메뉴 건너뛰기




Volumn 5, Issue 2, 2015, Pages 1172-1203

Evolutionary aspects and regulation of tetrapyrrole biosynthesis in cyanobacteria under aerobic and anaerobic environments

Author keywords

Analogous enzymes; Chlorophyll biosynthesis; ChlR; Hypoxia; Nitrogen fixation; Transcriptional regulator

Indexed keywords

CYANOBACTERIA;

EID: 84961289624     PISSN: None     EISSN: 20751729     Source Type: Journal    
DOI: 10.3390/life5021172     Document Type: Review
Times cited : (33)

References (135)
  • 1
    • 84865680653 scopus 로고    scopus 로고
    • Origins of mitchondria and plastids
    • Bock, R., Knoop, V., Eds.; Springer: Dordrecht, The Netherlands
    • Gray, M.W.; Archibald, J.M. Origins of mitchondria and plastids. In Genomics of Chloroplasts and Mitochondria; Bock, R., Knoop, V., Eds.; Springer: Dordrecht, The Netherlands, 2012; pp. 1-30.
    • (2012) Genomics of Chloroplasts and Mitochondria , pp. 1-30
    • Gray, M.W.1    Archibald, J.M.2
  • 2
    • 51549094335 scopus 로고    scopus 로고
    • Cyanobacterial nitrogen fixation in the ocean: Diversity, regulation, and ecology
    • Herrero, A., Flores, E., Eds.; Caister Academic Press: Norfolk, UK
    • Stal, L.J.; Zehr, J.P. Cyanobacterial nitrogen fixation in the ocean: Diversity, regulation, and ecology. In The Cyanobacteria: Molecular Biology, Genomics and Evolution; Herrero, A., Flores, E., Eds.; Caister Academic Press: Norfolk, UK, 2008; pp. 423-446.
    • (2008) The Cyanobacteria: Molecular Biology, Genomics and Evolution , pp. 423-446
    • Stal, L.J.1    Zehr, J.P.2
  • 3
    • 0002941787 scopus 로고
    • Diurnal cycle of oxygen and sulfide microgradients and microbial photosynthesis in a cyanobacterial mat sediment
    • Jørgensen, B.B.; Revsbech, N.P.; Blackburn, T.H.; Cohen, Y. Diurnal cycle of oxygen and sulfide microgradients and microbial photosynthesis in a cyanobacterial mat sediment. Appl. Environ. Microbiol. 1979, 38, 46-58.
    • (1979) Appl. Environ. Microbiol , vol.38 , pp. 46-58
    • Jørgensen, B.B.1    Revsbech, N.P.2    Blackburn, T.H.3    Cohen, Y.4
  • 5
    • 33645211903 scopus 로고    scopus 로고
    • The effect of oxygen on biochemical networks and the evolution of complex life
    • Raymond, J.; Segrè, D. The effect of oxygen on biochemical networks and the evolution of complex life. Science 2006, 311, 1764-1767.
    • (2006) Science , vol.311 , pp. 1764-1767
    • Raymond, J.1    Segrè, D.2
  • 6
    • 76149105866 scopus 로고    scopus 로고
    • Regulation of gene expression in response to oxygen tension
    • Hunter, C.N., Daldal, F., Thurnauer, M.C., Beatty, J.T., Eds.; Springer: Houten, The Netherlands
    • Bauer, C.E.; Setterdahl, A.; Wu, J.; Robinson, B.R. Regulation of gene expression in response to oxygen tension. In The Purple Photosynthetic Bacteria; Hunter, C.N., Daldal, F., Thurnauer, M.C., Beatty, J.T., Eds.; Springer: Houten, The Netherlands, 2009; pp. 707-725.
    • (2009) The Purple Photosynthetic Bacteria , pp. 707-725
    • Bauer, C.E.1    Setterdahl, A.2    Wu, J.3    Robinson, B.R.4
  • 8
    • 34250807129 scopus 로고    scopus 로고
    • Tetrapyrrole biosynthesis in higher plants
    • Tanaka, R.; Tanaka, A. Tetrapyrrole biosynthesis in higher plants. Annu. Rev. Plant Biol. 2007, 58, 321-346.
    • (2007) Annu. Rev. Plant Biol , vol.58 , pp. 321-346
    • Tanaka, R.1    Tanaka, A.2
  • 9
    • 34548512297 scopus 로고    scopus 로고
    • Chlorophyll biosynthesis in bacteria: The origins of structural and functional diversity
    • Chew, A.G.; Bryant, D.A. Chlorophyll biosynthesis in bacteria: The origins of structural and functional diversity. Annu. Rev. Microbiol. 2007, 61, 113-129.
