アイキャッチ

LIST OF PUBLICATIONS

Original paper (2021~)

  • "Crystal structural analysis of aldoxime dehydratase from Bacillus sp. OxB-1: Importance of surface residues in optimization for crystallization"
    D. Matsui, N. Muraki, K. Chen, T. Mori, A. A. Ingram, K. Oike, H. Gröger, S. Aono, and Y. Asano
    Journal of Inorganic Biochemistry, 230, (2022)

  • "Heme controls the structural rearrangement of its sensor protein mediating the hemolytic bacterial survival."
    M. Nishinaga, H. Sugimoto, Y. Nishitani, S. Nagai, S. Nagatoishi, N. Muraki, T. Tosha, K. Tsumoto, S. Aono, Y. Shiro and H. Sawai
    Communications Biology, 4, Article number: 467, (2021)
    プレスリリースはこちらです。

  • "Use of a Ferritin L134P Mutant for the Facile Conjugation of Prussian Blue in the Apoferritin Cavity"
    Y. Ikenoue, Y. O. Tahara, M. Miyata, T. Nishioka, S. Aono, and H. Nakajima
    Inorg. Chem., 60, 7, 4693–4704, (2021)

  • "Structructural Characterization of Y29F Mutant of Thermoglobin from a Hyperthermophilic Bacterium Aquifex aeolicus."
    N. Muraki, K. Takeda, D. Nam, M. Muraki, S. Aono
    Chemistry Letters, 50(4), 603–606 (2021)

    Original paper (2011~2020)

  • "Structural basis for the heme transfer reaction in heme uptake machinery from Corynebacteria."
    N. Muraki, C. Kitatsuji, Y. Okamoto, T. Uchida, K. Ishimori, S. Aono
    Chemical Communication (Cambridge), 14, 13864-13867 (2019)
    プレスリリースはこちらです。

  • "Structural characterization of HypX responsible for CO biosynthesis in the maturation of NiFe-hydrogenase."
    N. Muraki, K. Ishii, S. Uchiyama, S. G. Itoh, H. Okumura, S. Aono,
    Communications Biology, 2, 385 (2019)
    プレスリリースはこちらです。

  • "Protein Dynamics of the Sensor Protein HemAT as Probed by Time-Resolved Step-Scan FTIR Spectroscopy."
    A. Pavlou, H. Yoshimura, S. Aono, E. Pinakoulaki,
    Biophys J., 114 (2018)

  • "Probing the Role of the Heme Distal and Proximal Environment in Ligand Dynamics in the Signal Transducer Protein HemAT by Time-Resolved Step-Scan FTIR and Resonance Raman Spectroscopy."
    A. Pavlou, A. Loullis, H. Yoshimura, S. Aono, E. Pinakoulaki,
    Biochemistry., 56 (2017)

  • "Structural Characterization of Heme Environmental Mutants of CgHmuT that Shuttles Heme Molecules to Heme Transporters."
    N. Muraki, C. Kitatsuji, M. Ogura, T. Uchida, K. Ishimori, S. Aono,
    Int J Mol Sci. 17 (2016)

  • "A Study of the Dynamics of the Heme Pocket and C-helix in CooA upon CO Dissociation Using Time-Resolved Visible and UV Resonance Raman Spectroscopy."
    A. Otomo, H. Ishikawa, M. Mizuno, T. Kimura, M. Kubo, Y. Shiro, S. Aono, Y. Mizutani,
    J Phys Chem B., 120 (2016)

  • "Structural Basis for Heme Recognition by HmuT Responsible for Heme Transport to the Heme Transporter in Corynebacterium glutamicum"
    N. Muraki, S. Aono,
    Chem. Lett., 45, 24-26 (2015).

  • "A new biological function of heme as a signaling molecule"
    N. Muraki, C. Kitatsuji, S. Aono,
    J. Porphyrins & Phthalocyanines., 19, 9-20 (2015).

  • "Heme-binding properties of HupD functioning as a substrate-binding protein in a heme-uptake ABC-transporter system in Listeria monocytogenes"
    Y. Okamoto, H. Sawai, M. Ogura, T. Uchida, K. Ishimori, T. Hayashi, S. Aono,
    Bull. Chem. Soc. Jpn., 87, 1140-1146 (2014).

  • "Molecular mechanism for heme-mediated inhibition of 5-aminolevulinic acid synthase 1"
    C. Kitatsuji, M. Ogura, T. Uchida, K. Ishimori, S. Aono,
    Bull. Chem. Soc. Jpn., 87, 997-1004 (2014).

