메뉴 건너뛰기




Volumn 82, Issue 6, 2006, Pages 1677-1685

Photoinduced hydrogen production by direct electron transfer from photosystem I cross-linked with cytochrome c3 to [NiFe]-hydrogenase

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CYTOCHROME C; CYTOCHROME C(3); HYDROGEN; HYDROGENASE; NICKEL IRON HYDROGENASE; NICKEL-IRON HYDROGENASE; PRIMER DNA; PROTEIN SUBUNIT; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 33846469977     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1562/2006-05-07-RA-893     Document Type: Article
Times cited : (56)

References (43)
  • 1
    • 0032856298 scopus 로고    scopus 로고
    • Photobiological hydrogen production
    • Asada, Y. and J. Miyake (1999) Photobiological hydrogen production. J. Biosci. Bioeng. 88, 1-6.
    • (1999) J. Biosci. Bioeng , vol.88 , pp. 1-6
    • Asada, Y.1    Miyake, J.2
  • 3
    • 29944442773 scopus 로고    scopus 로고
    • Genomics of green algal hydrogen research
    • Melis, A., M. Seibert and T. Happe (2004) Genomics of green algal hydrogen research. Photosynth. Res. 82, 277-288.
    • (2004) Photosynth. Res , vol.82 , pp. 277-288
    • Melis, A.1    Seibert, M.2    Happe, T.3
  • 5
    • 0037203077 scopus 로고    scopus 로고
    • Hydrogen production by cyanobacteria in an automated outdoor photobioreactor under aerobic conditions
    • Tsygankov, A. A., S. Fedorov, S. N. Kosourov and K. K. Rao (2002) Hydrogen production by cyanobacteria in an automated outdoor photobioreactor under aerobic conditions. Biotechnol. Bioeng. 80, 777-783.
    • (2002) Biotechnol. Bioeng , vol.80 , pp. 777-783
    • Tsygankov, A.A.1    Fedorov, S.2    Kosourov, S.N.3    Rao, K.K.4
  • 6
    • 0036827173 scopus 로고    scopus 로고
    • Photobiological hydrogen production: Photochemical efficiency and bioreactor design
    • Akkerman, I., M. Janssen, J. Rocha and R. H. Wijffels (2002) Photobiological hydrogen production: Photochemical efficiency and bioreactor design. Int. J. Hydrogen Energy 27, 1195-1208.
    • (2002) Int. J. Hydrogen Energy , vol.27 , pp. 1195-1208
    • Akkerman, I.1    Janssen, M.2    Rocha, J.3    Wijffels, R.H.4
  • 7
    • 0026097297 scopus 로고
    • Ferredoxin-dependent chloroplast enzymes
    • Knaff, D. B. and M. Hirasawa (1991) Ferredoxin-dependent chloroplast enzymes. Biochim. Biophys. Acta 1056, 93-125.
    • (1991) Biochim. Biophys. Acta , vol.1056 , pp. 93-125
    • Knaff, D.B.1    Hirasawa, M.2
  • 8
    • 0035976018 scopus 로고    scopus 로고
    • Ferredoxin and flavodoxin reduction by photosystem I
    • Sétif, P. (2001) Ferredoxin and flavodoxin reduction by photosystem I. Biochim. Biophys. Acta 1507, 161-179.
    • (2001) Biochim. Biophys. Acta , vol.1507 , pp. 161-179
    • Sétif, P.1
  • 10
    • 0034082075 scopus 로고    scopus 로고
    • The bidirectional hydrogenase of Synechocystis sp. PCC 6803 works as an electron valve during photosynthesis
    • Appel, J., S. Phunpruch, K. Steinmüller, and R. Schulz (2000) The bidirectional hydrogenase of Synechocystis sp. PCC 6803 works as an electron valve during photosynthesis. Arch. Microbiol. 173, 333-338.
