메뉴 건너뛰기




Volumn 39, Issue 32, 2014, Pages 18574-18582

The proton iron-sulfur cluster environment of the [FeFe]-hydrogenase maturation protein HydF from Thermotoga neapolitana

Author keywords

EPR; HydF; Hydrogenase; Iron sulfur cluster coordination; Iron sulfur proteins

Indexed keywords

AMINO ACIDS; IRON; LIGANDS; PARAMAGNETIC RESONANCE; PROTEINS; SULFUR;

EID: 84908248525     PISSN: 03603199     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijhydene.2013.12.164     Document Type: Conference Paper
Times cited : (10)

References (43)
  • 1
    • 35748974830 scopus 로고    scopus 로고
    • Occurrence, classification, and biological function of hydrogenases: An overview
    • P.M. Vignais, and B. Billoud Occurrence, classification, and biological function of hydrogenases: an overview Chem Rev 107 2007 4206 4272
    • (2007) Chem Rev , vol.107 , pp. 4206-4272
    • Vignais, P.M.1    Billoud, B.2
  • 3
    • 79957993544 scopus 로고    scopus 로고
    • Oxygen-tolerant hydrogenases in hydrogen-based technologies
    • B. Friedrich, J. Fritsch, and O. Lenz Oxygen-tolerant hydrogenases in hydrogen-based technologies Curr Opin Biotechnol 22 2011 358 364
    • (2011) Curr Opin Biotechnol , vol.22 , pp. 358-364
    • Friedrich, B.1    Fritsch, J.2    Lenz, O.3
  • 4
    • 38849180102 scopus 로고    scopus 로고
    • Comparative analysis of Fe-only hydrogenase from Thermotogales indicates the molecular basis of resistance to oxygen inactivation
    • S.C.E. Tosatto, S. Toppo, D. Carbonera, G.M. Giacometti, and P. Costantini Comparative analysis of Fe-only hydrogenase from Thermotogales indicates the molecular basis of resistance to oxygen inactivation Int J Hydrogen Energy 33 2008 570 578
    • (2008) Int J Hydrogen Energy , vol.33 , pp. 570-578
    • Tosatto, S.C.E.1    Toppo, S.2    Carbonera, D.3    Giacometti, G.M.4    Costantini, P.5
  • 5
    • 35748930865 scopus 로고    scopus 로고
    • Structure/function relationships of [NiFe]-And [FeFe]-hydrogenases
    • J.C. Fontecilla-Camps, A. Volbeda, C. Cavazza, and Y. Nicolet Structure/function relationships of [NiFe]-And [FeFe]-hydrogenases Chem Rev 107 2007 4273 4303
    • (2007) Chem Rev , vol.107 , pp. 4273-4303
    • Fontecilla-Camps, J.C.1    Volbeda, A.2    Cavazza, C.3    Nicolet, Y.4
  • 7
    • 0025975104 scopus 로고
    • Molecular chracterization of an operon (hyp) necessary for the activity of the three hydrogenase isoenzymes in Escherichia coli
    • S. Lutz, A. Jacobi, V. Schlensog, R. Böhm, G. Sawers, and A. Böck Molecular chracterization of an operon (hyp) necessary for the activity of the three hydrogenase isoenzymes in Escherichia coli Mol Microbiol 5 1991 123 135
    • (1991) Mol Microbiol , vol.5 , pp. 123-135
    • Lutz, S.1    Jacobi, A.2    Schlensog, V.3    Böhm, R.4    Sawers, G.5    Böck, A.6
  • 8
    • 0035340936 scopus 로고    scopus 로고
    • Maturation of the NiFe]-hydrogenases
    • L. Casalot, and M. Rousset Maturation of the NiFe]-hydrogenases Trends Microbiol 9 2001 228 237
    • (2001) Trends Microbiol , vol.9 , pp. 228-237
    • Casalot, L.1    Rousset, M.2
  • 9
    • 84861881676 scopus 로고    scopus 로고
    • Emerging paradigms for complex iron-sulfur cofactor assembly and insertion
    • J.W. Peters, and J.B. Broderick Emerging paradigms for complex iron-sulfur cofactor assembly and insertion Annu Rev Biochem 81 2012 429 450