  • "The Dos family of globin-related sensors using PAS domains to accommodate haem acting as the active site for sensing external signals"
    S. Aono,
    Adv. Microbial Physiol., 63, 273-327 (2013).

  • "Structural basis for the transcriptional regulation of heme homeostasis in Lactococcus lactis"
    H. Sawai, M. Yamanaka, H. Sugimoto, Y. Shiro, S. Aono,
    J. Biol. Chem., 287, 30755-30768 (2012).

    Original Paper (2001~2010)

  • "The role of the Fe-S cluster in the sensory domain of nitrogenase transcriptional activator VnfA from Azotobacter vinelandii."
    H. Nakajima, N. Takatani, K. Yoshimitsu, M. Itoh, S. Aono, Y. Takahashi, Y. Watanabe
    FEBS J., 2010, 277, 817-832

  • "Molecular oxygen regulates the enzymatic activity of a heme-containing diguanylate cyclase (HemDGC) for the synthesis of cyclic di-GMP."
    H. Sawai, S. Yoshioka, T. Uchida, M. Hyodo, Y. Hayakawa, K. Ishimori, S. Aono
    Biochim. Biophys. Acta, 2010, 1804, 166-172

  • "X-ray crystal structure of michaelis complex of aldoxime dehydratase."
    H. Sawai, H. Sugimoto, Y. Kato, Y. Asano, Y. Shiro, S. Aono
    J. Biol. Chem., 2009, 284, 32089-32096 [Papers of the week]

  • "Metal-containing sensor proteins sensing diatomic gas molecules."
    S. Aono
    Dalton Trans., 2008, 28, 3137-3146

  • "Protein conformation changes of HemAT-Bs upon ligand binding probed by ultraviolet resonance Raman spectroscopy."
    S. F. EI-Mashtoly, Y. Gu, H. Yoshimura, S. Yoshioka, S. Aono, T. Kitagawa
    J. Biol. Chem., 2008, 283, 6942-6949

  • "The formation of hydrogen bond in the proximal heme pocket of HemAT-Bs upon ligand binding."
    H. Yoshimura, S. Yoshioka, Y. Mizutani, S. Aono
    Biochem. Biophys. Res. Commun., 2007, 357, 1053-1057

  • "Crystal structure of CO-sensing transcription activator CooA bound to exogenous ligand imidazole."
    H. Komori, S. Inagaki, S. Yoshioka, S. Aono, Y. Higuchi
    J. Mol. Biol., 2007, 367, 864-871

  • "Systematic regulation of the enzymatic activity of phenylacetaldoxime dehydratase by exogenous ligands."
    K. Kobayashi, M. Kubo, S. Yoshioka, T. Kitagawa, Y. Kato, Y. Asano, S. Aono
    Chem. Bio. Chem., 2006, 7, 2004-2009

  • "Two ligand-binding sites in the O2-sensing signal transducer HemAT: implications for ligand recognition/discrimination and signaling."
    E. Pinakoulaki, H. Yoshimura, V. Daskalakis, S. Yoshioka, S. Aono, C. Varotsis
    Proc. Natl. Acad. Sci. U. S. A., 2006, 103, 14796-14801

  • "Effect of mutation on the dissociation and recombination dynamics of CO in transcriptional regulator CooA: a picosecond infrared transient absorption study."
    T. Zhang, IV. Rubtsov, H. Nakajima, S. Aono, K. Yoshihara
    Biochemistry, 2006, 45, 9246-9253

  • "Specific hydrogen-bonding networks responsible for selective O2 sensing of the oxygen sensor protein HemAT from Bacillus subtilis."
    H. Yoshimura, S. Yoshioka, K. Kobayashi, T. Ohta, T. Uchida, M. Kubo, T. Kitagawa, S. Aono
    Biochemistry, 2006, 45, 8301-8307

  • "Recognition and discrimination of gases by the oxygen-sensing signal transducer protein HemAT as revealed by FTIR spectroscopy."
    E. Pinakoulaki, H. Yoshimura, S. Yoshioka, S. Aono, C. Varotsis
    Biochemistry, 2006, 45, 7763-7766

  • "Crystallization and preliminary X-ray analysis of CooA from Carboxydothermus hydrogenoformans."
    H. Komori, K. Satomoto, Y. Ueda, N. Shibata, S. Inagaki, S. Yoshioka, S. Aono, Y. Higuchi
    Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun., 2006, 62, 471-473

  • "Evidence for displacements of the C-helix by CO ligation and DNA binding to CooA revealed by UV resonance Raman spectroscopy."
    M. Kubo, S. Inagaki, S. Yoshioka, T. Uchida, Y. Mizutani, S. Aono, T. Kitagawa
    J. Biol. Chem., 2006, 281, 11271-11278