    • (2007) Annu. Rev. Microbiol , vol.61 , pp. 113-129
    • Chew, A.G.1    Bryant, D.A.2
  • 10
    • 53749102865 scopus 로고    scopus 로고
    • Regulation and evolution of chlorophyll metabolism. Photochem
    • Masuda, T.; Fujita, Y. Regulation and evolution of chlorophyll metabolism. Photochem. Photobiol. Sci. 2008, 7, 1131-1149.
    • (2008) Photobiol. Sci , vol.7 , pp. 1131-1149
    • Masuda, T.1    Fujita, Y.2
  • 11
    • 0036670802 scopus 로고    scopus 로고
    • Terminal steps of haem biosynthesis
    • Dailey, H. Terminal steps of haem biosynthesis. Biochem. Soc. Trans. 2002, 30, 590-595.
    • (2002) Biochem. Soc. Trans , vol.30 , pp. 590-595
    • Dailey, H.1
  • 12
    • 3042715767 scopus 로고    scopus 로고
    • Coproporphyrinogen III and protoporphyrinogen IX oxidases
    • Biosynthesis, Structure, and Degradation; Kadish, K.M., Smith, K.M., Guilard, R., Eds.; Elsevier: New York, NY, USA
    • Akhtar, M. Coproporphyrinogen III and protoporphyrinogen IX oxidases. In The Porphyrin Handbook, Volume 12/Iron and Cobalt Pigments: Biosynthesis, Structure, and Degradation; Kadish, K.M., Smith, K.M., Guilard, R., Eds.; Elsevier: New York, NY, USA, 2003; pp. 75-92.
    • (2003) The Porphyrin Handbook, Volume 12/Iron and Cobalt Pigments , pp. 75-92
    • Akhtar, M.1
  • 13
    • 77952721867 scopus 로고    scopus 로고
    • Transformation of uroporphyrinogen III into Protoheam
    • Warren, M.J., Smith, A.G., Eds.; Springer: Austin, TX, USA
    • Cornah, J.E.; Smith, A.G. Transformation of uroporphyrinogen III into Protoheam. In Tetrapyrroles: Birth, Life and Death; Warren, M.J., Smith, A.G., Eds.; Springer: Austin, TX, USA, 2009; pp. 74-88.
    • (2009) Tetrapyrroles: Birth, Life and Death , pp. 74-88
    • Cornah, J.E.1    Smith, A.G.2
  • 14
    • 0028107485 scopus 로고
    • Isolation of the hemF operon containing the gene for the Escherichia coli aerobic coproporphyrinogen III oxidase by in vivo complementation of a yeast hem13 mutant
    • Troup, B.; Jahn, M.; Hungerer, C.; Jahn, D. Isolation of the hemF operon containing the gene for the Escherichia coli aerobic coproporphyrinogen III oxidase by in vivo complementation of a yeast hem13 mutant. J. Bacteriol. 1994, 176, 673-680.
    • (1994) J. Bacteriol , vol.176 , pp. 673-680
    • Troup, B.1    Jahn, M.2    Hungerer, C.3    Jahn, D.4
  • 16
  • 18
    • 0029009423 scopus 로고
    • Cloning and characterization of the Escherichia coli hemN gene encoding the oxygen-independent coproporphyrinogen III oxidase
    • Troup, B.; Hungerer, C.; Jahn, D. Cloning and characterization of the Escherichia coli hemN gene encoding the oxygen-independent coproporphyrinogen III oxidase. J. Bacteriol. 1995, 177, 3326-3331.
    • (1995) J. Bacteriol , vol.177 , pp. 3326-3331
    • Troup, B.1    Hungerer, C.2    Jahn, D.3
  • 19
    • 0037072870 scopus 로고    scopus 로고
    • Oxygen-independent coproporphyrinogen-III oxidase HemN from Escherichia coli
    • Layer, G.; Verfürth, K.; Mahlitz, E.; Jahn, D. Oxygen-independent coproporphyrinogen-III oxidase HemN from Escherichia coli. J. Biol. Chem. 2002, 277, 34136-34142.
    • (2002) J. Biol. Chem , vol.277 , pp. 34136-34142
    • Layer, G.1    Verfürth, K.2    Mahlitz, E.3    Jahn, D.4
  • 20
    • 0347504850 scopus 로고    scopus 로고
    • Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of radical sam enzymes
    • Layer, G.; Moser, J.; Heinz, D.W.; Jahn, D.; Schubert, W.D. Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of radical sam enzymes. EMBO J. 2003, 22, 6214-6224.