    • (2012) Annu Rev Biochem , vol.81 , pp. 429-450
    • Peters, J.W.1    Broderick, J.B.2
  • 10
    • 84859982642 scopus 로고    scopus 로고
    • Structure-function relationships in [FeFe]-hydrogenase active site maturation
    • Y. Nicolet, and J.C. Fontecilla-Camps Structure-function relationships in [FeFe]-hydrogenase active site maturation J Biol Chem 287 2012 13532 13540
    • (2012) J Biol Chem , vol.287 , pp. 13532-13540
    • Nicolet, Y.1    Fontecilla-Camps, J.C.2
  • 11
    • 0032483966 scopus 로고    scopus 로고
    • X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 angstrom resolution
    • J.W. Peters, W.N. Lanzilotta, B.J. Lemon, and L.C. Seefeldt X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 angstrom resolution Science 282 1998 1853 1858
    • (1998) Science , vol.282 , pp. 1853-1858
    • Peters, J.W.1    Lanzilotta, W.N.2    Lemon, B.J.3    Seefeldt, L.C.4
  • 12
    • 0033556301 scopus 로고    scopus 로고
    • Desulfovibrio desulfuricans iron hydrogenase: The structure shows unusual coordination to an active site Fe binuclear center
    • Y. Nicolet, C. Piras, P. Legrand, C.E. Hatchikian, and J.C. Fontecilla-Camps Desulfovibrio desulfuricans iron hydrogenase: the structure shows unusual coordination to an active site Fe binuclear center Structure 7 1999 13 23
    • (1999) Structure , vol.7 , pp. 13-23
    • Nicolet, Y.1    Piras, C.2    Legrand, P.3    Hatchikian, C.E.4    Fontecilla-Camps, J.C.5
  • 13
    • 2942586665 scopus 로고    scopus 로고
    • Discovery of two novel radical S-Adenosylmethionine proteins required for the assembly of an active [Fe] hydrogenase
    • M.C. Posewitz, P.W. King, S.L. Smolinski, L. Zhang, M. Seibert, and M.L. Ghirardi Discovery of two novel radical S-Adenosylmethionine proteins required for the assembly of an active [Fe] hydrogenase J Biol Chem 279 2004 25711 25720
    • (2004) J Biol Chem , vol.279 , pp. 25711-25720
    • Posewitz, M.C.1    King, P.W.2    Smolinski, S.L.3    Zhang, L.4    Seibert, M.5    Ghirardi, M.L.6
  • 15
    • 24144494192 scopus 로고    scopus 로고
    • Biochemical characterization of the HydE and HydG iron-only hydrogenase maturation enzymes from Thermotoga maritima
    • J.K. Ruback, X. Brazzolotto, J. Gaillard, and M. Fontecave Biochemical characterization of the HydE and HydG iron-only hydrogenase maturation enzymes from Thermotoga maritima FEBS Lett 579 2005 5055 5060
    • (2005) FEBS Lett , vol.579 , pp. 5055-5060
    • Ruback, J.K.1    Brazzolotto, X.2    Gaillard, J.3    Fontecave, M.4
  • 18
    • 49649115936 scopus 로고    scopus 로고
    • X-ray structure of the [FeFe]-hydrogenase maturase HydE from Thermotoga maritima
    • Y. Nicolet, J.K. Rubach, M.C. Posewitz, P. Amara, P. Mathevon, and M. Atta X-ray structure of the [FeFe]-hydrogenase maturase HydE from Thermotoga maritima J Biol Chem 283 2008 18861 18872
    • (2008) J Biol Chem , vol.283 , pp. 18861-18872
    • Nicolet, Y.1    Rubach, J.K.2    Posewitz, M.C.3    Amara, P.4    Mathevon, P.5    Atta, M.6
  • 19
    • 33644852344 scopus 로고    scopus 로고
    • The [FeFe]-hydrogenase maturation protein HydF from Thermotoga maritima is a GTPase with iron-sulfur cluster
