메뉴 건너뛰기




Volumn 31, Issue , 2016, Pages 103-112

Fresh insight to functioning of selected enzymes of the nitrogen cycle

Author keywords

[No Author keywords available]

Indexed keywords

COPPER DERIVATIVE; NITRIC OXIDE REDUCTASE; NITRITE REDUCTASE; NITROGENASE; NITROUS OXIDE REDUCTASE; ENZYME; NITROGEN;

EID: 84959561566     PISSN: 13675931     EISSN: 18790402     Source Type: Journal    
DOI: 10.1016/j.cbpa.2016.02.009     Document Type: Review
Times cited : (14)

References (42)
  • 1
    • 84899531961 scopus 로고    scopus 로고
    • Biosynthesis of nitrogenase metalloclusters
    • Ribbe M.W., Hu Y., Hodgson K.O., Hedman B. Biosynthesis of nitrogenase metalloclusters. Chem Rev 2014, 114:4063-4080.
    • (2014) Chem Rev , vol.114 , pp. 4063-4080
    • Ribbe, M.W.1    Hu, Y.2    Hodgson, K.O.3    Hedman, B.4
  • 5
    • 77952559475 scopus 로고    scopus 로고
    • Conformational gating of electron transfer from the nitrogenase Fe protein to MoFe protein
    • Danyal K., Mayweather D., Dean D.R., Seedfeldt L.C., Hoffman B.M. Conformational gating of electron transfer from the nitrogenase Fe protein to MoFe protein. J Am Chem Soc 2010, 123:6894-6895.
    • (2010) J Am Chem Soc , vol.123 , pp. 6894-6895
    • Danyal, K.1    Mayweather, D.2    Dean, D.R.3    Seedfeldt, L.C.4    Hoffman, B.M.5
  • 6
    • 84921047445 scopus 로고    scopus 로고
    • Structural evidence for asymmetrical nucleotide interactions in nitrogenase
    • Tezcan F.A., Kaiser J.T., Howard J.B., Rees D.C. Structural evidence for asymmetrical nucleotide interactions in nitrogenase. J Am Chem Soc 2014, 137:146-149.
    • (2014) J Am Chem Soc , vol.137 , pp. 146-149
    • Tezcan, F.A.1    Kaiser, J.T.2    Howard, J.B.3    Rees, D.C.4
  • 7
    • 84943553906 scopus 로고    scopus 로고
    • Evidence for functionally relevant encounter complexes in nitrogenase catalysis
    • Owens C.P., Katz F.E.H., Carter C.H., Luca M.A., Tezcan F.A. Evidence for functionally relevant encounter complexes in nitrogenase catalysis. J Am Chem Soc 2015, 137:12704-12712.
    • (2015) J Am Chem Soc , vol.137 , pp. 12704-12712
    • Owens, C.P.1    Katz, F.E.H.2    Carter, C.H.3    Luca, M.A.4    Tezcan, F.A.5
  • 8
    • 80054972869 scopus 로고    scopus 로고
    • Electron transfer within nitrogenase: evidence for a deficit-spending mechanism
    • Danyal K., Dean D.R., Hoffman B.M., Seefeldt L.C. Electron transfer within nitrogenase: evidence for a deficit-spending mechanism. Biochemistry 2011, 50:9255-9263.
    • (2011) Biochemistry , vol.50 , pp. 9255-9263
    • Danyal, K.1    Dean, D.R.2    Hoffman, B.M.3    Seefeldt, L.C.4
  • 9
    • 79955577511 scopus 로고    scopus 로고
    • Molybdenum nitrogenase catalyzes the reduction and coupling of CO to form hydrocarbons
    • Yang Z.-Y., Dean D.R., Seefeldt L.C. Molybdenum nitrogenase catalyzes the reduction and coupling of CO to form hydrocarbons. J Biol Chem 2011, 286.
    • (2011) J Biol Chem , pp. 286
    • Yang, Z.-Y.1    Dean, D.R.2    Seefeldt, L.C.3
  • 10
    • 84910010879 scopus 로고    scopus 로고
    • Structural characterization of CO-inhibited Mo-nitrogenase by combined application of nuclear resonance vibrational spectroscopy, extended X-ray absorption fine structure, and density functional theory: new insights into the effects of CO binding and the role of the interstitial atom