    • (2000) Arch. Microbiol , vol.173 , pp. 333-338
    • Appel, J.1    Phunpruch, S.2    Steinmüller, K.3    Schulz, R.4
  • 12
    • 0035927420 scopus 로고    scopus 로고
    • Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution
    • Jordan, P., P. Fromme, H. T. Witt, O. Klukas, W. Saenger and N. Krauss (2001) Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution. Nature 411, 909-917.
    • (2001) Nature , vol.411 , pp. 909-917
    • Jordan, P.1    Fromme, P.2    Witt, H.T.3    Klukas, O.4    Saenger, W.5    Krauss, N.6
  • 13
    • 0029944853 scopus 로고    scopus 로고
    • Characterization of a redox active cross-linked complex between cyanobacterial photosystem I and soluble ferredoxin
    • Lelong, C., E. J. Boekema, J. Kruip, H. Bottin, M. Rögner and P. Setif (1996) Characterization of a redox active cross-linked complex between cyanobacterial photosystem I and soluble ferredoxin. EMBO J. 15, 2160-2168.
    • (1996) EMBO J , vol.15 , pp. 2160-2168
    • Lelong, C.1    Boekema, E.J.2    Kruip, J.3    Bottin, H.4    Rögner, M.5    Setif, P.6
  • 14
    • 0027480340 scopus 로고
    • Small subunits of photosystem I reaction center complexes from Synechococcus elongatus. II. The psaE gene product has a role to promote interaction between the terminal electron acceptor and ferredoxin
    • Sonoike, K., H. Hatanaka and S. Katoh (1993) Small subunits of photosystem I reaction center complexes from Synechococcus elongatus. II. The psaE gene product has a role to promote interaction between the terminal electron acceptor and ferredoxin. Biochim. Biophys. Acta 1141, 52-57.
    • (1993) Biochim. Biophys. Acta , vol.1141 , pp. 52-57
    • Sonoike, K.1    Hatanaka, H.2    Katoh, S.3
  • 15
    • 0027161399 scopus 로고
    • On the function of subunit PsaE in chloroplast photosystem I
    • Weber, N. and H. Strotmann (1993) On the function of subunit PsaE in chloroplast photosystem I. Biochim. Biophys. Acta 1143, 204-210.
    • (1993) Biochim. Biophys. Acta , vol.1143 , pp. 204-210
    • Weber, N.1    Strotmann, H.2
  • 16
    • 2142653130 scopus 로고    scopus 로고
    • Molecular biology of microbial hydrogenases
    • Vignais, P. M. and A. Colbeau (2004) Molecular biology of microbial hydrogenases. Curr. Issues Mol. Biol. 6, 159-188.
    • (2004) Curr. Issues Mol. Biol , vol.6 , pp. 159-188
    • Vignais, P.M.1    Colbeau, A.2
  • 17
    • 0028568063 scopus 로고
    • Nickel hydrogenases: In search of the active site
    • Albracht, S. P. J. (1994) Nickel hydrogenases: In search of the active site. Biochim. Biophys. Acta 1188, 167-204.
    • (1994) Biochim. Biophys. Acta , vol.1188 , pp. 167-204
    • Albracht, S.P.J.1
  • 19
    • 0031756314 scopus 로고    scopus 로고
    • Electron transfer between hydrogenases and mono- and multiheme cytochromes in Desulfovibrio ssp
    • Pereira, I. A., C. V. Romão, A. V. Xavier, J. LeGall and M. Teixeira (1998) Electron transfer between hydrogenases and mono- and multiheme cytochromes in Desulfovibrio ssp. J. Biol. Inorg. Chem. 3, 494-498.
    • (1998) J. Biol. Inorg. Chem , vol.3 , pp. 494-498
    • Pereira, I.A.1    Romão, C.V.2    Xavier, A.V.3    LeGall, J.4    Teixeira, M.5
  • 20
    • 0019802315 scopus 로고
    • Hydrogen cycling as a general mechanism for energy coupling in the sulfate-reducing bacteria, Desulfovibrio sp
    • Odom, J. M. and H. D. Peck, Jr. (1981) Hydrogen cycling as a general mechanism for energy coupling in the sulfate-reducing bacteria, Desulfovibrio sp. FEMS Microbiol. Lett. 12, 47-50.