    • X. Brazzolotto, J.K. Rubach, J. Gaillard, S. Gambarelli, M. Atta, and M. Fontecave The [FeFe]-hydrogenase maturation protein HydF from Thermotoga maritima is a GTPase with iron-sulfur cluster J Biol Chem 281 2006 769 774
    • (2006) J Biol Chem , vol.281 , pp. 769-774
    • Brazzolotto, X.1    Rubach, J.K.2    Gaillard, J.3    Gambarelli, S.4    Atta, M.5    Fontecave, M.6
  • 24
    • 84867753153 scopus 로고    scopus 로고
    • Biochemical analysis of the interactions between the proteins involved in the [FeFe]-hydrogenase maturation process
    • F. Vallese, P. Berto, M. Ruzzene, L. Cendron, S. Sarno, and E. De Rosa Biochemical analysis of the interactions between the proteins involved in the [FeFe]-hydrogenase maturation process J Biol Chem 287 2012 36544 36555
    • (2012) J Biol Chem , vol.287 , pp. 36544-36555
    • Vallese, F.1    Berto, P.2    Ruzzene, M.3    Cendron, L.4    Sarno, S.5    De Rosa, E.6
  • 25
    • 30644471959 scopus 로고    scopus 로고
    • A radical solution for the biosynthesis of the H-cluster of the hydrogenase
    • J.W. Peters, R.K. Szilagyi, A. Naumov, and T. Douglas A radical solution for the biosynthesis of the H-cluster of the hydrogenase FEBS Lett 580 2006 363 367
    • (2006) FEBS Lett , vol.580 , pp. 363-367
    • Peters, J.W.1    Szilagyi, R.K.2    Naumov, A.3    Douglas, T.4
  • 29
    • 33644850541 scopus 로고    scopus 로고
    • Functional studies of [FeFe] hydrogenase maturation in an Escherichia coli biosynthetic system
    • P.W. King, M.C. Posewitz, M.L. Ghirardi, and M. Seibert Functional studies of [FeFe] hydrogenase maturation in an Escherichia coli biosynthetic system J Bacteriol 188 2006 2163 2172
    • (2006) J Bacteriol , vol.188 , pp. 2163-2172
    • King, P.W.1    Posewitz, M.C.2    Ghirardi, M.L.3    Seibert, M.4
  • 30
    • 78650856177 scopus 로고    scopus 로고
    • The [FeFe]-hydrogenase maturation protein HydF contains a H-cluster like [4Fe-4S]-2Fe site
    • I. Czech, S. Stripp, O. Sanganas, N. Leidel, T. Happe, and M. Haumann The [FeFe]-hydrogenase maturation protein HydF contains a H-cluster like [4Fe-4S]-2Fe site FEBS Lett 585 2011 225 230
    • (2011) FEBS Lett , vol.585 , pp. 225-230
    • Czech, I.1    Stripp, S.2    Sanganas, O.3    Leidel, N.4    Happe, T.5    Haumann, M.6
  • 32
    • 83755168841 scopus 로고    scopus 로고
    • Crystal structure of HydF scaffold protein provides insights into [FeFe]-hydrogenase maturation
    • L. Cendron, P. Berto, S. D'Adamo, F. Vallese, C. Govoni, and M.C. Posewitz Crystal structure of HydF scaffold protein provides insights into [FeFe]-hydrogenase maturation J Biol Chem 286 2011 43944 43950
    • (2011) J Biol Chem , vol.286 , pp. 43944-43950
    • Cendron, L.1    Berto, P.2    D'Adamo, S.3    Vallese, F.4    Govoni, C.5    Posewitz, M.C.6
  • 33
    • 84867507153 scopus 로고    scopus 로고
    • The [4Fe-4S]-cluster coordination sphere of [FeFe]-hydrogenase maturation protein HydF as revealed by EPR and HYSCORE spectroscopies
    • P. Berto, M. Di Valentin, L. Cendron, F. Vallese, M. Albertini, and E. Salvadori The [4Fe-4S]-cluster coordination sphere of [FeFe]-hydrogenase maturation protein HydF as revealed by EPR and HYSCORE spectroscopies Biochim Biophys Acta 1817 2012 2149 2157
    • (2012) Biochim Biophys Acta , vol.1817 , pp. 2149-2157
    • Berto, P.1    Di Valentin, M.2    Cendron, L.3    Vallese, F.4    Albertini, M.5    Salvadori, E.6