    • Scott A.D., Pelmenschikov V., Guo Y., Yan L., Wang H., George S.J., Dapper C.H., Newton W.E., Yoda Y., Tanaka Y., Cramer S.P. Structural characterization of CO-inhibited Mo-nitrogenase by combined application of nuclear resonance vibrational spectroscopy, extended X-ray absorption fine structure, and density functional theory: new insights into the effects of CO binding and the role of the interstitial atom. J Am Chem Soc 2014, 136:15942-15954.
    • (2014) J Am Chem Soc , vol.136 , pp. 15942-15954
    • Scott, A.D.1    Pelmenschikov, V.2    Guo, Y.3    Yan, L.4    Wang, H.5    George, S.J.6    Dapper, C.H.7    Newton, W.E.8    Yoda, Y.9    Tanaka, Y.10    Cramer, S.P.11
  • 11
    • 84907444294 scopus 로고    scopus 로고
    • Ligand binding to FeMo-cofactor: structures of CO-bound and reactivated nitrogenase
    • Spatzal T., Perez K.A., Einsle O., Howard J.B., Rees D.C. Ligand binding to FeMo-cofactor: structures of CO-bound and reactivated nitrogenase. Science 2014, 345:1620-1623.
    • (2014) Science , vol.345 , pp. 1620-1623
    • Spatzal, T.1    Perez, K.A.2    Einsle, O.3    Howard, J.B.4    Rees, D.C.5
  • 15
    • 84907646505 scopus 로고    scopus 로고
    • Nitrite and hydroxylamine as nitrogenase substrates: mechanistic implications for the pathway of N2 reduction
    • Shaw S., Lukoyoyanov D., Danyal K., Dean D.R., Hoffman B.M., Seefeldt L.C. Nitrite and hydroxylamine as nitrogenase substrates: mechanistic implications for the pathway of N2 reduction. J Am Chem Soc 2014, 136:12776-12783.
    • (2014) J Am Chem Soc , vol.136 , pp. 12776-12783
    • Shaw, S.1    Lukoyoyanov, D.2    Danyal, K.3    Dean, D.R.4    Hoffman, B.M.5    Seefeldt, L.C.6
  • 17
    • 84925267110 scopus 로고    scopus 로고
    • Identification of a key catalytic intermediate demonstrates that nitrogenase is activated by the reversible exchange of N2 for H2
    • Lukoyoyanov D., Yang Z.-Y., Khada N., Dean D.R., Seefeldt L.C., Hoffman B.M. Identification of a key catalytic intermediate demonstrates that nitrogenase is activated by the reversible exchange of N2 for H2. J Am Chem Soc 2015, 137:3610-3615.
    • (2015) J Am Chem Soc , vol.137 , pp. 3610-3615
    • Lukoyoyanov, D.1    Yang, Z.-Y.2    Khada, N.3    Dean, D.R.4    Seefeldt, L.C.5    Hoffman, B.M.6
  • 18
    • 84883705903 scopus 로고    scopus 로고
    • Catalytic conversion of nitrogen to ammonia by an iron model complex
    • Anderson J.S., Rittle J., Peters J.C. Catalytic conversion of nitrogen to ammonia by an iron model complex. Nature 2013, 501:84-88.
    • (2013) Nature , vol.501 , pp. 84-88
    • Anderson, J.S.1    Rittle, J.2    Peters, J.C.3
  • 22
    • 84861907161 scopus 로고    scopus 로고
    • Laser-flash photolysis indicates that internal electron transfer is triggered by proton uptake by Alcaligenes xylosoxidans copper-dependent nitrite reductase
    • Leferink N.G.H., Eady R.R., Hasnain S.S., Scrutton N.S. Laser-flash photolysis indicates that internal electron transfer is triggered by proton uptake by Alcaligenes xylosoxidans copper-dependent nitrite reductase. FEBS J 2012, 279:2174-2181.
    • (2012) FEBS J , vol.279 , pp. 2174-2181
    • Leferink, N.G.H.1    Eady, R.R.2    Hasnain, S.S.3    Scrutton, N.S.4
  • 23
    • 80053063915 scopus 로고    scopus 로고
