1.
Morgan, J. W. and Anderst, E. "Chemical composition of Earth, Venus, and Mercury". Proc.
Natl. Acad. Sci. U. S. A. 77, 6973–6977 (1980).
2.
Steudel, R. The chemical sulfur cycle. In Environmental Technologies to Treat Sulfur
Pollution: Principles and Engineering. Part II The Sulfur Cycle. (2000).
3.
Sevier, C. S. and Kaiser, C. A. "Conservation and diversity of the cellular disulfide bond
formation pathways". Antioxid. Redox Signal. 8, 797–811 (2006).
4.
Loenen, W. A. M. "S-adenosylmethionine: jack of all trades and master of everything?".
(2006).
5.
Morris, A. A. M. et al. "Guidelines for the diagnosis and management of cystathionine betasynthase deficiency". J. Inherit. Metab. Desease (2016) doi:10.1007/s10545-016-9979-0.
6.
Ansar, H. et al. "Onion : Nature Protection Against Physiological Threats Onion : Nature
Protection Against". Food Sci. Nutr. 8398, (2015).
7.
Hakamata, W. et al. "A Simple Synthesis of Alliin and allo -Alliin: X-ray Diffraction
Analysis and Determination of Their Absolute Configurations". J. Agric. Food Chem. 63,
10778–10784 (2015).
8.
Pratt, D. A. "Garlic and Other Alliums. The Lore and the Science. By Eric Block.".
Angewandte Chemie International Edition vol. 49 7162–7162 (2010).
9.
Krest, I., Glodek, J. and Keusgen, M. "Cysteine Sulfoxides and Alliinase Activity of Some
Allium Species". J. Agric. Food Chem. (2000).
10.
He, Q., Kubec, R., Jadhav, A. P. and Musah, R. A. "First insights into the mode of action of a
‘lachrymatory factor synthase’ - Implications for the mechanism of lachrymator formation in
Petiveria alliacea, Allium cepa and Nectaroscordum species". Phytochemistry 72, 1939–1946
(2011).
11.
Kris-etherton, P. M. et al. "Bioactive Compounds in Foods : Their Role in the Prevention of
Cardiovascular Disease and Cancer ASSOCIATION BETWEEN FOOD AND". Am. J. Med.
9343, (2002).
12.
Revard, H. U. B. and Oulain, D. A. J. "Identification of New , Odor-Active Thiocarbamates
in Cress Extracts and Structure − Activity Studies on Synthesized Homologues". J. Agric.
Food Chem. 1932–1938 (2007) doi:10.1021/jf062856e.
13.
Naithani, R. et al. "Antiviral activity of phytochemicals: a comprehensive review". Mini Rev.
Med. Chem. 8, 1106–1133 (2008).
14.
Bones, A. M. and John, T. "The myrosinase-glucosinolate system , its organisation and
biochemistry". Physiol. Plant. 194–208 (1996).
15.
Ishida, M., Hara, M., Fukino, N., Kakizaki, T. and Morimitsu, Y. "Glucosinolate
104
metabolism , functionality and breeding for the improvement of Brassicaceae vegetables".
Breed. Sci. 59, 48–59 (2014).
16.
Vanduchova, A., Anzenbacher, P. and Anzenbacherova, E. "Isothiocyanate from Broccoli,
Sulforaphane, and Its Properties". J. Med. Food 22, 121–126 (2019).
17.
Borlinghaus, J., Albrecht, F., Gruhlke, M., Nwachukwu, I. and Slusarenko, A. "Allicin:
Chemistry and Biological Properties". Molecules 19, 12591–12618 (2014).
18.
Nicastro, H. L., Ross, S. A. and Milner, J. A. "Garlic and onions : Their cancer prevention
properties". Cancer Prev. Res. 8, 181–189 (2016).
19.
Blažević, I. et al. "Phytochemistry Glucosinolate structural diversity , identification ,
chemical synthesis and metabolism in plants". Phytochemistry 169, 112100 (2020).
20.
Sønderby, I. E., Geu-flores, F. and Halkier, B. A. "Biosynthesis of glucosinolates – gene
discovery and beyond". Trends Plant Sci. 283–290 (2010) doi:10.1016/j.tplants.2010.02.005.
21.
Block, E. "The Organosulfur Chemistry of the Genus Allium – Implications for the Organic
Chemistry of Sulfur". Angew. Chemie Int. Ed. English 31, 1135–1178 (1992).
22.
Yoshimoto, N., Saito, K. and Kopriva, S. "S-Alk(en)ylcysteine sulfoxides in the genus
Allium: Proposed biosynthesis, chemical conversion, and bioactivities". J. Exp. Bot. 70,
4123–4137 (2019).