  • "Spectroscopic and substrate binding properties of heme-containing aldoxime dehydratases, OxdB and OxdRE."
    K. Kobayashi, B. Pal, S. Yoshioka, Y. Kato, Y. Asano, T. Kitagawa, S. Aono
    J. Inorg. Biochem., 2006, 100, 1069-1074

  • "Biophysical properties of a c-type heme in chemotaxis signal transducer protein DcrA."
    S. Yoshioka, K. Kobayashi, H. Yoshimura, T. Uchida, T. Kitagawa, S. Aono
    Biochemistry, 2005, 44, 15406-15413

  • "Regulation of aldoxime dehydratase activity by redox-dependent change in the coordination structure of the aldoxime-heme complex"
    K. Kobayashi, S. Yoshioka, Y. Kato, Y. Asano, S. Aono
    J. Biol. Chem., 2005, 280, 5486-5490

  • "Spectroscopic and redox propertiesof a CooA homologue from Carboxydothermus hydrogenoformans"
    S. Inagaki, C. Masuda, T. Akaishi, H. Nakajima, S. Yoshioka, T. Ohta, T. Kitagawa, S. Aono
    J. Biol. Chem., 2005, 280, 3269-3274

  • "Oxygen sensing mechanism of HemAT from B.subtilis: A resonance Raman spectroscopic study"
    T. Ohta, H. Yoshimura, S. Yoshioka, S. Aono, T. Kitagawa
    J. Am. Chem. Soc., 2004, 126, 15000-15001

  • "Activation mechanisms of transcriptinal regulator CooA revealed by small-angle X-ray scattering"
    S. Akiyama, T. Fujisawa, K. Ishimori, I. Morishima, S. Aono
    J. Mol. Biol., 2004, 341, 651-668

  • "Resonance Raman and ligand binding analysis of the oxygen-sensing signal transducer protein HemAT from Bacillus subtilis"
    S. Aono, H. Nakajima, T. Ohta, T. Kitagawa
    Methods in Enzymology, 2003, 381, 618-628

  • "Biochemical and biophysicalproperties ofthe CO-sensing transcriptional activator CooA"
    S. Aono
    Acc. Chem. Res., 2003, 36, 825-831

  • "Characterization of the heme environmental structure of cytoglobin, a fourth globin in humans"
    H. Sawai, N. Kawada, K. Yoshizato, H. Nakajima, S. Aono, Y. Shiro
    Biochemistry, 2003, 42, 5133-5142

  • "Resonance Raman and ligand binding studies of the oxygen sensing signal transducer protein HemAT from Bacillus subtilis"
    S. Aono, T. Kato, M. Matsuki, H. Nakajima, T. Ohta, T. Uchida, T. Kitagawa
    J. Biol. Chem., 2002, 227, 13528-13538

  • "Conformational dynamics of transcriptional regulator CooA protein studied by subpicosecond mid-infrared vibrational spectroscopy" 
    I. V. Rubtsov, T. Zhang, H. Nakajima, S. Aono, G. I. Rubtsov, S. Kumazaki, K. Yoshihara
    J. Am. Chem. Soc., 2001, 123, 10056-10062

  • "Ligand-switching intermediates for the CO-sensing transcriptional activator CooA measured by pulse radiolysis"
    H. Nakajima, E. Nakagawa, K. Kobayashi, S. Tagawa, S. Aono
    J. Biol. Chem., 2001, 276, 37895-37899

  • "Binding of CO at the Pro2 side is crucial for the activation of CO-sensing transcriptional activator CooA. 1H NMR spectroscopic studies"
    K. Yamamoto, H. Ishikawa, S. Takahashi, K. Ishimori, I. Morishima, H. Nakajima, S. Aono 
    J. Biol. Chem., 2001, 276, 11473-11476

  • "Redox properties and coordination structure of the heme in the CO-sensing transcriptional activator, CooA"
    H. Nakajima, Y. Honma, T. Tawara, T. Kato, S.-Y. Park, H. Miyatake, Y. Shiro, S. Aono 
    J. Biol. Chem., 2001, 276, 7055-7061

    Original Paper (~2000)

  • "Dissociation and recombination between ligands and heme in a CO-sensing transcriptional activator CooA. A flash photolysis study"
    S. Kumazaki, H. Nakajima, T. Sakaguchi, E. Nakagawa, H. Shinohara, K. Yoshihara, S. Aono
    J.Biol. Chem., 2000, 275, 38378-38383