    • Spectroelectrochemical investigation of intramolecular and interfacial electron-transfer rates reveals differences between nitrite reductase at rest and during turnover
    • Krzemiński L., Ndamba L., Canters G.W., Aartsma T.J., Evans S.D., Jeuken L.J.C. Spectroelectrochemical investigation of intramolecular and interfacial electron-transfer rates reveals differences between nitrite reductase at rest and during turnover. J Am Chem Soc 2011, 133:15085-15093.
    • (2011) J Am Chem Soc , vol.133 , pp. 15085-15093
    • Krzemiński, L.1    Ndamba, L.2    Canters, G.W.3    Aartsma, T.J.4    Evans, S.D.5    Jeuken, L.J.C.6
  • 24
    • 62649090829 scopus 로고    scopus 로고
    • Spectroscopic and computational studies of nitrite reductase: proton induced electron transfer and backbonding contributions to reactivity
    • Ghosh S., Dey A., Sun Y., Scholes C.P., Solomon E.I. Spectroscopic and computational studies of nitrite reductase: proton induced electron transfer and backbonding contributions to reactivity. J Am Chem Soc 2009, 131:277-288.
    • (2009) J Am Chem Soc , vol.131 , pp. 277-288
    • Ghosh, S.1    Dey, A.2    Sun, Y.3    Scholes, C.P.4    Solomon, E.I.5
  • 25
    • 84904466534 scopus 로고    scopus 로고
    • Impact of residues remote from the catalytic centre on enzyme catalysis of copper nitrite reductase
    • Leferink N.G.H., Antonyuk S.V., Houwman J.A., Scrutton N.S., Eady R.R., Hasnain S.S. Impact of residues remote from the catalytic centre on enzyme catalysis of copper nitrite reductase. Nat Commun 2014, 5:4395-4443.
    • (2014) Nat Commun , vol.5 , pp. 4395-4443
    • Leferink, N.G.H.1    Antonyuk, S.V.2    Houwman, J.A.3    Scrutton, N.S.4    Eady, R.R.5    Hasnain, S.S.6
  • 26
    • 70449116515 scopus 로고    scopus 로고
    • Structural basis of inter-protein electron transfer for nitrite reduction in denitrification
    • Nojiri M., Koteishi H., Nakagami T., Kobayashi K., Inoue T., Yamaguchi K., Suzuki S. Structural basis of inter-protein electron transfer for nitrite reduction in denitrification. Nature 2009, 462:117-121.
    • (2009) Nature , vol.462 , pp. 117-121
    • Nojiri, M.1    Koteishi, H.2    Nakagami, T.3    Kobayashi, K.4    Inoue, T.5    Yamaguchi, K.6    Suzuki, S.7
  • 29
    • 84875883028 scopus 로고    scopus 로고
    • Structures of protein-protein complexes involved in electron transfer
    • Antonyuk S.V., Han C., Eady R.R., Hasnain S.S. Structures of protein-protein complexes involved in electron transfer. Nature 2013, 496:123-127.
    • (2013) Nature , vol.496 , pp. 123-127
    • Antonyuk, S.V.1    Han, C.2    Eady, R.R.3    Hasnain, S.S.4
  • 30
    • 84879967534 scopus 로고    scopus 로고
    • Structural and mechanistic insights into the electron flow through protein for cytochrome c-tethering copper nitrite reductase
    • Tsuda A., Ishikawa R., Koteishi H., Tange K., Fukuda Y., Kobayashi K., Inoue T., Nojiri M. Structural and mechanistic insights into the electron flow through protein for cytochrome c-tethering copper nitrite reductase. J Biochem 2013, 154:51-60.
    • (2013) J Biochem , vol.154 , pp. 51-60
    • Tsuda, A.1    Ishikawa, R.2    Koteishi, H.3    Tange, K.4    Fukuda, Y.5    Kobayashi, K.6    Inoue, T.7    Nojiri, M.8
  • 31
    • 84860880998 scopus 로고    scopus 로고
    • Characterization of a novel copper heme c dissimilatory nitrite reductase from Ralstonia pickettii