23.
Yoshimoto, N. et al. "Garlic γ-glutamyl transpeptidases that catalyze deglutamylation of
biosynthetic intermediate of alliin". Front. Plant Sci. 5, 1–11 (2015).
24.
Maccelli, A. et al. "Metabolic profiling of different wild and cultivated Allium species based
on high-resolution mass spectrometry , high- performance liquid chromatographyphotodiode array detector , and color analysis". J. Mass Spectrom. 1–12 (2020)
doi:10.1002/jms.4525.
25.
Dopson, M. and Johnson, D. B. "Biodiversity , metabolism and applications of acidophilic
sulfur-metabolizing microorganisms". Environ. Microbiol. 14, 2620–2631 (2012).
26.
Robertson, L. A. and Kuenen, J. G. "Sulfur Production by Obligately Chemolithoautotrophic
Thiobacillus Species Sulfur Production by Obligately Chemolithoautotrophic Thiobacillus
Species". Appl. Environ. Microbiol. (1997) doi:10.1128/AEM.63.6.2300-2305.1997.
27.
Brierley, J. A. "A perspective on developments in biohydrometallurgy". Hydrometallurgy 94,
2–7 (2011).
28.
Brock, T. D., Brock, K. M., Belly, R. T. and Weiss, R. L. "Sulfolobus : A New Genus of
Sulfur-Oxidizing Bacteria Living at Low pH and High Temperature". Arch. Microbiol. 68,
54–68 (1972).
29.
Wächtershäuser, G. "Before Enzymes and Templates: Theory of Surface Metabolism".
Microbiol. Rev. 52, 452–484 (1988).
30.
Wächtershäuser, G. "Evolution of the first metabolic cycles". Proc. Natl. Acad. Sci. U. S. A.
105
87, 200–204 (1990).
31.
Wächtershäuser, G. "Life in a ligand sphere". Proc. Natl. Acad. Sci. U. S. A. 91, 4283–4287
(1994).
32.
Jez, J. M. "Structural biology of plant sulfur metabolism : from sulfate to glutathione". J.
Exp. Bot. 70, 4089–4103 (2019).
33.
Linder, T. "Assimilation of alternative sulfur sources in fungi". World J. Microbiol.
Biotechnol. 34, 1–7 (2018).
34.
Jørgensen, B. B., Findlay, A. J. and Pellerin, A. "The Biogeochemical Sulfur Cycle of
Marine Sediments". Front. Microbiol. 10, 1–27 (2019).
35.
Kletzin, A., Urich, T., Fabian, M., Bandeiras, T. M. and Gomes, M. "Dissimilatory Oxidation
and Reduction of Elemental Sulfur in Thermophilic Archaea". J. Bioenerg. Biomembr. 36,
(2004).
36.
Yamamoto, M. and Takai, K. "Sulfur metabolisms in epsilon- and gamma- Proteobacteria in
deep-sea hydrothermal fields". Front. Microbiol. 2, 1–8 (2011).
37.
Takeuchi, K. and Hirowatari, K. "Production of H2SO4 in Bioreactor at Geothermal Power
Station". J. Geotherm. Res. Soc. Japan 21, 353–358 (1999).
38.
Dopson, M., Lindstro, R. J. E. and Bo, E. "Potential Role of Thiobacillus caldus in
Arsenopyrite Bioleaching". Appl. Environ. Microbiol. 65, 36–40 (1999).
39.
Rawlings, D. E. and Johnson, D. B. "The microbiology of biomining : development and
optimization of mineral-oxidizing microbial consortia". Microbiology 315–324 (2007)
doi:10.1099/mic.0.2006/001206-0.
40.
Imai, S. et al. "An onion enzyme that makes the eyes water". Nature 419, 685 (2002).
41.
Yoshimoto, N. et al. "Identification of a flavin-containing S-oxygenating monooxygenase
involved in alliin biosynthesis in garlic". Plant J. 83, 941–951 (2015).
42.
Valentino, H. et al. "Structure and function of a flavin-dependent S-monooxygenase from
garlic ( Allium sativum )". J. Biol. Chem. (2020) doi:10.1074/jbc.RA120.014484.
43.
Brodnitz, M. H. and Pascale, J. V. "Thiopropanal S-Oxide: A Lachrymatory Factor in
Onions". J. Agric. Food Chem. 19, 269–272 (1971).
44.