    • (1981) FEMS Microbiol. Lett , vol.12 , pp. 47-50
    • Odom, J.M.1    Peck Jr., H.D.2
  • 27
    • 0033988688 scopus 로고    scopus 로고
    • A sequential electron transfer from hydrogenases to cytochromes in sulfate-reducing bacteria
    • Aubert, C., M. Brugna, A. Dolla, M. Bruschi and M. T. Giudici-Orticoni (2000) A sequential electron transfer from hydrogenases to cytochromes in sulfate-reducing bacteria. Biochim. Biophys. Acta 1476, 85-92.
    • (2000) Biochim. Biophys. Acta , vol.1476 , pp. 85-92
    • Aubert, C.1    Brugna, M.2    Dolla, A.3    Bruschi, M.4    Giudici-Orticoni, M.T.5
  • 30
    • 0037125959 scopus 로고    scopus 로고
    • The stable assembly of newly synthesized PsaE into the photosystem I complex occurring via the exchange mechanism is facilitated by electrostatic interactions
    • Lushy, A., L. Verchovsky and R. Nechushtai (2002) The stable assembly of newly synthesized PsaE into the photosystem I complex occurring via the exchange mechanism is facilitated by electrostatic interactions. Biochemistry 41, 11192-11199.
    • (2002) Biochemistry , vol.41 , pp. 11192-11199
    • Lushy, A.1    Verchovsky, L.2    Nechushtai, R.3
  • 31
    • 0027692693 scopus 로고
    • Stable assembly of PsaE into cyanobacterial photosynthetic membranes is dependent on the presence of other accessory subunits of photosystem I
    • Cohen, Y., V. P. Chitnis, R. Nechushtai and P. R. Chitnis (1993) Stable assembly of PsaE into cyanobacterial photosynthetic membranes is dependent on the presence of other accessory subunits of photosystem I. Plant Mol. Biol. 23, 895-900.
    • (1993) Plant Mol. Biol , vol.23 , pp. 895-900
    • Cohen, Y.1    Chitnis, V.P.2    Nechushtai, R.3    Chitnis, P.R.4
  • 32
    • 0034629486 scopus 로고    scopus 로고
    • Essential role of a single arginine of photosystem I in stabilizing the electron transfer complex with ferredoxin
    • Barth, P., I. Guillouard, P. Setif and B. Lagoutte (2000) Essential role of a single arginine of photosystem I in stabilizing the electron transfer complex with ferredoxin. J. Biol. Chem. 275, 7030-7036.
    • (2000) J. Biol. Chem , vol.275 , pp. 7030-7036
    • Barth, P.1    Guillouard, I.2    Setif, P.3    Lagoutte, B.4
  • 33
    • 0024962577 scopus 로고
    • Structure and targeted mutagenesis of the gene encoding 8-kDa subunit of photosystem I from the cyanobacterium Synechocystis sp. PCC 6803
    • Chitnis, P. R., P. A. Reilly, M. C. Miedel and N. Nelson (1989) Structure and targeted mutagenesis of the gene encoding 8-kDa subunit of photosystem I from the cyanobacterium Synechocystis sp. PCC 6803. J. Biol. Chem. 264, 18374-18380.
    • (1989) J. Biol. Chem , vol.264 , pp. 18374-18380
    • Chitnis, P.R.1    Reilly, P.A.2    Miedel, M.C.3    Nelson, N.4
  • 34
    • 0025204752 scopus 로고
    • Redox process of iron-sulfur clusters of the soluble-domain of the membrane-bound hydrogenase from Desulfovibrio vulgaris Miyazaki F studied by resonance Raman spectroscopy
    • Furuichi, H., Y. Ozaki, K. Niki, and H. Akutsu (1990) Redox process of iron-sulfur clusters of the soluble-domain of the membrane-bound hydrogenase from Desulfovibrio vulgaris Miyazaki F studied by resonance Raman spectroscopy. J. Biochem. Tokyo 108, 707-710.
