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Volumn 289, Issue 4, 2014, Pages 1930-1937

The bidirectional NiFe-hydrogenase in synechocystis sp. PCC 6803 Is reduced by flavodoxin and ferredoxin and is essential under mixotrophic, nitrate-limiting conditions

Author keywords

[No Author keywords available]

Indexed keywords

ELECTRON SINK; FLAVODOXIN; HYDROGENASES; MIXOTROPHIC; NAD(P)H; PHYSIOLOGICAL FUNCTIONS; SYNECHOCYSTIS SP. PCC 6803;

EID: 84893141463     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.526376     Document Type: Article
Times cited : (111)

References (52)
  • 1
    • 35748974830 scopus 로고    scopus 로고
    • Occurrence, classification, and biological function of hydrogenases: An overview
    • Vignais, P. M., and Billoud, B. (2007) Occurrence, classification, and biological function of hydrogenases: an overview. Chem. Rev. 107, 4206-4272
    • (2007) Chem. Rev. , vol.107 , pp. 4206-4272
    • Vignais, P.M.1    Billoud, B.2
  • 2
    • 0034082075 scopus 로고    scopus 로고
    • The bidirectional hydrogenase of Synechocystis sp. PCC 6803 works as an electron valve during photosynthesis
    • Appel, J., Phunpruch, S., Steinmüller, K., and Schulz, R. (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
  • 3
    • 1542286924 scopus 로고    scopus 로고
    • Sustained photoevolution of molecular hydrogen in a mutant of Synechocystis sp strain PCC 6803 deficient in the type i NADPH-dehydrogenase complex
    • Cournac, L., Guedeney, G., Peltier, G., and Vignais, P. M. (2004) Sustained photoevolution of molecular hydrogen in a mutant of Synechocystis sp. strain PCC 6803 deficient in the type I NADPH-dehydrogenase complex. J. Bacteriol. 186, 1737-1746
    • (2004) J. Bacteriol. , vol.186 , pp. 1737-1746
    • Cournac, L.1    Guedeney, G.2    Peltier, G.3    Vignais, P.M.4
  • 4
  • 6
    • 0035913370 scopus 로고    scopus 로고
    • The role of microbial mats in the production of reduced gases on the early Earth
    • Hoehler, T. M., Bebout, B. M., and Des Marais, D. J. (2001) The role of microbial mats in the production of reduced gases on the early Earth. Nature 412, 324-327
    • (2001) Nature , vol.412 , pp. 324-327
    • Hoehler, T.M.1    Bebout, B.M.2    Des Marais, D.J.3
  • 8
    • 0019436382 scopus 로고
    • Comparative characterization of 2 distinct hydrogenases from Anabaena sp strain 7120
    • Houchins, J. P., and Burris, R. H. (1981) Comparative characterization of 2 distinct hydrogenases from Anabaena sp. strain 7120. J. Bacteriol. 146, 215-221
    • (1981) J. Bacteriol. , vol.146 , pp. 215-221
    • Houchins, J.P.1    Burris, R.H.2
  • 9
    • 0018153934 scopus 로고
    • Characterization of hydrogenases from blue-green algae
    • Llama, M. J., Serra, J. L., Rao, K. K., and Hall, D. O. (1978) Characterization of hydrogenases from blue-green algae. Biochem. Soc. Trans. 6, 1337-1339
    • (1978) Biochem. Soc. Trans. , vol.6 , pp. 1337-1339
    • Llama, M.J.1    Serra, J.L.2    Rao, K.K.3    Hall, D.O.4
  • 10
    • 0030571582 scopus 로고    scopus 로고
    • Sequence analysis of an operon of a NAD(P)-reducing nickel hydrogenase from the cyanobacterium Synechocystis sp. PCC 6803 gives additional evidence for direct coupling of the enzyme to NAD(P)H-dehydrogenase (complex I)
    • Appel, J., and Schulz, R. (1996) Sequence analysis of an operon of a NAD(P)-reducing nickel hydrogenase from the cyanobacterium Synechocystis sp. PCC 6803 gives additional evidence for direct coupling of the enzyme to NAD(P)H-dehydrogenase (complex I). Biochim. Biophys. Acta 1298, 141-147