Block, E. et al. "Allium chemistry: Microwave spectroscopic identification, mechanism of
formation, synthesis, and reactions of (E,Z)-propanethial S-oxide, the lachrymatory factor of
the onion (Allium cepa)". J. Am. Chem. Soc. 118, 7492–7501 (1996).
45.
Aoyagi, M. et al. "Structure and Bioactivity of Thiosulfinates Resulting from Suppression of
Lachrymatory Factor Synthase in Onion". J. Agric. Food Chem. 10893–10900 (2011)
doi:10.1021/jf202446q.
46.
Gupta, V. and Carroll, K. S. "Sulfenic acid chemistry, detection and cellular lifetime".
Biochim. Biophys. Acta - Gen. Subj. 1840, 847–875 (2014).
106
47.
Yang, J., Gupta, V., Carroll, K. S. and Liebler, D. C. "Site-specific mapping and
quantification of protein S-sulphenylation in cells". Nat. Commun. 2–13 (2014)
doi:10.1038/ncomms5776.
48.
Yeh, J. I., Claiborne, A. and Hol, W. G. J. "Structure of the Native Cysteine-Sulfenic Acid
Redox Center of Enterococcal NADH Peroxidase Refined at 2.8 Å Resolution".
Biochemistry 2960, 9951–9957 (1996).
49.
Arakawa, T. et al. "Structure of Thiocyanate Hydrolase : A New Nitrile Hydratase Family
Protein with a Novel Five-coordinate Cobalt ( III ) Center". J. Mol. Biol. 1497–1509 (2007)
doi:10.1016/j.jmb.2006.12.011.
50.
Yoshimura, T. et al. "Synthesis of a stable sulfenic acid, trans-decalin-9-sulfenic acid". J.
Chem. Soc. Chem. Commun. 1337–1338 (1992).
51.
Masamura, N., Aoyagi, M., Tsuge, N., Kamoi, T. and Imai, S. "Proton transfer in a reaction
catalyzed by onion lachrymatory factor synthase". Biosci. Biotechnol. Biochem. 76, 1799–
1801 (2012).
52.
Arakawa, T. et al. "Structure of Allium lachrymatory factor synthase elucidates catalysis on
sulfenic acid substrate". bioRxiv (2017).
53.
佐藤優太. "催涙因子合成酵素の構造・機能解析(修士論文)". (2018).
54.
Dawson, R. M. C., Elliott, D. C., Elliott, W. H. and Jones, K. M. Data for Biochemical
Research (3rd ed.). (1986).
55.
Okuyama, T. et al. "Equilibrium and Kinetic Studies of Reactions of 2-Methyl-2propanesulfenic Acid". Heteroat. Chem. 3, 577–583 (1992).
56.
Gutteridge, A. and Thornton, J. M. "Understanding nature ’ s catalytic toolkit". TRENDS
Biochem. Sci. 30, (2005).
57.
Golczak, M. "Enzyme That Makes You Cry − Crystal Structure of Lachrymatory Factor
Synthase from Allium cepa". ACS Chem. Biol. (2017) doi:10.1021/acschembio.7b00336.
58.
Laemmli, U. K. "Cleavage of Structura l Proteins during the Assembly of the Head of
Bacteriop hage T4". Nature 227, 680–685 (1970).
59.
高辺潤平. "催涙因子合成酵素の結晶化及び構造解析(修士論文)". (2015).
60.
OTWINOWSKI, Z. and WLADEK, M. "Processing of X-Ray Diffraction Data Collected in
Oscillation Mode". Method Enzymol. 276, 306–315 (1997).
61.
Kabsch, W. "XDS". Acta Crystallogr. Sect. D Biol. Crystallogr. 125–132 (2010)
doi:10.1107/S0907444909047337.
62.
Winn, M. D. et al. "Overview of the CCP 4 suite and current developments". Acta
Crystallogr. Sect. D Biol. Crystallogr. 4449, 235–242 (2011).
63.
Evans, P. R. and Garib, N. "How good are my data and what is the resolution ?". Acta
Crystallogr. Sect. D Biol. Crystallogr. 1204–1214 (2013) doi:10.1107/S0907444913000061.
107
64.
Vagin, A. and Teplyakov, A. "Molecular replacement with MOLREP". Acta Crystallogr.
Sect. F 364–366 (2012).
65.
Emsley, P., Lohkamp, B., Scott, W. G. and Cowtan, K. "Features and development of Coot".
Acta Crystallogr. Sect. D Biol. Crystallogr. 66, 486–501 (2010).
66.
Murshudov, G. N. and Nicholls, R. A. "REFMAC 5 for the refinement of macromolecular
crystal structures". Acta Crystallogr. Sect. D Biol. Crystallogr. 355–367 (2011)
doi:10.1107/S0907444911001314.