    • (2003) EMBO J , vol.22 , pp. 6214-6224
    • Layer, G.1    Moser, J.2    Heinz, D.W.3    Jahn, D.4    Schubert, W.D.5
  • 21
    • 23844452716 scopus 로고    scopus 로고
    • Radical S-adenosylmethionine enzyme coproporphyrinogen III oxidase HemN: Functional features of the [4Fe-4S] cluster and the two bound S-adenosyl-Lmethionines
    • Layer, G.; Grage, K.; Teschner, T.; Schünemann, V.; Breckau, D.; Masoumi, A.; Jahn, M.; Heathcote, P.; Trautwein, A.; Jahn, D. Radical S-adenosylmethionine enzyme coproporphyrinogen III oxidase HemN: Functional features of the [4Fe-4S] cluster and the two bound S-adenosyl-Lmethionines. J. Biol. Chem. 2005, 280, 29038-29046.
    • (2005) J. Biol. Chem , vol.280 , pp. 29038-29046
    • Layer, G.1    Grage, K.2    Teschner, T.3    Schünemann, V.4    Breckau, D.5    Masoumi, A.6    Jahn, M.7    Heathcote, P.8    Trautwein, A.9    Jahn, D.10
  • 22
    • 77952916829 scopus 로고    scopus 로고
    • Fujita, Y. Functional differentiation of two analogous coproporphyrinogen III oxidases for heme and chlorophyll biosynthesis pathways in the cyanobacterium Synechocystis sp. PCC 6803
    • Goto, T.; Aoki, R.; Minamizaki, K.; Fujita, Y. Functional differentiation of two analogous coproporphyrinogen III oxidases for heme and chlorophyll biosynthesis pathways in the cyanobacterium Synechocystis sp. PCC 6803. Plant Cell Physiol. 2010, 51, 650-663.
    • (2010) Plant Cell Physiol , vol.51 , pp. 650-663
    • Goto, T.1    Aoki, R.2    Minamizaki, K.3
  • 23
    • 84856908720 scopus 로고    scopus 로고
    • Lactococcus lactis HemW (HemN) is a haem-binding protein with a putative role in haem trafficking
    • Abicht, H.K.; Martinez, J.; Layer, G.; Jahn, D.; Solioz, M. Lactococcus lactis HemW (HemN) is a haem-binding protein with a putative role in haem trafficking. Biochem. J. 2012, 442, 335-343.
    • (2012) Biochem. J , vol.442 , pp. 335-343
    • Abicht, H.K.1    Martinez, J.2    Layer, G.3    Jahn, D.4    Solioz, M.5
  • 24
    • 0027724541 scopus 로고
    • Nucleotide sequence of the hemG gene involved in the protoporphyrinogen oxidase activity of Escherichia coli K12
    • Sasarman, A.; Letowski, J.; Czaika, G.; Ramirez, V.; Nead, M.A.; Jacobs, J.M.; Morais, R. Nucleotide sequence of the hemG gene involved in the protoporphyrinogen oxidase activity of Escherichia coli K12. Can. J. Microbiol. 1993, 39, 1155-1161.
    • (1993) Can. J. Microbiol , vol.39 , pp. 1155-1161
    • Sasarman, A.1    Letowski, J.2    Czaika, G.3    Ramirez, V.4    Nead, M.A.5    Jacobs, J.M.6    Morais, R.7
  • 25
    • 0026676696 scopus 로고
    • Cloning and characterization of the Bacillus subtilis hemEHY gene cluster, which encodes protoheme IX biosynthetic enzymes
    • Hansson, M.; Hederstedt, L. Cloning and characterization of the Bacillus subtilis hemEHY gene cluster, which encodes protoheme IX biosynthetic enzymes. J. Bacteriol. 1992, 174, 8081-8093.
    • (1992) J. Bacteriol , vol.174 , pp. 8081-8093
    • Hansson, M.1    Hederstedt, L.2
  • 26
    • 78049279741 scopus 로고    scopus 로고
    • Identification of a gene essential for protoporphyrinogen IX oxidase activity in the cyanobacterium Synechocystis sp. PCC 6803
    • Kato, K.; Tanaka, R.; Sano, S.; Tanaka, A.; Hosaka, H. Identification of a gene essential for protoporphyrinogen IX oxidase activity in the cyanobacterium Synechocystis sp. PCC 6803. Proc. Natl. Acad. Sci. USA 2010, 107, 16649-16654.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 16649-16654
    • Kato, K.1    Tanaka, R.2    Sano, S.3    Tanaka, A.4    Hosaka, H.5
  • 27
    • 2442563409 scopus 로고    scopus 로고
    • Crystal structure of protoporphyrinogen IX oxidase: A key enzyme in haem and chlorophyll biosynthesis
    • Koch, M.; Breithaupt, C.; Kiefersauer, R.; Freigang, J.; Huber, R.; Messerschmidt, A. Crystal structure of protoporphyrinogen IX oxidase: A key enzyme in haem and chlorophyll biosynthesis. EMBO J. 2004, 23, 1720-1728.
