Thompson, R. L. et al. Acceleration of global N2O emissions seen from two decades of atmospheric inversion. Nat. Clim. Chang. 9, 993–997 (2019).
Ravishankara, A. R., Daniel, J. S. & Portmann, R. W. Nitrous oxide (N2O): the dominant ozone-depleting substance emitted in the 21st century. Science 326, 123–125 (2009).
Tian, H. Q. et al. A comprehensive quantification of global nitrous oxide sources and sinks. Nature 586, 248–256 (2020).
Honisch, U. & Zumft, W. G. Operon structure and regulation of the nos gene region of Pseudomonas stutzeri, encoding an ABC-type ATPase for maturation of nitrous oxide reductase. J. Bacteriol. 185, 1895–1902 (2003).
Zumft, W. G. & Kroneck, P. M. H. Respiratory transformation of nitrous oxide (N2O) to dinitrogen by Bacteria and Archaea. Adv. Microb. Physiol. 52, 107–225 (2007).
Pomowski, A., Zumft, W. G., Kroneck, P. M. H. & Einsle, O. N2O binding at a [4Cu:2S] copper–sulphur cluster in nitrous oxide reductase. Nature 477, 234–237 (2011).
Thomson, A. J., Giannopoulos, G., Pretty, J., Baggs, E. M. & Richardson, D. J. Biological sources and sinks of nitrous oxide and strategies to mitigate emissions. Phil. Trans. R. Soc. B 367, 1157–1168 (2012).
Butterbach-Bahl, K., Baggs, E. M., Dannenmann, M., Kiese, R. & Zechmeister-Boltenstern, S. Nitrous oxide emissions from soils: how well do we understand the processes and their controls? Phil. Trans. R. Soc. B 368, 20130122 (2013).
Jansson, J. K. & Hofmockel, K. S. Soil microbiomes and climate change. Nat. Rev. Microbiol. 18, 35–46 (2020).
Stein, L. Y. The long-term relationship between microbial metabolism and greenhouse gases. Trends Microbiol. 28, 500–511 (2020).
Torres, M. J. et al. Nitrous oxide metabolism in nitrate-reducing bacteria: physiology and regulatory mechanisms. Adv. Microb. Physiol. 68, 353–432 (2016).
Pauleta, S. R., Carepo, M. S. P. & Moura, I. Source and reduction of nitrous oxide. Coord. Chem. Rev. 387, 436–449 (2019).
Solomon, E. I. et al. Copper active sites in biology. Chem. Rev. 114, 3659–3853 (2014).
Dupont, C. L., Grass, G. & Rensing, C. Copper toxicity and the origin of bacterial resistance—new insights and applications. Metallomics 3, 1109–1118 (2011).
Schneider, L. K. & Einsle, O. Role of calcium in secondary structure stabilization during maturation of nitrous oxide reductase. Biochemistry 55, 1433–1440 (2016).
Locher, K. P. Mechanistic diversity in ATP-binding cassette (ABC) transporters. Nat. Struct. Mol. Biol. 23, 487–493 (2016).
Higgins, C. F. ABC transporters: from microorganisms to man. Annu. Rev. Cell Biol. 8, 67–113 (1992).
Li, Y. Y., Orlando, B. J. & Liao, M. F. Structural basis of lipopolysaccharide extraction by the LptB2FGC complex. Nature 567, 486–490 (2019).
Fitzpatrick, A. W. P. et al. Structure of the MacAB–TolC ABC-type tripartite multidrug efflux pump. Nat. Microbiol. 2, 17070 (2017).
Zumft, W. G., Viebrock-Sambale, A. & Braun, C. Nitrous oxide reductase from denitrifying Pseudomonas stutzeri—genes for copper-processing and properties of the deduced products, including a new member of the family of ATP/GTP-binding proteins. Eur. J. Biochem. 192, 591–599 (1990).
Zhang, L., Wüst, A., Prasser, B., Müller, C. & Einsle, O. Functional assembly of nitrous oxide reductase provides insights into copper site maturation. Proc. Natl Acad. Sci. USA 116, 12822–12827 (2019).
Zumft, W. G. Biogenesis of the bacterial respiratory CuA, Cu–S enzyme nitrous oxide reductase. J. Mol. Microbiol. Biotechnol. 10, 154–166 (2005).
Wunsch, P. & Zumft, W. G. Functional domains of NosR, a novel transmembrane iron-sulfur flavoprotein necessary for nitrous oxide respiration. J. Bacteriol. 187, 1992–2001 (2005).
Bennett, S. P. et al. NosL is a dedicated copper chaperone for assembly of the CuZ center of nitrous oxide reductase. Chem. Sci. 10, 4985–4993 (2019).
McGuirl, M. A., Bollinger, J. A., Cosper, N., Scott, R. A. & Dooley, D. M. Expression, purification, and characterization of NosL, a novel Cu(II) protein of the nitrous oxide reductase (nos) gene cluster. J. Biol. Inorg. Chem. 6, 189–195 (2001).
Okuda, S. & Tokuda, H. Lipoprotein sorting in bacteria. Annu. Rev. Microbiol. 65, 239–259 (2011).
Ciccarelli, F. D., Copley, R. R., Doerks, T., Russell, R. B. & Bork, P. CASH—a β-helix domain widespread among carbohydrate-binding proteins. Trends Biochem. Sci. 27, 59–62 (2002).
Lee, J. Y. et al. Crystal structure of the human sterol transporter ABCG5/ABCG8. Nature 533, 561–564 (2016).