67.
Potterton, E., Briggs, P., Turkenburg, M. and Dodson, E. "A graphical user interface to the
CCP 4 program suite". Acta Crystallogr. Sect. D Biol. Crystallogr. 1131–1137 (2003)
doi:10.1107/S0907444903008126.
68.
Frisch, M. J. et al. "Gaussian 16 Revision A.03". (2016).
69.
Jorgensen, W. L., Chandrasekhar, J., Madura, J. D., Impey, R. W. and Klein, M. L.
"Comparison of simple potential functions for simulating liquid water". J. Chem. Phys. 926,
(2016).
70.
Case, D. A. et al. "The Amber Biomolecular Simulation Programs". J. Comput. Chem.
12255, (2005).
71.
Simmerling, C. "ff14SB: Improving the Accuracy of Protein Side Chain and Backbone
Parameters from ff 99SB". J. Chem. Theory Comput. (2015) doi:10.1021/acs.jctc.5b00255.
72.
Wang, J., Wang, W., Kollman, P. A. and Case, D. A. "Automatic atom type and bond type
perception in molecular mechanical calculations". J. Mol. Graph. Model. 25, 247–260
(2006).
73.
Wang, J., Wolf, R. M., Caldwell, J. W., Kollman, P. A. and Case, D. A. "Development and
Testing of a General Amber Force Field". J. Comput. Chem. 56531, (2004).
74.
Stephens, P. J., Devlin, F. J., Chabalowski, C. F. and Frisch, M. J. "Ab Initio Calculation of
Vibrational Absorption and Circular Dichroism Spectra Using Density Functional Force
Fields". J. Phys. Chem. 98, 11623–11627 (1994).
75.
Hehre, W. J., Ditchfield, R. and Pople, J. A. "Self — Consistent Molecular Orbital Methods .
XII . Further Extensions of Gaussian — Type Basis Sets for Use in Molecular Orbital
Studies of Organic Molecules". J. Chem. Phys. 6796, (2003).
76.
Fischer, C. F. "GENERAL HARTREE-FOCK PROGRAM". Comput. Phys. Commun. 43,
(1987).
77.
Bayly, C. I., Cieplak, P., Wendy, D. and Kollman, P. A. "A Well-Behaved Electrostatic
Potential Based Method Using Charge Restraints for Deriving Atomic Charges: The RESP
Model". J. Phys. Chem. 10269–10280 (1993) doi:10.1021/j100142a004.
78.
Darden, T., York, D. and Pedersen, L. "Particle mesh Ewald : An N ⋅ log ( N ) method for
Ewald sums in large systems in large systems". J. Chem. Phys. 10089, 1–5 (2010).
108
79.
Bussi, G., Donadio, D. and Parrinello, M. "Canonical sampling through velocity rescaling
Canonical sampling through velocity rescaling". J. Chem. Phys. 014101, (2007).
80.
Parrinello, M. and Rahman, A. "Polymorphic transitions in single crystals : A new molecular
dynamics method". J. Appl. Phys. 7182, (2010).
81.
Maseras, F. and Morokuma, K. "IMOMM : A New Integrated Ab Initio + Molecular
Mechanics Geometry Optimization Scheme of Equilibrium Structures and Transition States".
J. Comput. Chem. 16, (1995).
82.
Becke, A. D. "Denstry-Function Themochemistry. II . The effect of the Perdew – Wang
generalized-gradient correlation correction". J. Chem. Phys. 9173, (1998).
83.
Lee, C., Yang, W. and Parr, R. G. "Development of the Colle-Salvetti correlation-energy
formula into a functional of the electron density". Phys. Rev. B 37, (1988).
84.
Vreven, T. et al. "Combining Quantum Mechanics Methods with Molecular Mechanics
Methods in ONIOM". J. Chem. Theory Comput. 815–826 (2006) doi:10.1021/ct050289g.
85.
Svensson, M., Froese, R. D. J., Matsubara, T., Sieber, S. and Morokuma, K. "ONIOM: A
Multilayered Integrated MO + MM Method for Geometry Optimizations and Single Point
Energy Predictions. A Test for Diels - Alder Reactions and Pt(P( t -Bu) 3 ) 2 + H 2 Oxidative
Addition". J. Phys. Chem. 3654, 19357–19363 (1996).
86.
Field, M. J., Bash, P. A. and Karplus, M. "A Combined Quantum Mechanical and Molecular
Mechanical Potential for Molecular Dynamics Simulations". J. Comput. Chem. 11, 700–733
(1990).