    • (2004) EMBO J. , vol.23 , pp. 1720-1728
    • Koch, M.1    Breithaupt, C.2    Kiefersauer, R.3    Freigang, J.4    Huber, R.5    Messerschmidt, A.6
  • 28
    • 67651222271 scopus 로고    scopus 로고
    • Identification of Escherichia coli HemG as a novel, menadione-dependent flavodoxin with protoporphyrinogen oxidase activity
    • Boynton, T.O.; Daugherty, L.E.; Dailey, T.A.; Dailey, H.A. Identification of Escherichia coli HemG as a novel, menadione-dependent flavodoxin with protoporphyrinogen oxidase activity. Biochemistry 2009, 48, 6705-6711.
    • (2009) Biochemistry , vol.48 , pp. 6705-6711
    • Boynton, T.O.1    Daugherty, L.E.2    Dailey, T.A.3    Dailey, H.A.4
  • 29
    • 84923177266 scopus 로고    scopus 로고
    • Molecular phylogeny and intricate evolutionary history of the three isofunctional enzymes involved in the oxidation of protoporphyrinogen IX
    • Kobayashi, K.; Masuda, T.; Tajima, N.; Wada, H.; Sato, N. Molecular phylogeny and intricate evolutionary history of the three isofunctional enzymes involved in the oxidation of protoporphyrinogen IX. Genome Biol. Evol. 2014, 6, 2141-2155.
    • (2014) Genome Biol. Evol , vol.6 , pp. 2141-2155
    • Kobayashi, K.1    Masuda, T.2    Tajima, N.3    Wada, H.4    Sato, N.5
  • 30
    • 84940912592 scopus 로고    scopus 로고
    • In The Porphyrin Handbook, vol. 13, Chlorophylls and Bilins: Synthesis, and Degradation; Kadish, K.M., Smith, K.M., Guilard, R., Eds.; Elsevier: Amsterdam, The Netherlands
    • Bollivar, D.W. Intermediate steps in chlorophyll biosynthesis: Methylation and cyclization. In The Porphyrin Handbook, vol. 13, Chlorophylls and Bilins: Synthesis, and Degradation; Kadish, K.M., Smith, K.M., Guilard, R., Eds.; Elsevier: Amsterdam, The Netherlands, 2003; Volume 13, pp. 49-69.
    • (2003) Intermediate Steps in Chlorophyll Biosynthesis: Methylation and Cyclization , vol.13 , pp. 49-69
    • Bollivar, D.W.1
  • 31
    • 0029914197 scopus 로고    scopus 로고
    • The chlorophyll biosynthetic enzyme Mg-protoporphyrin IX monomethyl ester (Oxidative) cyclase (characterization and partial purification from Chlamydomonas reinhardtii and Synechocystis sp. PCC 6803)
    • Bollivar, D.W.; Beale, S.I. The chlorophyll biosynthetic enzyme Mg-protoporphyrin IX monomethyl ester (oxidative) cyclase (characterization and partial purification from Chlamydomonas reinhardtii and Synechocystis sp. PCC 6803). Plant Physiol. 1996, 112, 105-114.
    • (1996) Plant Physiol , vol.112 , pp. 105-114
    • Bollivar, D.W.1    Beale, S.I.2
  • 32
    • 0036178443 scopus 로고    scopus 로고
    • Rubrivivax gelatinosus acsF (Previously orf358) codes for a conserved, putative binuclear-iron-cluster-containing protein involved in aerobic oxidative cyclization of Mg-protoporphyrin IX monomethylester
    • Pinta, V.; Picaud, M.; Reiss-Husson, F.; Astier, C. Rubrivivax gelatinosus acsF (previously orf358) codes for a conserved, putative binuclear-iron-cluster-containing protein involved in aerobic oxidative cyclization of Mg-protoporphyrin IX monomethylester. J. Bacteriol. 2002, 184, 746-753.
