메뉴 건너뛰기




Volumn 12, Issue 1, 2016, Pages 46-50

Mechanism of hydrogen activation by [NiFe] hydrogenases

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ASPARAGINE; ENZYME VARIANT; GUANIDINE; HYDROGEN; LYSINE; NICKEL IRON HYDROGENASE; ESCHERICHIA COLI PROTEIN; HYDROGENASE; HYDROGENASE 1, E COLI; IRON; NICKEL;

EID: 84951567017     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.1976     Document Type: Article
Times cited : (98)

References (41)
  • 2
    • 84859464540 scopus 로고    scopus 로고
    • 2-tolerant [NiFe]-hydrogenase 1 from Escherichia coli
    • 2-tolerant [NiFe]-hydrogenase 1 from Escherichia coli. Proc. Natl. Acad. Sci. USA 109, 5305-5310 (2012).
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 5305-5310
    • Volbeda, A.1
  • 3
    • 73349126734 scopus 로고    scopus 로고
    • Frustrated Lewis pairs: Metal-free hydrogen activation and more
    • Stephan, D.W. & Erker, G. Frustrated Lewis pairs: metal-free hydrogen activation and more. Angew. Chem. Int. Ed. Engl. 49, 46-76 (2010).
    • (2010) Angew. Chem. Int. Ed. Engl. , vol.49 , pp. 46-76
    • Stephan, D.W.1    Erker, G.2
  • 4
    • 84871851876 scopus 로고    scopus 로고
    • Analyses of the large subunit histidine-rich motif expose an alternative proton transfer pathway in [NiFe] hydrogenases
    • Szo{combining double acute accent}ri-Dorogházi, E. et al. Analyses of the large subunit histidine-rich motif expose an alternative proton transfer pathway in [NiFe] hydrogenases. PLoS One 7, e34666 (2012).
    • (2012) PLoS One , vol.7
    • Szori-Dorogházi, E.1
  • 5
    • 0030481349 scopus 로고    scopus 로고
    • Structure of the [NiFe] hydrogenase active site: Evidence for biologically uncommon Fe ligands
    • Volbeda, A. et al. Structure of the [NiFe] hydrogenase active site: evidence for biologically uncommon Fe ligands. J. Am. Chem. Soc. 118, 12989-12996 (1996).
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 12989-12996
    • Volbeda, A.1
  • 6
    • 0030805822 scopus 로고    scopus 로고
    • Infrared-spectroelectrochemical characterization of the [NiFe] hydrogenase of Desulfovibrio gigas
    • de Lacey, A.L. et al. Infrared-spectroelectrochemical characterization of the [NiFe] hydrogenase of Desulfovibrio gigas. J. Am. Chem. Soc. 119, 7181-7189 (1997).
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 7181-7189
    • De Lacey, A.L.1
  • 7
    • 0037257457 scopus 로고    scopus 로고
    • Spectroscopic and kinetic characterization of active site mutants of Desulfovibrio fructosovorans Ni-Fe hydrogenase
    • deLacey, A.L., Fernandez, V.M., Rousset, M., Cavazza, C. & Hatchikian, E.C. Spectroscopic and kinetic characterization of active site mutants of Desulfovibrio fructosovorans Ni-Fe hydrogenase. J. Biol. Inorg. Chem. 8, 129-134 (2003).
    • (2003) J. Biol. Inorg. Chem. , vol.8 , pp. 129-134
    • DeLacey, A.L.1    Fernandez, V.M.2    Rousset, M.3    Cavazza, C.4    Hatchikian, E.C.5
  • 8
    • 84874101282 scopus 로고    scopus 로고
    • Principles of sustained enzymatic hydrogen oxidation in the presence of oxygen - The crucial influence of high potential Fe-S clusters in the electron relay of [NiFe]-hydrogenases
    • Evans, R.M. et al. Principles of sustained enzymatic hydrogen oxidation in the presence of oxygen - the crucial influence of high potential Fe-S clusters in the electron relay of [NiFe]-hydrogenases. J. Am. Chem. Soc. 135, 2694-2707 (2013).