87.
Foster, J. P. and Weinhold, F. "Natural hybrid orbitals". Jounal Am. Chem. Soc. 4, 7211–
7218 (1980).
88.
Adams, P. D. et al. "PHENIX: Building new software for automated crystallographic
structure determination". Acta Crystallogr. Sect. D Biol. Crystallogr. 58, 1948–1954 (2002).
89.
Liebschner, D. et al. "Polder maps : improving OMIT maps by excluding bulk solvent". Acta
Crystallogr. Sect. D Struct. Biol. 148–157 (2017) doi:10.1107/S2059798316018210.
90.
Yin, P. et al. "Structural insights into the mechanism of abscisic acid signaling by PYL
proteins". Nat. Struct. Mol. Biol. 16, 1230–1236 (2009).
91.
Zhang, X. et al. "Structural Insights into the Abscisic Acid Stereospecificity by the ABA
Receptors PYR/PYL/RCAR". PLoS One 8, (2013).
92.
Hibi, M. et al. "Enzymatic synthesis of chiral amino acid sulfoxides by Fe(II)/αketoglutarate-dependent dioxygenase". Tetrahedron Asymmetry 24, 990–994 (2013).
93.
Li, C., Jing, H., Ma, G. and Liang, P. "Allicin induces apoptosis through activation of both
intrinsic and extrinsic pathways in glioma cells". Mol. Med. Rep. 5976–5981 (2018)
doi:10.3892/mmr.2018.8552.
94.
Ossama, M., Hathout, R. M., Attia, D. A. and Mortada, N. D. "Enhanced Allicin Cytotoxicity
109
on HEPG - 2 Cells Using Glycyrrhetinic Acid Surface-Decorated Gelatin Nanoparticles".
ACS Omega (2019) doi:10.1021/acsomega.9b01580.
95.
Motohashi, K. "A simple and efficient seamless DNA cloning method using SLiCE from
Escherichia coli laboratory strains and its application to SLiP site-directed mutagenesis".
BMC Biotechnol. (2015) doi:10.1186/s12896-015-0162-8.
96.
Kubitza, C., Faust, A., Gutt, M. and Ga, L. "Crystal structure of pyrrolizidine alkaloid N oxygenase from the grasshopper Zonocerus variegatus research papers". Acta Crystallogr.
Sect. D Struct. Biol. 422–432 (2018) doi:10.1107/S2059798318003510.
97.
Cowtan, K. "The Buccaneer software for automated model building . 1 . Tracing protein
chains". Acta Crystallogr. Sect. D Biol. Crystallogr. 1002–1011 (2006)
doi:10.1107/S0907444906022116.
98.
Perrakis, A., Harkiolaki, M., Wilson, K. S. and Lamzin, V. S. "ARP / wARP and molecular
replacement". Acta Crystallogr. Sect. D Biol. Crystallogr. 1445–1450 (2001)
doi:10.1107/S0907444901014007.
99.
Holm, L. and Rosenström, P. "Dali server: Conservation mapping in 3D". Nucleic Acids Res.
38, 545–549 (2010).
100.
Bonanno, J. B. et al. "Mechanism of action of a flavin- containing monooxygenase". Proc.
Natl. Acad. Sci. U. S. A. 104, (2007).
101.
Lon, N. et al. "Characterization of a thermostable flavin-containing monooxygenase from
Nitrincola lacisaponensis ( NiFMO )". Appl. Microbiol. Biotechnol. 1755–1764 (2019).
102.
Li, C. Y. et al. "Structural mechanism for bacterial oxidation of oceanic trimethylamine into
trimethylamine N-oxide". Mol. Microbiol. 103, 992–1003 (2017).
103.
Siddens, L. K., Krueger, S. K., Henderson, M. C. and Williams, D. E. "Mammalian flavincontaining monooxygenase (FMO) as a source of hydrogen peroxide". Biochem. Pharmacol.
89, 141–147 (2014).
104.
Moriwaki, Y. et al. "Understanding the Molecular Mechanism Underlying the High Catalytic
Activity of p - Hydroxybenzoate Hydroxylase Mutants for Producing Gallic Acid".
Biochemistry (2019) doi:10.1021/acs.biochem.9b00443.
105.
Nguyen, K. et al. "Characterization of the flavin monooxygenase involved in biosynthesis of
the antimalarial FR-900098". Org. Biomol. Chem. 17, 1506–1518 (2019).
106.
