메뉴 건너뛰기




Volumn 38, Issue 7, 2013, Pages 2998-3002

Arginine171 of Chlamydomonas reinhardtii [Fe-Fe] hydrogenase HydA1 plays a crucial role in electron transfer to its catalytic center

Author keywords

Fe Fe hydrogenases; Catalytic activity; Ferredoxin binding site; Hydrogen evolution

Indexed keywords

[FEFE]HYDROGENASES; ASPARTIC ACIDS; CATALYTIC CENTER; CHLAMYDOMONAS REINHARDTII; ELECTRON TRANSFER; ELECTRON TRANSPORT; ELECTRON-TRANSFER STEP; FERREDOXIN-BINDING SITE; H-CLUSTER; HYDROGEN EVOLUTION; HYDROGENASES; ORDERS OF MAGNITUDE; REDUCTION OF PROTONS; REINHARDTII; WILD-TYPE PROTEINS;

EID: 84873726380     PISSN: 03603199     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijhydene.2012.12.078     Document Type: Article
Times cited : (13)

References (23)
  • 2
    • 0023975044 scopus 로고    scopus 로고
    • Purification, properties and complete amino acid sequence of the ferredoxin from a green alga, Chlamydomonas reinhardtii
    • J.M. Schmitter, J.P. Jacquot, F. de Lamotte-Guery, C. Beauvallet, S. Dutka, and P. Gadal Purification, properties and complete amino acid sequence of the ferredoxin from a green alga, Chlamydomonas reinhardtii Eur J Biochem 172 1998 405 412
    • (1998) Eur J Biochem , vol.172 , pp. 405-412
    • Schmitter, J.M.1    Jacquot, J.P.2    De Lamotte-Guery, F.3    Beauvallet, C.4    Dutka, S.5    Gadal, P.6
  • 3
    • 24044434598 scopus 로고    scopus 로고
    • Synechocystis ferredoxin/ferredoxin-NADP(+)-reductase/NADP+ complex: Structural model obtained by NMR-restrained docking
    • P.N. Palma, B. Lagoutte, L. Krippahl, J.J. Moura, and F. Guerlesquin Synechocystis ferredoxin/ferredoxin-NADP(+)-reductase/NADP+ complex: structural model obtained by NMR-restrained docking FEBS Lett 579 2005 4585 4590
    • (2005) FEBS Lett , vol.579 , pp. 4585-4590
    • Palma, P.N.1    Lagoutte, B.2    Krippahl, L.3    Moura, J.J.4    Guerlesquin, F.5
  • 4
    • 0027153213 scopus 로고    scopus 로고
    • Isolation, characterization and N-terminal amino acid sequence of hydrogenase from the green alga Chlamydomonas reinhardtii
    • T. Happe, and J.D. Naber Isolation, characterization and N-terminal amino acid sequence of hydrogenase from the green alga Chlamydomonas reinhardtii Eur J Biochem 214 2003 475 481
    • (2003) Eur J Biochem , vol.214 , pp. 475-481
    • Happe, T.1    Naber, J.D.2
  • 5
    • 35748933836 scopus 로고    scopus 로고
    • Investigating and exploiting the catalytic properties of hydrogenases
    • K.A. Vincent, A. Parkin, and F. Armstrong Investigating and exploiting the catalytic properties of hydrogenases Chem Rev 107 2007 4366 4413
    • (2007) Chem Rev , vol.107 , pp. 4366-4413
    • Vincent, K.A.1    Parkin, A.2    Armstrong, F.3
  • 6
    • 0037715163 scopus 로고    scopus 로고
    • Expression of two [Fe]-hydrogenases in Chlamydomonas reinhardtii under anaerobic conditions
    • M. Forestier, P. King, L. Zhang, M. Posewitz, S. Schwarzer, and T. Happe Expression of two [Fe]-hydrogenases in Chlamydomonas reinhardtii under anaerobic conditions Eur J Biochem 270 2003 2750 2758
    • (2003) Eur J Biochem , vol.270 , pp. 2750-2758
    • Forestier, M.1    King, P.2    Zhang, L.3    Posewitz, M.4    Schwarzer, S.5    Happe, T.6
  • 7
    • 77952428962 scopus 로고    scopus 로고
    • Stepwise [FeFe]-hydrogenase H-cluster assembly revealed in the structure of HydA (DeltaEFG)
    • D.W. Mulder, E.S. Boyd, R. Sarma, R.K. Lange, J.A. Endrizzi, and J.B. Broderick Stepwise [FeFe]-hydrogenase H-cluster assembly revealed in the structure of HydA (DeltaEFG) Nature 465 2010 248 251
    • (2010) Nature , vol.465 , pp. 248-251
    • Mulder, D.W.1    Boyd, E.S.2    Sarma, R.3    Lange, R.K.4    Endrizzi, J.A.5    Broderick, J.B.6
  • 8
    • 73649099860 scopus 로고    scopus 로고
    • Characterization of the key step for light-driven hydrogen evolution in green algae
    • M. Winkler, S. Kuhlgert, M. Hippler, and T. Happe Characterization of the key step for light-driven hydrogen evolution in green algae J Biol Chem 284 2009 36620 36627
    • (2009) J Biol Chem , vol.284 , pp. 36620-36627
    • Winkler, M.1    Kuhlgert, S.2    Hippler, M.3    Happe, T.4
  • 9
    • 0036186921 scopus 로고    scopus 로고
    • Differential regulation of the Fe-hydrogenase during anaerobic adaptation in the green alga Chlamydomonas reinhardtii
    • T. Happe, and A. Kaminski Differential regulation of the Fe-hydrogenase during anaerobic adaptation in the green alga Chlamydomonas reinhardtii Eur J Biochem 269 2002 1022 1032