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 2694-2707
    • Evans, R.M.1
  • 9
    • 84863899218 scopus 로고    scopus 로고
    • Electrocatalytic mechanism of reversible hydrogen cycling by enzymes and distinctions between the major classes of hydrogenases
    • Hexter, S.V., Grey, F., Happe, T., Climent, V. & Armstrong, F.A. Electrocatalytic mechanism of reversible hydrogen cycling by enzymes and distinctions between the major classes of hydrogenases. Proc. Natl. Acad. Sci. USA 109, 11516-11521 (2012).
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 11516-11521
    • Hexter, S.V.1    Grey, F.2    Happe, T.3    Climent, V.4    Armstrong, F.A.5
  • 10
    • 84896967315 scopus 로고    scopus 로고
    • Transforming an oxygen-tolerant NiFe uptake hydrogenase into a proficient, reversible hydrogen producer
    • Murphy, B.J., Sargent, F. & Armstrong, F.A. Transforming an oxygen-tolerant NiFe uptake hydrogenase into a proficient, reversible hydrogen producer. Energy Environ. Sci. 7, 1426-1433 (2014).
    • (2014) Energy Environ. Sci. , vol.7 , pp. 1426-1433
    • Murphy, B.J.1    Sargent, F.2    Armstrong, F.A.3
  • 11
    • 76149104243 scopus 로고    scopus 로고
    • Dynamic electrochemical experiments on hydrogenases
    • Armstrong, F.A. Dynamic electrochemical experiments on hydrogenases. Photosynth. Res. 102, 541-550 (2009).
    • (2009) Photosynth. Res. , vol.102 , pp. 541-550
    • Armstrong, F.A.1
  • 12
    • 57649243241 scopus 로고    scopus 로고
    • Dynamic electrochemical investigations of hydrogen oxidation and production by enzymes and implications for future technology
    • Armstrong, F.A. et al. Dynamic electrochemical investigations of hydrogen oxidation and production by enzymes and implications for future technology. Chem. Soc. Rev. 38, 36-51 (2009).
    • (2009) Chem. Soc. Rev. , vol.38 , pp. 36-51
    • Armstrong, F.A.1
  • 13
    • 84922003331 scopus 로고    scopus 로고
    • Crystallographic studies of [NiFe]-hydrogenase mutants: Towards consensus structures for the elusive unready oxidized states
    • Volbeda, A. et al. Crystallographic studies of [NiFe]-hydrogenase mutants: towards consensus structures for the elusive unready oxidized states. J. Biol. Inorg. Chem. 20, 11-22 (2015).
    • (2015) J. Biol. Inorg. Chem. , vol.20 , pp. 11-22
    • Volbeda, A.1
  • 14
    • 84928538572 scopus 로고    scopus 로고
    • Hydrogens detected by subatomic resolution protein crystallography in a [NiFe] hydrogenase
    • Ogata, H., Nishikawa, K. & Lubitz, W. Hydrogens detected by subatomic resolution protein crystallography in a [NiFe] hydrogenase. Nature 520, 571-574 (2015).
    • (2015) Nature , vol.520 , pp. 571-574
    • Ogata, H.1    Nishikawa, K.2    Lubitz, W.3
  • 15
    • 35748930865 scopus 로고    scopus 로고
    • Structure/function relationships of [NiFe]- and [FeFe]-hydrogenases
    • Fontecilla-Camps, J.C., Volbeda, A., Cavazza, C. & Nicolet, Y. Structure/function relationships of [NiFe]- and [FeFe]-hydrogenases. Chem. Rev. 107, 4273-4303 (2007).