    • Han C., Wright G.S.A., Fisher K., Rigby S.E.J., Eady R.R., Hasnain S.S. Characterization of a novel copper heme c dissimilatory nitrite reductase from Ralstonia pickettii. Biochem J 2012, 444:219-226.
    • (2012) Biochem J , vol.444 , pp. 219-226
    • Han, C.1    Wright, G.S.A.2    Fisher, K.3    Rigby, S.E.J.4    Eady, R.R.5    Hasnain, S.S.6
  • 32
    • 84892396381 scopus 로고    scopus 로고
    • Steady-state kinetics with nitric oxide reductase (NOR): new considerations on substrate inhibition profile and catalytic mechanism
    • Duarte A.G., Cordas C.M., José J.G., Moura J.G.G., Moura I. Steady-state kinetics with nitric oxide reductase (NOR): new considerations on substrate inhibition profile and catalytic mechanism. Bichim Biophys Acta 2014, 1837:375-384.
    • (2014) Bichim Biophys Acta , vol.1837 , pp. 375-384
    • Duarte, A.G.1    Cordas, C.M.2    José, J.G.3    Moura, J.G.G.4    Moura, I.5
  • 35
    • 85137163644 scopus 로고    scopus 로고
    • Molecular dynamics simulations reveal proton transfer pathways in cytochrome c-dependent nitric oxide reductase
    • Pisliakov AV, Hino T, Shiro Y, Sugita Y: Molecular dynamics simulations reveal proton transfer pathways in cytochrome c-dependent nitric oxide reductase. PLoS Comput Biol 8: e1002674. doi:10.1371/journal.pcbi.
    • PLoS Comput Biol 8 , pp. e1002674
    • Pisliakov, A.V.1    Hino, T.2    Shiro, Y.3    Sugita, Y.4
  • 36
    • 84864711477 scopus 로고    scopus 로고
    • Structure and function of bacterial nitric oxide reductases nitric oxide reductase anaerobic enzymes
    • Shiro Y. Structure and function of bacterial nitric oxide reductases nitric oxide reductase anaerobic enzymes. Bichim Biophys Acta 2012, 1817:1907-1913.
    • (2012) Bichim Biophys Acta , vol.1817 , pp. 1907-1913
    • Shiro, Y.1
  • 37
    • 84869446703 scopus 로고    scopus 로고
    • Nature's way of handling a greenhouse gas: the copper-sulfur cluster of purple nitrous oxide reductase
    • Wüst A., Schneider L., Pomowski A., Zumft W.G., Kroneck P.M.H., Einsle O. Nature's way of handling a greenhouse gas: the copper-sulfur cluster of purple nitrous oxide reductase. Biol Chem 2014, 393:1067-1077.
    • (2014) Biol Chem , vol.393 , pp. 1067-1077
    • Wüst, A.1    Schneider, L.2    Pomowski, A.3    Zumft, W.G.4    Kroneck, P.M.H.5    Einsle, O.6
  • 38
    • 84892750385 scopus 로고    scopus 로고
    • Determination of the active form of the tetranuclear copper sulfur cluster in nitrous oxide reductase
    • Johnston E.M., Dell'Acqua S., Ramos S., Pauleta S.R., Moura I., Solomon E.I. Determination of the active form of the tetranuclear copper sulfur cluster in nitrous oxide reductase. J Am Chem Soc 2014, 136:614-617.
    • (2014) J Am Chem Soc , vol.136 , pp. 614-617
    • Johnston, E.M.1    Dell'Acqua, S.2    Ramos, S.3    Pauleta, S.R.4    Moura, I.5    Solomon, E.I.6
  • 40
    • 80052577976 scopus 로고    scopus 로고
    • 2O binding at a [4Cu:2S] copper-sulphur cluster in nitrous oxide reductase
    • 2O binding at a [4Cu:2S] copper-sulphur cluster in nitrous oxide reductase. Nature 2011, 477:234-237.
    • (2011) Nature , vol.477 , pp. 234-237
    • Pomowski, A.1    Zumft, W.G.2    Kroneck, P.M.H.3    Einsle, O.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.