    • (1990) J. Biochem. Tokyo , vol.108 , pp. 707-710
    • Furuichi, H.1    Ozaki, Y.2    Niki, K.3    Akutsu, H.4
  • 35
    • 0035229710 scopus 로고    scopus 로고
    • A simple, rapid, and highly efficient gene expression system for multiheme cytochrome c
    • Ozawa, K., F. Yasukawa, Y. Fujiwara and H. Akutsu (2001) A simple, rapid, and highly efficient gene expression system for multiheme cytochrome c. Biosci. Biotechnol. Biochem. 65, 185-189.
    • (2001) Biosci. Biotechnol. Biochem , vol.65 , pp. 185-189
    • Ozawa, K.1    Yasukawa, F.2    Fujiwara, Y.3    Akutsu, H.4
  • 38
    • 0033014401 scopus 로고    scopus 로고
    • Targeted inactivation of the gene psaK encoding a subunit of photosystem I from the cyanobacterium Synechocystis sp. PCC 6803
    • Nakamoto, H. and M. Hasegawa (1999) Targeted inactivation of the gene psaK encoding a subunit of photosystem I from the cyanobacterium Synechocystis sp. PCC 6803. Plant Cell Physiol. 40, 9-16.
    • (1999) Plant Cell Physiol , vol.40 , pp. 9-16
    • Nakamoto, H.1    Hasegawa, M.2
  • 39
    • 0000411157 scopus 로고
    • Absorption of light by chlorophyll solutions
    • MacKinney, G. (1941) Absorption of light by chlorophyll solutions. J. Biol. Chem. 140, 315-322.
    • (1941) J. Biol. Chem , vol.140 , pp. 315-322
    • MacKinney, G.1
  • 40
    • 0037172810 scopus 로고    scopus 로고
    • Proteomic analysis of a highly active photosystem II preparation from the cyanobacterium Synechocystis sp. PCC 6803 reveals the presence of novel polypeptides
    • Kashino, Y., W. M. Lauber, J. A. Carroll, Q. Wang, J. Whitmarsh, K. Satoh and H. B. Pakrashi (2002) Proteomic analysis of a highly active photosystem II preparation from the cyanobacterium Synechocystis sp. PCC 6803 reveals the presence of novel polypeptides. Biochemistry 41, 8004-8012.
    • (2002) Biochemistry , vol.41 , pp. 8004-8012
    • Kashino, Y.1    Lauber, W.M.2    Carroll, J.A.3    Wang, Q.4    Whitmarsh, J.5    Satoh, K.6    Pakrashi, H.B.7
  • 41
    • 0038392590 scopus 로고    scopus 로고
    • Reversed-phase HPLC determination of chlorophyll a′ and phylloquinone in Photosystem I of oxygenic photosynthetic organisms. Universal existence of one chlorophyll a′ molecule in Photosystem I
    • Nakamura, A., M. Akai, E. Yoshida, T. Taki and T. Watanabe (2003) Reversed-phase HPLC determination of chlorophyll a′ and phylloquinone in Photosystem I of oxygenic photosynthetic organisms. Universal existence of one chlorophyll a′ molecule in Photosystem I. Eur. J. Biochem. 270, 2446-2458.
    • (2003) Eur. J. Biochem , vol.270 , pp. 2446-2458
    • Nakamura, A.1    Akai, M.2    Yoshida, E.3    Taki, T.4    Watanabe, T.5
  • 42
    • 0033532162 scopus 로고    scopus 로고
    • 6 from Synechocystis sp. PCC 6803. The heme protein possesses a negatively charged area that may be isofunctional with the acidic patch of plastocyanin
    • 6 from Synechocystis sp. PCC 6803. The heme protein possesses a negatively charged area that may be isofunctional with the acidic patch of plastocyanin. J. Biol. Chem. 274, 13292-13297.
    • (1999) J. Biol. Chem , vol.274 , pp. 13292-13297
    • Cerda1    la, B.D.2    Díaz-Quintana, A.3    Navarro, J.A.4    Hárvas, M.5    la Rosa, M.A.D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.