    • (1996) Biochim. Biophys. Acta , vol.1298 , pp. 141-147
    • Appel, J.1    Schulz, R.2
  • 12
    • 0030024964 scopus 로고    scopus 로고
    • NAD(P)+-dependent hydrogenase activity in extracts from the cyanobacterium Anacystis nidulans
    • Schmitz, O., and Bothe, H. (1996) NAD(P)+-dependent hydrogenase activity in extracts from the cyanobacterium Anacystis nidulans. FEMS Microbiol. Lett. 135, 97-101
    • (1996) FEMS Microbiol. Lett. , vol.135 , pp. 97-101
    • Schmitz, O.1    Bothe, H.2
  • 13
    • 80255124825 scopus 로고    scopus 로고
    • Role of HoxE subunit in Synechocystis PCC6803 hydrogenase
    • Aubert-Jousset, E., Cano, M., Guedeney, G., Richaud, P., and Cournac, L. (2011) Role of HoxE subunit in Synechocystis PCC6803 hydrogenase. FEBS J. 278, 4035-4043
    • (2011) FEBS J. , vol.278 , pp. 4035-4043
    • Aubert-Jousset, E.1    Cano, M.2    Guedeney, G.3    Richaud, P.4    Cournac, L.5
  • 14
    • 0037156874 scopus 로고    scopus 로고
    • HoxE: A subunit specific for the pentameric bidirectional hydrogenase complex (HoxEFUYH) of cyanobacteria
    • Schmitz, O., Boison, G., Salzmann, H., Bothe, H., Schütz, K., Wang, S. H., and Happe, T. (2002) HoxE: a subunit specific for the pentameric bidirectional hydrogenase complex (HoxEFUYH) of cyanobacteria. Biochim. Biophys. Acta 1554, 66-74
    • (2002) Biochim. Biophys. Acta , vol.1554 , pp. 66-74
    • Schmitz, O.1    Boison, G.2    Salzmann, H.3    Bothe, H.4    Schütz, K.5    Wang, S.H.6    Happe, T.7
  • 15
    • 33845659481 scopus 로고    scopus 로고
    • Characterization of catalytic properties of hydrogenase isolated from the unicellular cyanobacterium Gloeocapsa alpicola CALU 743
    • Serebriakova, L. T., and Sheremet'eva, M. E. (2006) Characterization of catalytic properties of hydrogenase isolated from the unicellular cyanobacterium Gloeocapsa alpicola CALU 743. Biochemistry 71, 1370-1376
    • (2006) Biochemistry , vol.71 , pp. 1370-1376
    • Serebriakova, L.T.1    Sheremet'Eva, M.E.2
  • 16
    • 33845355867 scopus 로고    scopus 로고
    • Characterization of a HoxEFUYH type of [NiFe] hydrogenase from Allochromatium vinosum and some EPR and IR properties of the hydrogenase module
    • Long, M., Liu, J., Chen, Z., Bleijlevens, B., Roseboom, W., and Albracht, S. P. (2007) Characterization of a HoxEFUYH type of [NiFe] hydrogenase from Allochromatium vinosum and some EPR and IR properties of the hydrogenase module. J. Biol. Inorg. Chem. 12, 62-78
    • (2007) J. Biol. Inorg. Chem. , vol.12 , pp. 62-78
    • Long, M.1    Liu, J.2    Chen, Z.3    Bleijlevens, B.4    Roseboom, W.5    Albracht, S.P.6
  • 18
    • 0021753750 scopus 로고
    • Content and localization of FMN, F3-S clusters and nickel in the NAD-linked hydrogenase of Nocardia opaca 1B
    • Schneider, K., Cammack, R., and Schlegel, H. G. (1984) Content and localization of FMN, F3-S clusters and nickel in the NAD-linked hydrogenase of Nocardia opaca 1B. Eur. J. Biochem. 142, 75-84
    • (1984) Eur. J. Biochem. , vol.142 , pp. 75-84
    • Schneider, K.1    Cammack, R.2    Schlegel, H.G.3
  • 19
    • 73649123872 scopus 로고    scopus 로고
    • Overexpression, isolation, and spectroscopic characterization of the bidirectional [NiFe] hydrogenase from Synechocystis sp. PCC 6803