Luo, D., Smith, S. W. and Anderson, B. D. "Kinetics and Mechanism of the Reaction of
Cysteine and Hydrogen Peroxide in Aqueous Solution". J. Pharm. Sci. 94, 304–316 (2005).
107.
van Berkel, W. J. H., Kamerbeek, N. M. and Fraaije, M. W. "Flavoprotein monooxygenases,
a diverse class of oxidative biocatalysts". J. Biotechnol. 124, 670–689 (2006).
108.
Fraaije, M. W., Kamerbeek, N. M., Berkel, W. J. H. Van and Janssen, D. B. "Identification
of a Baeyer-Villiger monooxygenase sequence motif". FEBS Lett. 518, 43–47 (2002).
110
109.
Mishina, T. E. and Wuerzburg, D. "The Arabidopsis Flavin-Dependent Monooxygenase
FMO1 Is an Essential Component of Biologically Induced Systemic Acquired Resistance 1
[ OA ]". Plant Physiol. 141, 1666–1675 (2006).
110.
Zhao, Y. et al. "A Role for Flavin Monooxygenase – Like Enzymes in Auxin Biosynthesis".
Science (80-. ). 291, 306–310 (2001).
111.
Hansen, B. G., Kliebenstein, D. J. and Halkier, B. A. "Identification of a flavinmonooxygenase as the S-oxygenating enzyme in aliphatic glucosinolate biosynthesis in
Arabidopsis". Plant J. 902–910 (2007) doi:10.1111/j.1365-313X.2007.03101.x.
112.
Kumar, S., Stecher, G., Li, M., Knyaz, C. and Tamura, K. "MEGA X : Molecular
Evolutionary Genetics Analysis across Computing Platforms". Mol. Biol. Evol. 35, 1547–
1549 (2018).
113.
Nicoll, C. R. et al. "Ancestral-sequence reconstruction unveils the structural basis of function
in mammalian FMOs". Nat. Struct. Mol. Biol. 27, (2020).
114.
Catucci, G., Gao, C., Sadeghi, S. J. and Gilardi, G. "Chemical applications of Class B
flavoprotein monooxygenases". Rend. Lincei 28, 195–206 (2017).
115.
Bong, Y. K. et al. "Baeyer-Villiger Monooxygenase-Mediated Synthesis of Esomeprazole
As an Alternative for Kagan Sulfoxidation". J. Org. Chem. 83, 7453–7458 (2018).
116.
Masa, K., Hamada, A., Arimori, K., Fujii, J. and Nakano, M. "Pharmacokinetic differences
between lansoprazole enantiomers and contribution of cytochrome P450 isoforms to
enantioselective metabolism of lansoprazole in dogs". Biol. Pharm. Bull. 24, 274–277
(2001).
117.
Novotna, A. et al. "Differential effects of omeprazole and lansoprazole enantiomers on aryl
hydrocarbon receptor in human hepatocytes and cell lines". PLoS One 9, 1–8 (2014).
118.
Hamada, Y., Ikemura, K., Iwamoto, T. and Okuda, M. "Stereoselective Inhibition of Renal
Basolateral Human Organic Anion Transporter 3 by Lansoprazole Enantiomers".
Pharmacology 101, 176–183 (2018).
119.
Bordewick, S., Beier, A., Balke, K. and Bornscheuer, U. T. "Baeyer-Villiger
monooxygenases from Yarrowia lipolytica catalyze preferentially sulfoxidations". Enzyme
Microb. Technol. 109, 31–42 (2018).
120.
Matsui, T., Dekishima, Y. and Ueda, M. "Biotechnological production of chiral organic
sulfoxides : current state and perspectives". Appl. Microbiol. Biotechnol. 7699–7706 (2014)
doi:10.1007/s00253-014-5932-z.
121.
Zhang, Y. et al. "Discovery of two native Baeyer-Villiger monooxygenases for asymmetric
synthesis of bulky chiral sulfoxides". Appl. Environ. Microbiol. 84, 1–10 (2018).
122.
Kulikova, V. et al. "Non-stereoselective decomposition of (±)-S-alk(en)yl-L-cysteine
sulfoxides to antibacterial thiosulfinates catalyzed by C115H mutant methionine γ-lyase
111
from Citrobacter freundii". Biochimie 151, 42–44 (2018).
123.
Kletzin, A. "Coupled Enzymatic Production of Sulfite , Thiosulfate , and Hydrogen Sulfide
from Sulfur : Purification and Properties of a Sulfur Oxygenase Reductase from the
Facultatively Anaerobic Archaebacterium Desulfurolobus ambivalens". J. Bacteriol. 171,
1638–1643 (1989).
124.