    • (2002) J. Bacteriol , vol.184 , pp. 746-753
    • Pinta, V.1    Picaud, M.2    Reiss-Husson, F.3    Astier, C.4
  • 33
    • 41449093999 scopus 로고    scopus 로고
    • Identification of two homologous genes, chlAI and chlAII, that are differentially involved in isocyclic ring formation of chlorophyll a in the cyanobacterium Synechocystis sp
    • Minamizaki, K.; Mizoguchi, T.; Goto, T.; Tamiaki, H.; Fujita, Y. Identification of two homologous genes, chlAI and chlAII, that are differentially involved in isocyclic ring formation of chlorophyll a in the cyanobacterium Synechocystis sp. PCC 6803. J. Biol. Chem. 2008, 283, 2684-2692.
    • (2008) PCC 6803. J. Biol. Chem. , vol.283 , pp. 2684-2692
    • Minamizaki, K.1    Mizoguchi, T.2    Goto, T.3    Tamiaki, H.4    Fujita, Y.5
  • 34
    • 69449103993 scopus 로고    scopus 로고
    • Differential requirement of two homologous proteins encoded by sll1214 and sll1874 for the reaction of Mg protoporphyrin monomethylester oxidative cyclase under aerobic and micro-oxic growth conditions
    • Peter, E.; Salinas, A.; Wallner, T.; Jeske, D.; Dienst, D.; Wilde, A.; Grimm, B. Differential requirement of two homologous proteins encoded by sll1214 and sll1874 for the reaction of Mg protoporphyrin monomethylester oxidative cyclase under aerobic and micro-oxic growth conditions. Biochim. Biophys. Acta 2009, 1787, 1458-1467.
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 1458-1467
    • Peter, E.1    Salinas, A.2    Wallner, T.3    Jeske, D.4    Dienst, D.5    Wilde, A.6    Grimm, B.7
  • 36
    • 0034658505 scopus 로고    scopus 로고
    • The crd1 gene encodes a putative di-iron enzyme required for photosystem I accumulation in copper deficiency and hypoxia in Chlamydomonas reinhardtii
    • Moseley, J.; Quinn, J.; Eriksson, M.; Merchant, S. The crd1 gene encodes a putative di-iron enzyme required for photosystem I accumulation in copper deficiency and hypoxia in Chlamydomonas reinhardtii. EMBO J. 2000, 19, 2139-2151.
    • (2000) EMBO J , vol.19 , pp. 2139-2151
    • Moseley, J.1    Quinn, J.2    Eriksson, M.3    Merchant, S.4
  • 37
    • 84901233802 scopus 로고    scopus 로고
    • The Ycf54 protein is part of the membrane component of Mg-protoporphyrin IX monomethyl ester cyclase from barley (Hordeum vulgare L.)
    • Bollivar, D.W.; Braumann, I.; Berendt, K.; Gough, S.P.; Hansson, M. The Ycf54 protein is part of the membrane component of Mg-protoporphyrin IX monomethyl ester cyclase from barley (Hordeum vulgare L.). FEBS J. 2014, 281, 2377-2386.
    • (2014) FEBS J , vol.281 , pp. 2377-2386
    • Bollivar, D.W.1    Braumann, I.2    Berendt, K.3    Gough, S.P.4    Hansson, M.5
  • 38
    • 0034612350 scopus 로고    scopus 로고
    • Anaerobic chlorophyll isocyclic ring formation in Rhodobacter capsulatus requires a cobalamin cofactor
    • Gough, S.P.; Petersen, B.O.; Duus, J.O. Anaerobic chlorophyll isocyclic ring formation in Rhodobacter capsulatus requires a cobalamin cofactor. Proc. Natl. Acad. Sci. USA 2000, 97, 6908-6913.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6908-6913
    • Gough, S.P.1    Petersen, B.O.2    Duus, J.O.3
  • 39
    • 0023320838 scopus 로고
    • The use of continuous assays to characterize the oxidative cyclase that synthesizes the chlorophyll isocyclic ring
    • Nasrulhaq-Boyce, A.; Griffiths, W.T.; Jones, O.T. The use of continuous assays to characterize the oxidative cyclase that synthesizes the chlorophyll isocyclic ring. Biochem. J. 1987, 243, 23-29.
    • (1987) Biochem. J , vol.243 , pp. 23-29
    • Nasrulhaq-Boyce, A.1    Griffiths, W.T.2    Jones, O.T.3
  • 40
    • 0024969308 scopus 로고
    • Incorporation of atmospheric oxygen into the carbonyl functionality of the protochlorophyllide isocyclic ring
    • Walker, C.J.; Mansfield, K.E.; Smith, K.M.; Castelfranco, P.A. Incorporation of atmospheric oxygen into the carbonyl functionality of the protochlorophyllide isocyclic ring. Biochem. J. 1989, 257, 599-602.