    • Germer, F., Zebger, I., Saggu, M., Lendzian, F., Schulz, R., and Appel, J. (2009) Overexpression, isolation, and spectroscopic characterization of the bidirectional [NiFe] hydrogenase from Synechocystis sp. PCC 6803. J. Biol. Chem. 284, 36462-36472
    • (2009) J. Biol. Chem. , vol.284 , pp. 36462-36472
    • Germer, F.1    Zebger, I.2    Saggu, M.3    Lendzian, F.4    Schulz, R.5    Appel, J.6
  • 20
    • 0001280606 scopus 로고
    • Localization of the reversible hydrogenase of cyanobacteria
    • Kentemich, T., Bahnweg, M., Mayer, F., and Bothe, H. (1989) Localization of the reversible hydrogenase of cyanobacteria. Z. Naturforsch. 44, 384-391
    • (1989) Z. Naturforsch. , vol.44 , pp. 384-391
    • Kentemich, T.1    Bahnweg, M.2    Mayer, F.3    Bothe, H.4
  • 21
    • 84871543231 scopus 로고    scopus 로고
    • Genetic analysis of the Hox hydrogenase in the cyanobacterium Synechocystis sp. PCC 6803 reveals subunit roles in association, assembly, maturation, and function
    • Eckert, C., Boehm, M., Carrieri, D., Yu, J., Dubini, A., Nixon, P. J., and Maness, P. C. (2012) Genetic analysis of the Hox hydrogenase in the cyanobacterium Synechocystis sp. PCC 6803 reveals subunit roles in association, assembly, maturation, and function. J. Biol. Chem. 287, 43502-43515
    • (2012) J. Biol. Chem. , vol.287 , pp. 43502-43515
    • Eckert, C.1    Boehm, M.2    Carrieri, D.3    Yu, J.4    Dubini, A.5    Nixon, P.J.6    Maness, P.C.7
  • 22
    • 0013797725 scopus 로고
    • Hydrogenase and NADP-reduction reactions by a cell-free preparation of Anabaena cylindrica
    • Fujita, Y., and Myers, J. (1965) Hydrogenase and NADP-reduction reactions by a cell-free preparation of Anabaena cylindrica. Arch. Biochem. Biophys. 111, 619-625
    • (1965) Arch. Biochem. Biophys. , vol.111 , pp. 619-625
    • Fujita, Y.1    Myers, J.2
  • 23
    • 33847137761 scopus 로고    scopus 로고
    • Inhibition of respiration and nitrate assimilation enhances photohydrogen evolution under low oxygen concentrations in Synechocystis sp. PCC 6803
    • Gutthann, F., Egert, M., Marques, A., and Appel, J. (2007) Inhibition of respiration and nitrate assimilation enhances photohydrogen evolution under low oxygen concentrations in Synechocystis sp. PCC 6803. Biochim. Biophys. Acta 1767, 161-169
    • (2007) Biochim. Biophys. Acta , vol.1767 , pp. 161-169
    • Gutthann, F.1    Egert, M.2    Marques, A.3    Appel, J.4
  • 24
    • 84867644452 scopus 로고    scopus 로고
    • Diversity in hydrogen evolution from bidirectional hydrogenases in cyanobacteria from terrestrial, freshwater and marine intertidal environments
    • Kothari, A., Potrafka, R., and Garcia-Pichel, F. (2012) Diversity in hydrogen evolution from bidirectional hydrogenases in cyanobacteria from terrestrial, freshwater and marine intertidal environments. J. Biotechnol. 162, 105-114
    • (2012) J. Biotechnol. , vol.162 , pp. 105-114
    • Kothari, A.1    Potrafka, R.2    Garcia-Pichel, F.3
  • 25
    • 68049100110 scopus 로고    scopus 로고
    • Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli
    • Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., and Rabinowitz, J. D. (2009) Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli. Nat. Chem. Biol. 5, 593-599
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 593-599
    • Bennett, B.D.1    Kimball, E.H.2    Gao, M.3    Osterhout, R.4    Van Dien, S.J.5    Rabinowitz, J.D.6
  • 26
    • 0032906898 scopus 로고    scopus 로고