    • (2007) Chem. Rev. , vol.107 , pp. 4273-4303
    • Fontecilla-Camps, J.C.1    Volbeda, A.2    Cavazza, C.3    Nicolet, Y.4
  • 16
    • 0000582831 scopus 로고
    • The crystal structures of hydrogen cyanide, HCN
    • Dulmage, W.J. & Lipscomb, W.N. The crystal structures of hydrogen cyanide, HCN. Acta Crystallogr. 4, 330-334 (1951).
    • (1951) Acta Crystallogr , vol.4 , pp. 330-334
    • Dulmage, W.J.1    Lipscomb, W.N.2
  • 17
    • 69949116438 scopus 로고    scopus 로고
    • X-H-π and X-H-N hydrogen bonds - Acetylene and hydrogen cyanide as proton acceptors
    • Domagała, M. & Grabowski, S.J. X-H-π and X-H-N hydrogen bonds - acetylene and hydrogen cyanide as proton acceptors. Chem. Phys. 363, 42-48 (2009).
    • (2009) Chem. Phys. , vol.363 , pp. 42-48
    • Domagała, M.1    Grabowski, S.J.2
  • 19
    • 84893804908 scopus 로고    scopus 로고
    • Estimating the acidity of transition metal hydride and dihydrogen complexes by adding ligand acidity constants
    • Morris, R.H. Estimating the acidity of transition metal hydride and dihydrogen complexes by adding ligand acidity constants. J. Am. Chem. Soc. 136, 1948-1959 (2014).
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 1948-1959
    • Morris, R.H.1
  • 20
    • 84938947130 scopus 로고    scopus 로고
    • Hydride bridge in [NiFe]-hydrogenase observed by nuclear resonance vibrational spectroscopy
    • Ogata, H. et al. Hydride bridge in [NiFe]-hydrogenase observed by nuclear resonance vibrational spectroscopy. Nat. Commun. 6, 7890 (2015).
    • (2015) Nat. Commun. , vol.6 , pp. 7890
    • Ogata, H.1
  • 21
    • 84871552098 scopus 로고    scopus 로고
    • A functional [NiFe]-hydrogenase model compound that undergoes biologically relevant reversible thiolate protonation
    • Weber, K. et al. A functional [NiFe]-hydrogenase model compound that undergoes biologically relevant reversible thiolate protonation. J. Am. Chem. Soc. 134, 20745-20755 (2012).
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 20745-20755
    • Weber, K.1
  • 22
    • 84873509989 scopus 로고    scopus 로고
    • 2
    • 2. Science 339, 682-684 (2013).
    • (2013) Science , vol.339 , pp. 682-684
    • Ogo, S.1
  • 23
    • 1642355691 scopus 로고    scopus 로고
    • A glutamate is the essential proton transfer gate during the catalytic cycle of the [NiFe] hydrogenase
    • Dementin, S. et al. A glutamate is the essential proton transfer gate during the catalytic cycle of the [NiFe] hydrogenase. J. Biol. Chem. 279, 10508-10513 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 10508-10513
    • Dementin, S.1
  • 24
    • 9744226460 scopus 로고    scopus 로고
    • A twisted base? The role of arginine in enzyme-catalyzed proton abstractions
    • Guillén Schlippe, Y.V. & Hedstrom, L. A twisted base? The role of arginine in enzyme-catalyzed proton abstractions. Arch. Biochem. Biophys. 433, 266-278 (2005).
    • (2005) Arch. Biochem. Biophys. , vol.433 , pp. 266-278
    • Guillén Schlippe, Y.V.1    Hedstrom, L.2
  • 25
    • 33745972079 scopus 로고    scopus 로고
    • A proton delivery pathway in the soluble fumarate reductase from Shewanella frigidimarina
    • Pankhurst, K.L. et al. A proton delivery pathway in the soluble fumarate reductase from Shewanella frigidimarina. J. Biol. Chem. 281, 20589-20597 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 20589-20597
    • Pankhurst, K.L.1
  • 26
    • 0035901492 scopus 로고    scopus 로고
    • Probing the active site of L-aspartate oxidase by site-directed mutagenesis: Role of basic residues in fumarate reduction
    • Tedeschi, G. et al. Probing the active site of L-aspartate oxidase by site-directed mutagenesis: role of basic residues in fumarate reduction. Biochemistry 40, 4738-4744 (2001).