    • (1989) Biochem. J , vol.257 , pp. 599-602
    • Walker, C.J.1    Mansfield, K.E.2    Smith, K.M.3    Castelfranco, P.A.4
  • 41
    • 0029132620 scopus 로고
    • Formation of the isocyclic ring of chlorophyll by isolated Chlamydomonas reinhardtii chloroplasts
    • Bollivar, D.W.; Beale, S.I. Formation of the isocyclic ring of chlorophyll by isolated Chlamydomonas reinhardtii chloroplasts. Photosynth. Res. 1995, 43, 113-124.
    • (1995) Photosynth. Res , vol.43 , pp. 113-124
    • Bollivar, D.W.1    Beale, S.I.2
  • 42
    • 47849127156 scopus 로고    scopus 로고
    • NADPH-dependent thioredoxin reductase and 2-Cys peroxiredoxins are needed for the protection of Mgprotoporphyrin monomethyl ester cyclase
    • Stenbaek, A.; Hansson, A.; Wulff, R.P.; Hansson, M.; Dietz, K.J.; Jensen, P.E. NADPH-dependent thioredoxin reductase and 2-Cys peroxiredoxins are needed for the protection of Mgprotoporphyrin monomethyl ester cyclase. FEBS Lett. 2008, 582, 2773-2778.
    • (2008) FEBS Lett , vol.582 , pp. 2773-2778
    • Stenbaek, A.1    Hansson, A.2    Wulff, R.P.3    Hansson, M.4    Dietz, K.J.5    Jensen, P.E.6
  • 43
    • 84865015496 scopus 로고    scopus 로고
    • Conserved chloroplast open-reading frame ycf54 is required for activity of the magnesium protoporphyrin monomethylester oxidative cyclase in Synechocystis PCC 6803
    • Hollingshead, S.; Kopecná, J.; Jackson, P.J.; Canniffe, D.P.; Davison, P.A.; Dickman, M.J.; Sobotka, R.; Hunter, C.N. Conserved chloroplast open-reading frame ycf54 is required for activity of the magnesium protoporphyrin monomethylester oxidative cyclase in Synechocystis PCC 6803. J. Biol. Chem. 2012, 287, 27823-27833.
    • (2012) J. Biol. Chem , vol.287 , pp. 27823-27833
    • Hollingshead, S.1    Kopecná, J.2    Jackson, P.J.3    Canniffe, D.P.4    Davison, P.A.5    Dickman, M.J.6    Sobotka, R.7    Hunter, C.N.8
  • 44
    • 84870776667 scopus 로고    scopus 로고
    • LCAA, a novel factor required for magnesium protoporphyrin monomethylester cyclase accumulation and feedback control of aminolevulinic acid biosynthesis in tobacco
    • Albus, C.A.; Salinas, A.; Czarnecki, O.; Kahlau, S.; Rothbart, M.; Thiele, W.; Lein, W.; Bock, R.; Grimm, B.; Schöttler, M.A. LCAA, a novel factor required for magnesium protoporphyrin monomethylester cyclase accumulation and feedback control of aminolevulinic acid biosynthesis in tobacco. Plant Physiol. 2012, 160, 1923-1939.
    • (2012) Plant Physiol , vol.160 , pp. 1923-1939
    • Albus, C.A.1    Salinas, A.2    Czarnecki, O.3    Kahlau, S.4    Rothbart, M.5    Thiele, W.6    Lein, W.7    Bock, R.8    Grimm, B.9    Schöttler, M.A.10
  • 45
    • 0028277918 scopus 로고
    • Directed mutational analysis of bacteriochlorophyll a biosynthesis in Rhodobacter capsulatus
    • Bollivar, D.; Suzuki, J.; Beatty, J.; Dobrowolski, J.; Bauer, C. Directed mutational analysis of bacteriochlorophyll a biosynthesis in Rhodobacter capsulatus. J. Mol. Biol. 1994, 237, 622-640.
    • (1994) J. Mol. Biol , vol.237 , pp. 622-640
    • Bollivar, D.1    Suzuki, J.2    Beatty, J.3    Dobrowolski, J.4    Bauer, C.5
  • 46
    • 1342282989 scopus 로고    scopus 로고
    • Aerobic and anaerobic Mg-protoporphyrin monomethyl ester cyclases in purple bacteria: A strategy adopted to bypass the repressive oxygen control system
    • Ouchane, S.; Steunou, A.; Picaud, M.; Astier, C. Aerobic and anaerobic Mg-protoporphyrin monomethyl ester cyclases in purple bacteria: A strategy adopted to bypass the repressive oxygen control system. J. Biol. Chem. 2004, 279, 6385-6394.