    • The steady-state internal redox state (NADH/NAD) reflects the external redox state and is correlated with catabolic adaptation in Escherichia coli
    • de Graef, M. R., Alexeeva, S., Snoep, J. L., and Teixeira de Mattos, M. J. (1999) The steady-state internal redox state (NADH/NAD) reflects the external redox state and is correlated with catabolic adaptation in Escherichia coli. J. Bacteriol. 181, 2351-2357
    • (1999) J. Bacteriol. , vol.181 , pp. 2351-2357
    • De Graef, M.R.1    Alexeeva, S.2    Snoep, J.L.3    Teixeira De Mattos, M.J.4
  • 27
    • 83055188821 scopus 로고    scopus 로고
    • Metabolome remodeling during the acidogenic-solventogenic transition in Clostridium acetobutylicum
    • Amador-Noguez, D., Brasg, I. A., Feng, X. J., Roquet, N., and Rabinowitz, J. D. (2011) Metabolome remodeling during the acidogenic-solventogenic transition in Clostridium acetobutylicum. Appl. Environ. Microbiol. 77, 7984-7997
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 7984-7997
    • Amador-Noguez, D.1    Brasg, I.A.2    Feng, X.J.3    Roquet, N.4    Rabinowitz, J.D.5
  • 28
    • 0014556275 scopus 로고
    • Respiration in blue-green algae
    • Biggins, J. (1969) Respiration in blue-green algae. J. Bacteriol. 99, 570-575
    • (1969) J. Bacteriol. , vol.99 , pp. 570-575
    • Biggins, J.1
  • 29
    • 0032475858 scopus 로고    scopus 로고
    • 2D-isolation of pure plasma and thylakoid membranes from the cyanobacterium Synechocystis sp. PCC 6803
    • Norling, B., Zak, E., Andersson, B., and Pakrasi, H. (1998) 2D-isolation of pure plasma and thylakoid membranes from the cyanobacterium Synechocystis sp. PCC 6803. FEBS Lett. 436, 189-192
    • (1998) FEBS Lett. , vol.436 , pp. 189-192
    • Norling, B.1    Zak, E.2    Andersson, B.3    Pakrasi, H.4
  • 30
    • 33748748114 scopus 로고    scopus 로고
    • Mutagenesis of hydrogenase accessory genes of Synechocystis sp. PCC 6803
    • Hoffmann, D., Gutekunst, K., Klissenbauer, M., Schulz-Friedrich, R., and Appel, J. (2006) Mutagenesis of hydrogenase accessory genes of Synechocystis sp. PCC 6803. FEBS J. 273, 4516-4527
    • (2006) FEBS J. , vol.273 , pp. 4516-4527
    • Hoffmann, D.1    Gutekunst, K.2    Klissenbauer, M.3    Schulz-Friedrich, R.4    Appel, J.5
  • 31
    • 34548593310 scopus 로고    scopus 로고
    • Complete activity profile of Clostridium acetobutylicum FeFe-hydrogenase and kinetic parameters for endogenous redox partners
    • Demuez, M., Cournac, L., Guerrini, O., Soucaille, P., and Girbal, L. (2007) Complete activity profile of Clostridium acetobutylicum FeFe-hydrogenase and kinetic parameters for endogenous redox partners. FEMS Microbiol. Lett. 275, 113-121
    • (2007) FEMS Microbiol. Lett. , vol.275 , pp. 113-121
    • Demuez, M.1    Cournac, L.2    Guerrini, O.3    Soucaille, P.4    Girbal, L.5
  • 32
    • 0033214609 scopus 로고    scopus 로고
    • Purification and catalytic properties of Ech hydrogenase from Methanosarcina barkeri
    • Meuer, J., Bartoschek, S., Koch, J., Künkel, A., and Hedderich, R. (1999) Purification and catalytic properties of Ech hydrogenase from Methanosarcina barkeri. Eur. J. Biochem. 265, 325-335
    • (1999) Eur. J. Biochem. , vol.265 , pp. 325-335
    • Meuer, J.1    Bartoschek, S.2    Koch, J.3    Künkel, A.4    Hedderich, R.5
  • 33
    • 73649099860 scopus 로고    scopus 로고
    • Characterization of the key step for light-driven hydrogen evolution in green algae