Chen, Z., Jiang, C., She, Q., Liu, S. and Zhou, P. "Key Role of Cysteine Residues in
Catalysis and Subcellular Localization of Sulfur Oxygenase-Reductase of Acidianus
tengchongensis". Appl. Environ. Microbiol. 71, 621–628 (2005).
125.
Pelletier, N., Leroy, G., Guiral, M., Giudici-Orticoni, M.-T. and Aubert, C. "First
characterisation of the active oligomer form of sulfur oxygenase reductase from the
bacterium Aquifex aeolicus". Extremophiles 205–215 (2008) doi:10.1007/s00792-007-01195.
126.
Veith, A., Botelho, H. M., Kindinger, F., Gomes, C. M. and Kletzin, A. "The Sulfur
Oxygenase Reductase from the Mesophilic Bacterium Halothiobacillus neapolitanus Is a
Highly Active Thermozyme". J. Bacteriol. 677–685 (2012) doi:10.1128/JB.06531-11.
127.
Janosch, C., Remonsellez, F., Sand, W. and Vera, M. "Sulfur Oxygenase Reductase (Sor) in
the Moderately Thermoacidophilic Leaching Bacteria: Studies in Sulfobacillus
thermosulfidooxidans and Acidithiobacillus caldus". Microorganisms 707–724 (2015)
doi:10.3390/microorganisms3040707.
128.
Bacterium, H., Low, A. and Activity, R. "A Sulfur Oxygenase from the Haloalkaliphilic
Bacterium Thioalkalivibrio paradoxus with Atypically Low Reductase Activity". J.
Bacteriol. 199, 1–15 (2017).
129.
Grogant, D. W. "Phenotypic Characterization of the Archaebacterial Genus Sulfolobus :
Comparison of Five Wild-Type Strains". J. Bacteriol. 171, 6710–6719 (1989).
130.
Kurosawa, N. et al. "Sulfurisphaera ohwakuensis gen. nov., sp. nov., anovel extremely
thermophlic acidophile of the order Sulfolobus". Int. J. Syst. Bacteriol. 20, (1998).
131.
Suzuki, T. et al. "Sulfolobus tokodaii sp . nov . ( f . Sulfolobus sp . strain 7 ), a new member
of the genus Sulfolobus isolated from Beppu Hot Springs , Japan". Extremophiles 39–44
(2002).
132.
矢吹崇吏. "Sulfolobus tokodaii 由来の硫黄代謝関連酵素および脂肪酸代謝関連酵素に
関する研究(博士論文)". (東京大学, 2007).
133.
Glaeser, R. M., Typke, D., Tiemeijer, P. C., Pulokas, J. and Cheng, A. "Precise beam-tilt
alignment and collimation are required to minimize the phase error associated with coma in
high-resolution cryo-EM". J. Struct. Biol. 174, 1–10 (2011).
134.
Zheng, S. Q. et al. "MotionCor2 : anisotropic correction of beam-induced motion for
improved cryo-electron microscopy Automatic tracing of ultra-volumes of neuronal images".
112
Nat. Methods 14, 331–332 (2017).
135.
Rohou, A. and Grigorieff, N. "CTFFIND4 : Fast and accurate defocus estimation from
electron micrographs". J. Struct. Biol. 192, 216–221 (2015).
136.
Zhang, K. "Gctf : Real-time CTF determination and correction". J. Struct. Biol. 193, 1–12
(2016).
137.
Moriya, T. et al. "High-resolution Single Particle Analysis from Electron Cryo-microscopy
Images Using SPHIRE 1 . PROJECT : Set Constant Parameter Values for This Project 2 .
MOVIE : Align the Frames of Each Movie Micrograph to Correct the Overall Motion of the
Sample". J. Vis. Exp. 1–11 (2017) doi:10.3791/55448.
138.
Wagner, T. et al. "SPHIRE-crYOLO is a fast and accurate fully automated particle picker for
cryo-EM". Commun. Biol. 1–13 (2019) doi:10.1038/s42003-019-0437-z.
139.
Zivanov, J. et al. "New tools for automated high-resolution cryo-EM structure determination
in RELION-3". Elife 1–22 (2018).
140.
Goddard, T. D., Huang, C. C. and Ferrin, T. E. "Visualizing density maps with UCSF
Chimera". J. Struct. Biol. 157, 281–287 (2007).
141.
Tang, G. et al. "EMAN2 : An extensible image processing suite for electron microscopy". J.
Struct. Biol. 157, 38–46 (2007).
142.
