References
- Hau HH, Gralnick JA. Ecology and biotechnology of the genus Shewanella. Annu Rev Microbiol. 2007;61:237–258.
- Falkowski PG, Fenchel T, Delong EF. The microbial engines that drive Earth’s biogeochemical cycles. Science. 2008;320:1034–1039.
- Murakami C, Ohmae E, Tate S, et al. Cloning and characterization of dihydrofolate reductases from deep-sea bacteria. J Biochem. 2010;147:591–599.
- Murakami C, Ohmae E, Tate S, et al. Comparative study on dihydrofolate reductases from Shewanella species living in deep-sea and ambient atmospheric-pressure environments. Extremophiles. 2011;15:165–175.
- Masanari M, Wakai S, Ishida M, et al. Correlation between the optimal growth pressures of four Shewanella species and the stabilities of their cytochromes c5. Extremophiles. 2014;18:617–627.
- Masanari M, Fujii S, Kawahara K, et al. Comparative study on stabilization mechanism of monomeric cytochrome c5 from deep-sea piezophilic Shewanella violacea. Biosci Biotechnol Biochem. 2016;80:2365–2370.
- Fujii S, Masanari-Fujii M, Kobayashi S, et al. Commonly stabilized cytochromes c from deep-sea Shewanella and Pseudomonas. Biosci Biotechnol Biochem. 2018;82:792–799.
- Kawano H, Nakasone K, Matsumoto M, et al. Differential pressure resistance in the activity of RNA polymerase isolated from Shewanella violacea and Escherichia coli. Extremophiles. 2004;8:367–375.
- Kato C, Sato T, Abe F, et al. Discoveries of deep-sea piezophiles, and their pressure adapted enzymes. Proc 4th Int Conf High Pressure Biosci Biotechnol. 2007;1:114–121.
- Kasahara R, Sato T, Tamegai H, et al. Piezo-adapted 3-isopropylmalate dehydrogenase of the obligate piezophile Shewanella benthica DB21MT-2 isolated from the 11,000-m depth of the Mariana trench. Biosci Biotechnol Biochem. 2009;73:2541–2543.
- Sakai Y, Toda K, Mitani Y, et al. Properties of the membrane-bound 5ʹ-nucleotidase and utilization of extracellular ATP in Vibrio parahaemolyticus. J Gen Microbiol. 1987;133:2751–2757.
- Kuribayashi TA, Fujii S, Masanari M, et al. Difference in NaCl tolerance of membrane-bound 5ʹ-nucleotidases purified from deep-sea and brackish water Shewanella species. Extremophiles. 2017;21:357–368.
- Lowry OH, Rosebrough NJ, Farr AL, et al. Protein measurement with the folin phenol reagent. J Biol Chem. 1951;193:265–275.
- Fiske CH, Subbarow Y. The colorimetric determination of phosphorus. J Biol Chem. 1925;66:375–400.
- Yagi H, Isobe N, Itabashi N, et al. Characterization of a long-lived alginate lyase derived from Shewanella species YH1. Mar Drugs. 2017;16:E4.
- Micsonai A, Wien F, Kernya L, et al. Accurate secondary structure prediction and fold recognition for circular dichroism spectroscopy. Proc Natl Acad Sci USA. 2015;112:E3095–E3103.
- Micsonai A, Wien F, Bulyáki É, et al. BeStSel: a web server for accurate protein secondary structure prediction and fold recognition from the circular dichroism spectra. Nucleic Acids Res. 2018;46:W315–W322.
- Fujii S, Masanari M, Inoue H, et al. High thermal stability and unique trimer formation of cytochrome c’ from thermophilic Hydrogenophilus thermoluteolus. Biosci Biotechnol Biochem. 2013;77:1677–1681.
- Uchiyama S, Ohshima A, Nakamura S, et al. Complete thermal-unfolding profiles of oxidized and reduced cytochromes c. J Am Chem Soc. 2004;126:14684–14685.
- Biasini M, Bienert S, Waterhouse A, et al. SWISS-MODEL: modelling protein tertiary and quaternary structure using evolutionary information. Nucleic Acids Res. 2014;42:W252–W258.
- Lanyi JK. Salt-dependent properties of proteins from extremely halophilic bacteria. Bacteriol Rev. 1974;38:272–290.
- Wakai S, Abe A, Fujii S, et al. Pyrophosphate hydrolysis in the extremely halophilic archaeon Haloarcula japonica is catalyzed by a single enzyme with a broad ionic strength range. Extremophiles. 2017;21:471–477.
- Knöfel T, Sträter N. Mechanism of hydrolysis of phosphate esters by the dimetal center of 5ʹ-nucleotidase based on crystal structures. J Mol Biol. 2001;309:239–254.
- Neu HC. The 5′-nucleotidase of Escherichia coli. I. purification and properties. J Biol Chem. 1967;242:3896–3904.
- Pathak RK, Dessingou J, Rao CP. Multiple sensor array of Mn2+, Fe2+, Co2+, Ni2+, Cu2+, and Zn2+ complexes of a triazole linked imino-phenol based calix[4]arene conjugate for the selective recognition of Asp, Glu, Cys, and His. Anal Chem. 2012;84:8294–8300.
- Knöfel T, Sträter N. X-ray structure of the Escherichia coli periplasmic 5ʹ-nucleotidase containing a dimetal catalytic site. Nat Struct Biol. 1999;6:448–453.
- Nogi Y, Kato C, Horikoshi K. Taxonomic studies of deep-sea barophilic Shewanella strains and description of Shewanella violacea sp. nov. Arch Microbiol. 1998;170:331–338.
- Venkateswaran K, Dollhopf ME, Aller R, et al. Shewanella amazonensis sp. nov., a novel metal-reducing facultative anaerobe from amazonian shelf muds. Int J Syst Bacteriol. 1998;48:965–972.
- Lee CF, Makhatadze GI, Wong KB. Effects of charge-to-alanine substitutions on the stability of ribosomal protein L30e from Thermococcus celer. Biochemistry. 2005;44:16817–16825.
- Perl D, Mueller U, Heinemann U, et al. Two exposed amino acid residues confer thermostability on a cold shock protein. Nat Struct Biol. 2000;7:380–383.
- Riedel A, Mehnert M, Paul CE, et al. Functional characterization and stability improvement of a ‘thermophilic-like’ ene-reductase from Rhodococcus opacus 1CP. Front Microbiol. 2015;6:1073.
- Wu JP, Li M, Zhou Y, et al. Introducing a salt bridge into the lipase of Stenotrophomonas maltophilia results in a very large increase in thermal stability. Biotechnol Lett. 2015;37:403–407.