    • Winkler, M., Kuhlgert, S., Hippler, M., and Happe, T. (2009) Characterization of the key step for light-driven hydrogen evolution in green algae. J. Biol. Chem. 284, 36620-36627
    • (2009) J. Biol. Chem. , vol.284 , pp. 36620-36627
    • Winkler, M.1    Kuhlgert, S.2    Hippler, M.3    Happe, T.4
  • 34
    • 84871712835 scopus 로고    scopus 로고
    • Energy conservation via electron bifurcating ferredoxin reduction and proton/Na+ translocating ferredoxin oxidation
    • Buckel, W., and Thauer, R. K. (2013) Energy conservation via electron bifurcating ferredoxin reduction and proton/Na+ translocating ferredoxin oxidation. Biochim. Biophys. Acta 1827, 94-113
    • (2013) Biochim. Biophys. Acta , vol.1827 , pp. 94-113
    • Buckel, W.1    Thauer, R.K.2
  • 35
    • 0031803632 scopus 로고    scopus 로고
    • Targeted deletion and mutational analysis of the essential (2Fe-2S) plant-like ferredoxin in Synechocystis PCC 6803 by plasmid shuffling
    • Poncelet, M., Cassier-Chauvat, C., Leschelle, X., Bottin, H., and Chauvat, F. (1998) Targeted deletion and mutational analysis of the essential (2Fe-2S) plant-like ferredoxin in Synechocystis PCC 6803 by plasmid shuffling. Mol. Microbiol. 28, 813-821
    • (1998) Mol. Microbiol. , vol.28 , pp. 813-821
    • Poncelet, M.1    Cassier-Chauvat, C.2    Leschelle, X.3    Bottin, H.4    Chauvat, F.5
  • 36
    • 0020485044 scopus 로고
    • The pyruvate-ferredoxin oxidoreductase in heterocysts of the cyanobacterium Anabaena cylindrica
    • Neuer, G., and Bothe, H. (1982) The pyruvate-ferredoxin oxidoreductase in heterocysts of the cyanobacterium Anabaena cylindrica. Biochim. Biophys. Acta 716, 358-365
    • (1982) Biochim. Biophys. Acta , vol.716 , pp. 358-365
    • Neuer, G.1    Bothe, H.2
  • 37
    • 79953282177 scopus 로고    scopus 로고
    • Characterization of a nifJ mutant of Synechococcus sp strain PCC 7002 lacking pyruvate:ferredoxin oxidoreductase
    • McNeely, K., Xu, Y., Ananyev, G., Bennette, N., Bryant, D. A., and Dismukes, G. C. (2011) Characterization of a nifJ mutant of Synechococcus sp. strain PCC 7002 lacking pyruvate:ferredoxin oxidoreductase. Appl. Environ. Microbiol. 77, 2435-2444
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 2435-2444
    • McNeely, K.1    Xu, Y.2    Ananyev, G.3    Bennette, N.4    Bryant, D.A.5    Dismukes, G.C.6
  • 38
    • 3042653666 scopus 로고    scopus 로고
    • Response of bacteria to simulated upwelling phytoplankton blooms
    • Wetz, M. S., and Wheeler, P. A. (2004) Response of bacteria to simulated upwelling phytoplankton blooms. Mar. Ecol. Prog. Ser. 272, 49-57
    • (2004) Mar. Ecol. Prog. Ser. , vol.272 , pp. 49-57
    • Wetz, M.S.1    Wheeler, P.A.2
  • 40
    • 34249669794 scopus 로고    scopus 로고
    • DONas a source of bioavailable nitrogen for phytoplankton
    • Bronk, D. A., See, J. H., Bradley, P., and Killberg, L. (2007)DONas a source of bioavailable nitrogen for phytoplankton. Biogeosciences 4, 283-296
    • (2007) Biogeosciences , vol.4 , pp. 283-296
    • Bronk, D.A.1    See, J.H.2    Bradley, P.3    Killberg, L.4
  • 41
    • 84855285773 scopus 로고    scopus 로고
    • Bacterial community transcription patterns during a marine phytoplankton bloom
    • Rinta-Kanto, J. M., Sun, S., Sharma, S., Kiene, R. P., and Moran, M. A. (2012) Bacterial community transcription patterns during a marine phytoplankton bloom. Environ. Microbiol. 14, 228-239