    • (2002) Eur J Biochem , vol.269 , pp. 1022-1032
    • Happe, T.1    Kaminski, A.2
  • 10
    • 52749087981 scopus 로고    scopus 로고
    • Shewanella oneidensis: A new and efficient system for expression and maturation of heterologous [Fe-Fe] hydrogenase from Chlamydomonas reinhardtii
    • K. Sybirna, T. Antoine, P. Lindberg, V. Fourmond, M. Rousset, and V. Mejean Shewanella oneidensis: a new and efficient system for expression and maturation of heterologous [Fe-Fe] hydrogenase from Chlamydomonas reinhardtii BMC Biotechnol 8 2008 73
    • (2008) BMC Biotechnol , vol.8 , pp. 73
    • Sybirna, K.1    Antoine, T.2    Lindberg, P.3    Fourmond, V.4    Rousset, M.5    Mejean, V.6
  • 11
    • 0026631289 scopus 로고
    • Ferredoxin and flavodoxin from the cyanobacterium Synechocystis sp PCC 6803
    • H. Bottin, and B. Lagoutte Ferredoxin and flavodoxin from the cyanobacterium Synechocystis sp PCC 6803 Biochim Biophys Acta 1101 1992 48 56
    • (1992) Biochim Biophys Acta , vol.1101 , pp. 48-56
    • Bottin, H.1    Lagoutte, B.2
  • 14
    • 32344431599 scopus 로고    scopus 로고
    • Redox interaction of cytochrome c3 with [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F
    • N. Yahata, T. Saitoh, Y. Takayama, K. Ozawa, H. Ogata, and Y. Higuchi Redox interaction of cytochrome c3 with [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F Biochemistry 45 2006 1653 1662
    • (2006) Biochemistry , vol.45 , pp. 1653-1662
    • Yahata, N.1    Saitoh, T.2    Takayama, Y.3    Ozawa, K.4    Ogata, H.5    Higuchi, Y.6
  • 17
    • 33845932878 scopus 로고    scopus 로고
    • Electrochemical investigations of the interconversions between catalytic and inhibited states of the [FeFe]-hydrogenase from Desulfovibrio desulfuricans
    • A. Parkin, C. Cavazza, J.C. Fontecilla-Camps, and F.A. Armstrong Electrochemical investigations of the interconversions between catalytic and inhibited states of the [FeFe]-hydrogenase from Desulfovibrio desulfuricans J Am Chem Soc 128 2006 16808 16815
    • (2006) J Am Chem Soc , vol.128 , pp. 16808-16815
    • Parkin, A.1    Cavazza, C.2    Fontecilla-Camps, J.C.3    Armstrong, F.A.4
  • 18
    • 33646161964 scopus 로고    scopus 로고
    • Changing the ligation of the distal [4Fe4S] cluster in NiFe hydrogenase impairs inter- and intramolecular electron transfers
    • S. Dementin, V. Belle, P. Bertrand, B. Guigliarelli, G. Adryanczyk-Perrier, and A.L. De Lacey Changing the ligation of the distal [4Fe4S] cluster in NiFe hydrogenase impairs inter- and intramolecular electron transfers J Am Chem Soc 128 2006 5209 5218
    • (2006) J Am Chem Soc , vol.128 , pp. 5209-5218
    • Dementin, S.1    Belle, V.2    Bertrand, P.3    Guigliarelli, B.4    Adryanczyk-Perrier, G.5    De Lacey, A.L.6
  • 20
    • 79951841772 scopus 로고    scopus 로고
    • CO disrupts the reduced H-cluster of FeFe hydrogenase. A combined DFT and protein film voltammetry study
    • C. Baffert, L. Bertini, T. Lautier, C. Greco, K. Sybirna, and P. Ezanno CO disrupts the reduced H-cluster of FeFe hydrogenase. A combined DFT and protein film voltammetry study J Am Chem Soc 133 2011 2096 2099
    • (2011) J Am Chem Soc , vol.133 , pp. 2096-2099
    • Baffert, C.1    Bertini, L.2    Lautier, T.3    Greco, C.4    Sybirna, K.5    Ezanno, P.6
  • 21
    • 4644245238 scopus 로고    scopus 로고
    • Inhibition and aerobic inactivation kinetics of Desulfovibrio fructosovorans NiFe hydrogenase studied by protein film voltammetry
    • C. Leger, S. Dementin, P. Bertrand, M. Rousset, and B. Guigliarelli Inhibition and aerobic inactivation kinetics of Desulfovibrio fructosovorans NiFe hydrogenase studied by protein film voltammetry J Am Chem Soc 126 2004 12162 12172
    • (2004) J Am Chem Soc , vol.126 , pp. 12162-12172
    • Leger, C.1    Dementin, S.2    Bertrand, P.3    Rousset, M.4    Guigliarelli, B.5
  • 22
    • 33846273112 scopus 로고    scopus 로고
    • A needle in a haystack: The active site of the membrane-bound complex cytochrome c nitrite reductase
    • M.G. Almeida, C.M. Silveira, B. Guigliarelli, P. Bertrand, J.J. Moura, and I. Moura A needle in a haystack: the active site of the membrane-bound complex cytochrome c nitrite reductase FEBS Lett 581 2007 284 288
    • (2007) FEBS Lett , vol.581 , pp. 284-288
    • Almeida, M.G.1    Silveira, C.M.2    Guigliarelli, B.3    Bertrand, P.4    Moura, J.J.5    Moura, I.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.