  • "Identification of histidine 77 as the axial heme ligand of carbonmonoxy CooA by picosecond time-resolved resonance Raman spectroscopy"
    T. Uchida, H. Ishikawa, K. Ishimori, I. Morishima, H. Nakajima, S. Aono, Y. Mizutani, T. Kitagawa
    Biochemistry, 2000, 39, 12747-12752

  • "CO sensing and regulation of gene expression by the transcriptional activator CooA"
    S.Aono, Y. Honma, K. Ohkubo, T. Tawara, T. Kamiya, H. Nakajima
    J.Inorg. Biochem., 2000, 82, 51-56

  • "Transcriptional regulation of gene expression by metalloproteins" 
    S. Aono, H. Nakajima
    Progress in Reaction Kinetics and Mechanism, 2000, 25, 65-107

  • "Control of CooA activity by the mutation at the C-terminal end of the heme-binding domain" 
    H. Nakajima, T. Matsuo, T. Tawara, S. Aono
    J. Inorg. Biochem., 2000, 78, 63-68

  • "Redox properties of the heme in the CO-sensing transcriptional activator CooA: Electrochemical evidence of the redox-controlled ligand exchange of the heme"
    H. Nakajima, S. Aono
    Chem. Lett., 1999, 1233-1234

  • "Structure and function of CooA, a novel transcriptional regulator containing a b-type heme as a CO sensor" 
    S. Aono, H. Nakajima
    Coord. Chem. Rev., 1999, 190-192, 267-282

  • "Recognition of the target DNA and transcription activation by the CO-sensing transcriptional activator CooA" 
    S. Aono, H. Takasaki, H. Unno, T. Kamiya, H. Nakajima
    Biochem. Biophys. Res. Commun., 1999, 261, 270-275

  • "Solution structure of an artificial Fe8S8 ferredoxin : the D13C variant of Bacillusschlegelii Fe7S8 ferredoxin" 
    S. Aono, D. Bentrop, I. Bertini, G. Cosenza, C. Luchinat
    Eur. J. Biochem., 1998, 258, 502-514

  • "Redox-controlled ligand exchange of the heme in the CO-sensing transcriptional activator CooA" 
    S. Aono, K. Ohkubo, T. Matsuo, H. Nakajima
    J. Biol. Chem., 1998, 273, 25757-25764

  • "Heme environmental structure of CooA is modulated by the target DNA binding: Evidences from resonance Raman spectroscopy and CO rebinding kinetics"
    T. Uchida, H. Ishikawa, S. Takahashi, K. Ishimori, I. Morishima, K. Ohkubo, H. Nakajima, S. Aono
    J. Biol. Chem., 1998, 273, 19988-19992

  • "Solution structure of the oxidized Fe7S8 ferredoxin from the thermophilic bacterium Bacillus schlegelii by 1H NMR spectroscopy"
    S. Aono, D. Bentrop, I. Bertini, A. Donaire, C. Luchinat, Y. Niikura, and A. Rosato
    Biochemistry, 1998, 37, 9812-9826

  • "Site-directed mutagenesis of cysteine to serine in a superoxide responsive transcriptional regulator SoxR"
    S. Aono, H. Nakajima, K. Saito
    J. Mol. Catal., B: Enzymatic 1998, 4, 283-287

  • "Signal transduction in the transcriptional activator CooA containing a heme-based CO sensor: Isolation of a dominant positive mutant which is active as the transcriptional activator even in the absence of CO"
    S. Aono, T. Matsuo, T. Shimono, K. Ohkubo, H. Takasaki, H. Nakajima
    Biochem. Biophys. Res. Commun., 1997, 240, 783-786

  • "The D13C variant of Bacillus schlegelii 7Fe ferredoxin is an 8Fe ferredoxin as revealed by 1H-NMR spectroscopy"
    S. Aono, D. Bentrop, I. Bertini, C. Luchinat, R. Macinai
    FEBS Lett., 1997, 412, 501-505

  • "A novel heme protein that acts as a carbon monoxide-dependent transcriptional activator in Rhodospirillum rubrum"
    S. Aono, H. Nakajima, K. Saito, M. Okada
    Biochem. Biophys. Res. Commun., 1996, 228, 752-756

  • "H NMR studies of the Fe7S8 ferredoxin from Bacillus schlegelii: A further attempt to understand Fe3S4 clusters"
    S. Aono, I. Bertini, J. A. Cowan, C. Luchinat, A. Rosato, M. S. Viezzoli
    J. Biol. Inorg. Chem., 1996, 1, 523-528

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