    • (2012) Environ. Microbiol. , vol.14 , pp. 228-239
    • Rinta-Kanto, J.M.1    Sun, S.2    Sharma, S.3    Kiene, R.P.4    Moran, M.A.5
  • 42
    • 34547092918 scopus 로고    scopus 로고
    • Regulation of photosynthesis in the unicellular acidophilic red alga Galdieria sulphuraria
    • Oesterhelt, C., Schmälzlin, E., Schmitt, J. M., and Lokstein, H. (2007) Regulation of photosynthesis in the unicellular acidophilic red alga Galdieria sulphuraria. Plant J. 51, 500-511
    • (2007) Plant J. , vol.51 , pp. 500-511
    • Oesterhelt, C.1    Schmälzlin, E.2    Schmitt, J.M.3    Lokstein, H.4
  • 43
    • 0031037399 scopus 로고    scopus 로고
    • Amino acid transport in taxonomically diverse cyanobacteria and identification of two genes encoding elements of a neutral amino acid permease putatively involved in recapture of leaked hydrophobic amino acids
    • Montesinos, M. L., Herrero, A., and Flores, E. (1997) Amino acid transport in taxonomically diverse cyanobacteria and identification of two genes encoding elements of a neutral amino acid permease putatively involved in recapture of leaked hydrophobic amino acids. J. Bacteriol. 179, 853-862
    • (1997) J. Bacteriol. , vol.179 , pp. 853-862
    • Montesinos, M.L.1    Herrero, A.2    Flores, E.3
  • 44
    • 0037313141 scopus 로고    scopus 로고
    • High rate of uptake of organic nitrogen compounds by Prochlorococcus cyanobacteria as a key to their dominance in oligotrophic oceanic waters
    • Zubkov, M. V., Fuchs, B. M., Tarran, G. A., Burkill, P. H., and Amann, R. (2003) High rate of uptake of organic nitrogen compounds by Prochlorococcus cyanobacteria as a key to their dominance in oligotrophic oceanic waters. Appl. Environ. Microbiol. 69, 1299-1304
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 1299-1304
    • Zubkov, M.V.1    Fuchs, B.M.2    Tarran, G.A.3    Burkill, P.H.4    Amann, R.5
  • 45
    • 0018409915 scopus 로고
    • Generic assignments, strain histories and properties of pure cultures of cyanobacteria
    • Rippka, R., Deruelles, J., Waterbury, J. B., Herdman, M., and Stanier, R. Y. (1979) Generic assignments, strain histories and properties of pure cultures of cyanobacteria. J. Gen. Microbiol. 111, 1-61
    • (1979) J. Gen. Microbiol. , vol.111 , pp. 1-61
    • Rippka, R.1    Deruelles, J.2    Waterbury, J.B.3    Herdman, M.4    Stanier, R.Y.5
  • 47
    • 51649123143 scopus 로고    scopus 로고
    • High bacterivory by the smallest phytoplankton in the North Atlantic Ocean
    • Zubkov, M. V., and Tarran, G. A. (2008) High bacterivory by the smallest phytoplankton in the North Atlantic Ocean. Nature 455, 224-246
    • (2008) Nature , vol.455 , pp. 224-246
    • Zubkov, M.V.1    Tarran, G.A.2
  • 48
    • 84878120357 scopus 로고    scopus 로고
    • More mixotrophy in the marine microbial mix
    • Moore, L. R. (2013) More mixotrophy in the marine microbial mix. Proc. Natl. Acad. Sci. U.S.A. 110, 8323-8324
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 8323-8324
    • Moore, L.R.1
  • 50
    • 0141763509 scopus 로고    scopus 로고
    • Production and partitioning of organic matter during simulated phytoplankton blooms
    • Wetz, M. S., and Wheeler, P. A. (2003) Production and partitioning of organic matter during simulated phytoplankton blooms. Limnol. Oceanogr. 48, 1808-1817
    • (2003) Limnol. Oceanogr. , vol.48 , pp. 1808-1817
    • Wetz, M.S.1    Wheeler, P.A.2


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