    • (2004) J. Biol. Chem , vol.279 , pp. 6385-6394
    • Ouchane, S.1    Steunou, A.2    Picaud, M.3    Astier, C.4
  • 47
    • 34147146357 scopus 로고    scopus 로고
    • Global regulation of photosynthesis and respiration by FnrL: The first two targets in the tetrapyrrole pathway
    • Ouchane, S.; Picaud, M.; Therizols, P.; Reiss-Husson, F.; Astier, C. Global regulation of photosynthesis and respiration by FnrL: The first two targets in the tetrapyrrole pathway. J. Biol. Chem. 2007, 282, 7690-7699.
    • (2007) J. Biol. Chem. , vol.282 , pp. 7690-7699
    • Ouchane, S.1    Picaud, M.2    Therizols, P.3    Reiss-Husson, F.4    Astier, C.5
  • 48
    • 77953734607 scopus 로고    scopus 로고
    • Adaptation to oxygen: Role of terminal oxidases in photosynthesis initiation in the purple photosynthetic bacterium, Rubrivivax gelatinosus
    • Hassani, B.K.; Steunou, A.S.; Liotenberg, S.; Reiss-Husson, F.; Astier, C.; Ouchane, S. Adaptation to oxygen: Role of terminal oxidases in photosynthesis initiation in the purple photosynthetic bacterium, Rubrivivax gelatinosus. J. Biol. Chem. 2010, 285, 19891-19899.
    • (2010) J. Biol. Chem , vol.285 , pp. 19891-19899
    • Hassani, B.K.1    Steunou, A.S.2    Liotenberg, S.3    Reiss-Husson, F.4    Astier, C.5    Ouchane, S.6
  • 49
    • 79959661932 scopus 로고    scopus 로고
    • Lapidus, A.; et al. Complete genome sequence of the filamentous anoxygenic phototrophic bacterium Chloroflexus aurantiacus
    • Tang, K.H.; Barry, K.; Chertkov, O.; Dalin, E.; Han, C.S.; Hauser, L.J.; Honchak, B.M.; Karbach, L.E.; Land, M.L.; Lapidus, A.; et al. Complete genome sequence of the filamentous anoxygenic phototrophic bacterium Chloroflexus aurantiacus. BMC Genomics 2011, 12, doi:10.1186/1471-2164-12-334.
    • (2011) BMC Genomics , pp. 12
    • Tang, K.H.1    Barry, K.2    Chertkov, O.3    Dalin, E.4    Han, C.S.5    Hauser, L.J.6    Honchak, B.M.7    Karbach, L.E.8    Land, M.L.9
  • 50
    • 84876186732 scopus 로고    scopus 로고
    • Distribution and origin of oxygen-dependent and oxygen-independent forms of Mg-protoporphyrin monomethylester cyclase among phototrophic proteobacteria
    • Boldareva-Nuianzina, E.N.; Bláhová, Z.; Sobotka, R.; Koblízek, M. Distribution and origin of oxygen-dependent and oxygen-independent forms of Mg-protoporphyrin monomethylester cyclase among phototrophic proteobacteria. Appl. Environ. Microbiol. 2013, 79, 2596-2604.
    • (2013) Appl. Environ. Microbiol , vol.79 , pp. 2596-2604
    • Boldareva-Nuianzina, E.N.1    Bláhová, Z.2    Sobotka, R.3    Koblízek, M.4
  • 51
    • 3242883632 scopus 로고    scopus 로고
    • Novel insights into the enzymology, regulation and physiological functions of light-dependent protochlorophyllide oxidoreductase in angiosperms
    • Masuda, T.; Takamiya, K. Novel insights into the enzymology, regulation and physiological functions of light-dependent protochlorophyllide oxidoreductase in angiosperms. Photosynth. Res. 2004, 81, 1-29.
    • (2004) Photosynth. Res , vol.81 , pp. 1-29
    • Masuda, T.1    Takamiya, K.2
  • 52
    • 27544442817 scopus 로고    scopus 로고
    • Making light work of enzyme catalysis: Protochlorophyllide oxidoreductase
    • Heyes, D.; Hunter, C. Making light work of enzyme catalysis: Protochlorophyllide oxidoreductase. Trends Biochem. Sci. 2005, 30, 642-649.
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 642-649
    • Heyes, D.1    Hunter, C.2
  • 53
    • 0030175228 scopus 로고    scopus 로고
    • Protochlorophyllide reduction: A key step in the greening of plants
    • Fujita, Y. Protochlorophyllide reduction: A key step in the greening of plants. Plant Cell Physiol. 1996, 37, 411-421.