Terwilliger, T. C., Adams, P. D., Afonine, P. V. and Sobolev, O. V. "A fully automatic
method yielding initial models from high-resolution cryo-electron microscopy maps". Nat.
Methods 15, 905–908 (2018).
143.
Adams, P. D. "Real-space refinement in PHENIX for cryo-EM and crystallography research
papers". Acta Crystallogr. Sect. D Struct. Biol. 531–544 (2018)
doi:10.1107/S2059798318006551.
144.
Williams, C. J. et al. "MolProbity: More and better reference data for improved all-atom
structure validation". Protein Sci. 27, 293–315 (2018).
145.
Barad, B. A. et al. "EMRinger : side chain – directed model and map validation for 3D cryoelectron microscopy". Nat. Methods 12, (2015).
146.
Pettersen, E. F. et al. "UCSF Chimera — A Visualization System for Exploratory Research
and Analysis". J. Comput. Chem. (2004) doi:10.1002/jcc.20084.
147.
Zheng, H. et al. "CheckMyMetal : a macromolecular metal-binding validation tool research
papers". Acta Crystallogr. Sect. D Struct. Biol. 223–233 (2017)
doi:10.1107/S2059798317001061.
148.
Urich, T., Gomes, C. M., Kletzin, A. and Frazao, C. "X-ray Structure of a SelfCompartmentalizing Sulfur Cycle Metalloenzyme". Science (80-. ). (2006).
149.
Li, M. et al. "Biochemical and Biophysical Research Communications Crystal structure
studies on sulfur oxygenase reductase from Acidianus tengchongensis". Biochem. Biophys.
113
Res. Commun. 369, 919–923 (2008).
150.
Hattne, J. et al. "Analysis of Global and Site-Specific Radiation Damage in Cryo-EM Article
Analysis of Global and Site-Specific Radiation Damage in Cryo-EM". Structure 26, 759766.e4 (2018).
151.
Zillig, W. et al. "Desulfurolobus ambivalens, gen. nov., sp. nov., an autotrophic
archaebacterium facultatively oxidizing or reducing sulfur". Syst. Appl. Microbiol. 8, 197–
203 (1986).
152.
Ghosh, W. and Dam, B. "Biochemistry and molecular biology of lithotrophic sulfur
oxidation by taxonomically and ecologically diverse bacteria and archaea". FEMS Microbiol.
Revews (2009) doi:10.1111/j.1574-6976.2009.00187.x.
153.
Aussignargues, C. et al. "Rhodanese Functions as Sulfur Supplier for Key Enzymes in Sulfur
Energy Metabolism". J. Biol. Chem. 287, 19936–19948 (2012).
154.
Maki, J. S. "Bacterial Intracellular Sulfur Globules : Structure and Function". J. Mol.
Microbiol. Biotechnol. 270–280 (2013) doi:10.1159/000351335.
155.
Veith, A. et al. "Substrate pathways and mechanisms of inhibition in the sulfur oxygenase
reductase of Acidianus ambivalens". Front. Microbiol. 2, 1–12 (2011).
156.
Ida, T. et al. "Reactive cysteine persulfides and S-polythiolation regulate oxidative stress and
redox signaling". Proc. Natl. Acad. Sci. U. S. A. (2014) doi:10.1073/pnas.1321232111.
157.
Dóka, É. et al. "A novel persulfide detection method reveals protein persulfide- and
polysulfide-reducing functions of thioredoxin and glutathione systems". Sci. Adv. 1–15
(2016).
158.
Kunikata, H. et al. "Metabolomic profiling of reactive persulfides and polysulfides in the
aqueous and vitreous humors". Sci. Rep. 1–10 (2017) doi:10.1038/srep41984.
159.
Numakura, T. et al. "Production of reactive persulfide species in chronic obstructive
pulmonary disease". Thorax 1074–1083 (2017) doi:10.1136/thoraxjnl-2016-209359.
160.
Maki-yonekura, S. et al. "Hexameric and pentameric complexes of the ExbBD energizer in
the Ton system". Elife 1–24 (2018).
161.
Kujirai, T. et al. "Structural basis of the nucleosome transition during RNA polymerase II
passage". Science (80-. ). 598, 595–598 (2018).
162.
Wu, M., Lander, G. C. and Herzik Jr., M. A. "Sub-2 Angstrom resolution structure
determination using single-particle cryo-EM at 200 keV". J. Struct. Biol. X 4, 100020 (2020).
163.
Feathers, J. R., Spoth, K. A. and Fromme, J. C. "Surpassing the physical Nyquist limit to
produce super-resolution cryo-EM reconstructions". bioRxiv (2019).
114
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