  • 34
    • 33847670407 scopus 로고
    • Ferrozine-A new spectrophotometric reagent for iron
    • L.L. Stookey Ferrozine-A new spectrophotometric reagent for iron Anal Chem 42 1970 779 781
    • (1970) Anal Chem , vol.42 , pp. 779-781
    • Stookey, L.L.1
  • 35
    • 28844486080 scopus 로고    scopus 로고
    • EasySpin, a comprehensive software package for spectral simulation and analysis in EPR
    • S. Stoll, and A. Schweiger EasySpin, a comprehensive software package for spectral simulation and analysis in EPR J Magn Reson 178 2006 42 55
    • (2006) J Magn Reson , vol.178 , pp. 42-55
    • Stoll, S.1    Schweiger, A.2
  • 36
    • 4244204839 scopus 로고    scopus 로고
    • A practical strategy for determination of proton hyperfine interaction parameters in paramagnetic transition metal ion complexes by two-dimensional HYSCORE electron spin resonance spectroscopy in disordered systems
    • A. Pöppl, and L. Kevan A practical strategy for determination of proton hyperfine interaction parameters in paramagnetic transition metal ion complexes by two-dimensional HYSCORE electron spin resonance spectroscopy in disordered systems J Phys Chem 100 1996 3387 3394
    • (1996) J Phys Chem , vol.100 , pp. 3387-3394
    • Pöppl, A.1    Kevan, L.2
  • 37
    • 12944326891 scopus 로고    scopus 로고
    • An orientation-selected ENDOR and HYSCORE study of the Ni-C active state of Desulfovibrio vulgaris Miyazaki F hydrogenase
    • S. Foerster, M. Van Gastel, M. Brecht, and W. Lubitz An orientation-selected ENDOR and HYSCORE study of the Ni-C active state of Desulfovibrio vulgaris Miyazaki F hydrogenase J Biol Inorg Chem 10 2005 51 62
    • (2005) J Biol Inorg Chem , vol.10 , pp. 51-62
    • Foerster, S.1    Van Gastel, M.2    Brecht, M.3    Lubitz, W.4
  • 38
    • 67649389592 scopus 로고    scopus 로고
    • Synthesis and characterization of de novo designed peptides modelling the binding sites of [4Fe-4S] clusters in photosystem i
    • M.L. Antonkine, M.S. Koay, B. Epel, C. Breitenstein, O. Gopta, and W. Gärtner Synthesis and characterization of de novo designed peptides modelling the binding sites of [4Fe-4S] clusters in photosystem I Biochim Biophys Acta 1787 2009 995 1008
    • (2009) Biochim Biophys Acta , vol.1787 , pp. 995-1008
    • Antonkine, M.L.1    Koay, M.S.2    Epel, B.3    Breitenstein, C.4    Gopta, O.5    Gärtner, W.6
  • 42
    • 0033541085 scopus 로고    scopus 로고
    • 3+ cluster of Ecothiorhodospira halophila iso-II high-potential iron-sulfur protein by ENDOR spectroscopy
    • 3+ cluster of Ecothiorhodospira halophila iso-II high-potential iron-sulfur protein by ENDOR spectroscopy J Am Chem Soc 16 1999 1925 1935
    • (1999) J Am Chem Soc , vol.16 , pp. 1925-1935
    • Kappl, R.1    Ciurli, S.2    Luchinat, C.3    Huttermann, J.4
  • 43
    • 0024965232 scopus 로고
    • Engineering of protein bound iron-sulfur clusters. A tool for the study of protein and cluster chemistry and mechanism of iron-sulfur enzymes
    • H. Beinert, and M.C. Kennedy Engineering of protein bound iron-sulfur clusters. A tool for the study of protein and cluster chemistry and mechanism of iron-sulfur enzymes Eur J Biochem 186 1989 5 15
    • (1989) Eur J Biochem , vol.186 , pp. 5-15
    • Beinert, H.1    Kennedy, M.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.