Thomas, C. & Tampé, R. Multifaceted structures and mechanisms of ABC transport systems in health and disease. Curr. Opin. Struct. Biol. 51, 116–128 (2018).
Rees, D. C., Johnson, E. & Lewinson, O. ABC transporters: the power to change. Nat. Rev. Mol. Cell Biol. 10, 218–227 (2009).
Bi, Y. C., Mann, E., Whitfield, C. & Zimmer, J. Architecture of a channel-forming O-antigen polysaccharide ABC transporter. Nature 553, 361–365 (2018).
Qian, H. W. et al. Structure of the human lipid exporter ABCA1. Cell 169, 1228–1234 (2017).
Diederichs, K. et al. Crystal structure of MalK, the ATPase subunit of the trehalose/maltose ABC transporter of the archaeon Thermococcus litoralis. EMBO J. 19, 5951–5961 (2000).
Nguyen, P. T., Lai, J. Y., Lee, A. T., Kaiser, J. T. & Rees, D. C. Noncanonical role for the binding protein in substrate uptake by the MetNI methionine ATP binding cassette (ABC) transporter. Proc. Natl Acad. Sci. USA 115, E10596–E10604 (2018).
Oldham, M. L., Khare, D., Quiocho, F. A., Davidson, A. L. & Chen, J. Crystal structure of a catalytic intermediate of the maltose transporter. Nature 450, 515–521 (2007).
Manolaridis, I. et al. Cryo-EM structures of a human ABCG2 mutant trapped in ATP-bound and substrate-bound states. Nature 563, 426–430 (2018).
Banci, L., Bertini, I., Del Conte, R., Markey, J. & Ruiz-Duenas, F. J. Copper trafficking: the solution structure of Bacillus subtilis CopZ. Biochemistry 40, 15660–15668 (2001).
Culotta, V. C. et al. The copper chaperone for superoxide dismutase. J. Biol. Chem. 272, 23469–23472 (1997).
Prasser, B., Schöner, L., Zhang, L. & Einsle, O. The copper chaperone NosL forms a heterometal site for Cu delivery to nitrous oxide reductase. Angew. Chem. Int. Edn Engl. 60, 18810–18814 (2021).
Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K. & Pease, L. R. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77, 51–59 (1989).
Ritchie, T. K. et al. Reconstitution of membrane proteins in phospholipid bilayer nanodiscs. Methods Enzymol. 464, 211–231 (2009).
Chifflet, S., Torriglia, A., Chiesa, R. & Tolosa, S. A method for the determination of inorganic phosphate in the presence of labile organic phosphate and high concentrations of protein—application to lens ATPases. Anal. Biochem. 168, 1–4 (1988).
Mastronarde, D. N. Automated electron microscope tomography using robust prediction of specimen movements. J. Struct. Biol. 152, 36–51 (2005).
Zheng, S. Q. et al. MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy. Nat. Methods 14, 331–332 (2017).
Scheres, S. H. W. RELION: implementation of a Bayesian approach to cryo-EM structure determination. J. Struct. Biol. 180, 519–530 (2012).
Zivanov, J. et al. New tools for automated high-resolution cryo-EM structure determination in RELION-3. eLife 7, e42166 (2018).
Zhang, K. Gctf: real-time CTF determination and correction. J. Struct. Biol. 193, 1–12 (2016).
Rohou, A. & Grigorieff, N. CTFFIND4: fast and accurate defocus estimation from electron micrographs. J. Struct. Biol. 192, 216–221 (2015).
Punjani, A., Rubinstein, J. L., Fleet, D. J. & Brubaker, M. A. cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination. Nat. Methods 14, 290–296 (2017).
Zivanov, J., Nakane, T. & Scheres, S. H. W. A Bayesian approach to beam-induced motion correction in cryo-EM single-particle analysis. IUCrJ 6, 5–17 (2019).
Scheres, S. H. W. Processing of structurally heterogeneous cryo-EM data in RELION. Methods Enzymol. 579, 125–157 (2016).
Bai, X. C., Rajendra, E., Yang, G. H., Shi, Y. G. & Scheres, S. H. W. Sampling the conformational space of the catalytic subunit of human γ-secretase. eLife 4, e11182 (2015).
Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D 66, 213–221 (2010).
Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. Features and development of Coot. Acta Crystallogr. D 66, 486–501 (2010).
Williams, C. J. et al. MolProbity: more and better reference data for improved all-atom structure validation. Protein Sci. 27, 293–315 (2018).
Goddard, T. D., Huang, C. C. & Ferrin, T. E. Visualizing density maps with UCSF Chimera. J. Struct. Biol. 157, 281–287 (2007).
Zhang, L., Trncik, C., Andrade, S. L. & Einsle, O. The flavinyl transferase ApbE of Pseudomonas stutzeri matures the NosR protein required for nitrous oxide reduction. Biochim. Biophys. Acta 1858, 95–102 (2017).
Dell’Acqua, S. et al. Electron transfer complex between nitrous oxide reductase and cytochrome c552 from Pseudomonas nautica: kinetic, nuclear magnetic resonance, and docking studies. Biochemistry 47, 10852–10862 (2008).
Jumper, J. et al. Highly accurate protein structure prediction with AlphaFold. Nature 596, 583–589 (2021).
More News
Daily briefing: Why exercise is good for us
Daily briefing: Orangutan is first wild animal seen using medicinal plant
Old electric-vehicle batteries can find new purpose — on the grid