturation. Proceedings of the National Academy of Sciences of the United States of America, 116(26), 12822–12827. https://doi.org/10.1073/pnas.1903819116
   PubMed Web of Science ®Google Scholar
• Zhao, Z., Rothery, R. A., & Weiner, J. H. (2003). Transient kinetic studies of heme reduction in Escherichia coli nitrate reductase A (NarGHI) by menaquinol. Biochemistry, 42(18), 5403–5413. https://doi.org/10.1021/bi027221x
   PubMed Web of Science ®Google Scholar
• Zumft, W. G. (2005a). Biogenesis of the bacterial respiratory CuA, Cu-S enzyme nitrous oxide reductase. Journal of Molecular Microbiology and Biotechnology, 10(2-4), 154–166. https://doi.org/10.1159/000091562
   PubMed Web of Science ®Google Scholar
• Zumft, W. G. (2005b). Nitric oxide reductases of prokaryotes with emphasis on the respiratory, heme–copper oxidase type. Journal of Inorganic Biochemistry, 99(1), 194–215. https://doi.org/10.1016/j.jinorgbio.2004.09.024
   PubMed Web of Science ®Google Scholar