    • (2001) Biochemistry , vol.40 , pp. 4738-4744
    • Tedeschi, G.1
  • 29
    • 84879886576 scopus 로고    scopus 로고
    • Biomimetic assembly and activation of [FeFe]-hydrogenases
    • Berggren, G. et al. Biomimetic assembly and activation of [FeFe]-hydrogenases. Nature 499, 66-69 (2013).
    • (2013) Nature , vol.499 , pp. 66-69
    • Berggren, G.1
  • 30
    • 0141789788 scopus 로고    scopus 로고
    • A subset of bacterial inner membrane proteins integrated by the twin-arginine translocase
    • Hatzixanthis, K., Palmer, T. & Sargent, F. A subset of bacterial inner membrane proteins integrated by the twin-arginine translocase. Mol. Microbiol. 49, 1377-1390 (2003).
    • (2003) Mol. Microbiol. , vol.49 , pp. 1377-1390
    • Hatzixanthis, K.1    Palmer, T.2    Sargent, F.3
  • 31
    • 0024340114 scopus 로고
    • New method for generating deletions and gene replacements in Escherichia coli
    • Hamilton, C.M., Aldea, M., Washburn, B.K., Babitzke, P. & Kushner, S.R. New method for generating deletions and gene replacements in Escherichia coli. J. Bacteriol. 171, 4617-4622 (1989).
    • (1989) J. Bacteriol. , vol.171 , pp. 4617-4622
    • Hamilton, C.M.1    Aldea, M.2    Washburn, B.K.3    Babitzke, P.4    Kushner, S.R.5
  • 32
    • 80054971344 scopus 로고    scopus 로고
    • Oxygen-tolerant [NiFe]-hydrogenases: The individual and collective importance of supernumerary cysteines at the proximal Fe-S cluster
    • Lukey, M.J. et al. Oxygen-tolerant [NiFe]-hydrogenases: the individual and collective importance of supernumerary cysteines at the proximal Fe-S cluster. J. Am. Chem. Soc. 133, 16881-16892 (2011).
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 16881-16892
    • Lukey, M.J.1
  • 33
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254 (1976).
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 34
    • 0019879654 scopus 로고
    • Kinetic mechanism of the hydrogen-oxidizing hydrogenase from soybean nodule bacteroids
    • Arp, D.J. & Burris, R.H. Kinetic mechanism of the hydrogen-oxidizing hydrogenase from soybean nodule bacteroids. Biochemistry 20, 2234-2240 (1981).
    • (1981) Biochemistry , vol.20 , pp. 2234-2240
    • Arp, D.J.1    Burris, R.H.2
  • 36
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A.J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658-674 (2007).
    • (2007) J. Appl. Crystallogr. , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 38
    • 79953763877 scopus 로고    scopus 로고
    • REFMAC5 for the refinement of macromolecular crystal structures
    • Murshudov, G.N. et al. REFMAC5 for the refinement of macromolecular crystal structures. Acta Crystallogr. D Biol. Crystallogr. 67, 355-367 (2011).
    • (2011) Acta Crystallogr. D Biol. Crystallogr. , vol.67 , pp. 355-367
    • Murshudov, G.N.1
  • 39
    • 84893482610 scopus 로고
    • A solution for the best rotation to relate two sets of vectors
    • Kabsch, W. A solution for the best rotation to relate two sets of vectors. Acta Crystallogr. A 32, 922-923 (1976).
    • (1976) Acta Crystallogr. A , vol.32 , pp. 922-923
    • Kabsch, W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.