    • (1996) Plant Cell Physiol , vol.37 , pp. 411-421
    • Fujita, Y.1
  • 54
    • 84940920463 scopus 로고    scopus 로고
    • The light-independent protochlorophyllide reductase: A nitrogenase-like enzyme catalyzing a key reaction for greening in the dark
    • Kadish, K., Smith, K.M., Guilard, R., Eds.; Academic Press: Amsterdom, The Netherlands
    • Fujita, Y.; Bauer, C.E. The light-independent protochlorophyllide reductase: A nitrogenase-like enzyme catalyzing a key reaction for greening in the dark. In Chlorophylls and Bilins: Biosynthesis, Synthesis, and Degradation; Kadish, K., Smith, K.M., Guilard, R., Eds.; Academic Press: Amsterdom, The Netherlands, 2003; pp. 109-156.
    • (2003) Chlorophylls and Bilins: Biosynthesis, Synthesis, and Degradation , pp. 109-156
    • Fujita, Y.1    Bauer, C.E.2
  • 56
    • 0034604647 scopus 로고    scopus 로고
    • Reconstitution of light-independent protochlorophyllide reductase from purified BchL and BchN-BchB subunits. In vitro confirmation of nitrogenase-like features of a bacteriochlorophyll biosynthesis enzyme
    • Fujita, Y.; Bauer, C. Reconstitution of light-independent protochlorophyllide reductase from purified BchL and BchN-BchB subunits. In vitro confirmation of nitrogenase-like features of a bacteriochlorophyll biosynthesis enzyme. J. Biol. Chem. 2000, 275, 23583-23588.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23583-23588
    • Fujita, Y.1    Bauer, C.2
  • 57
    • 57449110787 scopus 로고    scopus 로고
    • Crystal structure of the L protein of Rhodobacter sphaeroides light-independent protochlorophyllide reductase with MgADP bound: A homologue of the nitrogenase Fe protein
    • Sarma, R.; Barney, B.; Hamilton, T.; Jones, A.; Seefeldt, L.; Peters, J. Crystal structure of the L protein of Rhodobacter sphaeroides light-independent protochlorophyllide reductase with MgADP bound: A homologue of the nitrogenase Fe protein. Biochemistry 2008, 47, 13004-13015.
    • (2008) Biochemistry , vol.47 , pp. 13004-13015
    • Sarma, R.1    Barney, B.2    Hamilton, T.3    Jones, A.4    Seefeldt, L.5    Peters, J.6
  • 60
    • 33750522524 scopus 로고    scopus 로고
    • Nitrogenase Fe protein-like Fe-S cluster is conserved in L-protein (BchL) of dark-operative protochlorophyllide reductase from Rhodobacter capsulatus
    • Nomata, J.; Kitashima, M.; Inoue, K.; Fujita, Y. Nitrogenase Fe protein-like Fe-S cluster is conserved in L-protein (BchL) of dark-operative protochlorophyllide reductase from Rhodobacter capsulatus. FEBS Lett. 2006, 580, 6151-6154.
    • (2006) FEBS Lett , vol.580 , pp. 6151-6154
    • Nomata, J.1    Kitashima, M.2    Inoue, K.3    Fujita, Y.4
  • 61
    • 44849114407 scopus 로고    scopus 로고
    • ATP-driven reduction by dark-operative protochlorophyllide oxidoreductase from Chlorobium tepidum mechanistically resembles nitrogenase catalysis
    • Bröcker, M.; Virus, S.; Ganskow, S.; Heathcote, P.; Heinz, D.; Schubert, W.; Jahn, D.; Moser, J. ATP-driven reduction by dark-operative protochlorophyllide oxidoreductase from Chlorobium tepidum mechanistically resembles nitrogenase catalysis. J. Biol. Chem. 2008, 283, 10559-10567.
    • (2008) J. Biol. Chem , vol.283 , pp. 10559-10567
    • Bröcker, M.1    Virus, S.2    Ganskow, S.3    Heathcote, P.4    Heinz, D.5    Schubert, W.6    Jahn, D.7    Moser, J.8
  • 62
    • 41449089777 scopus 로고    scopus 로고
    • NB-protein (BchN-BchB) of dark-operative protochlorophyllide reductase is the catalytic component containing oxygentolerant Fe-S clusters
    • Nomata, J.; Ogawa, T.; Kitashima, M.; Inoue, K.; Fujita, Y. NB-protein (BchN-BchB) of dark-operative protochlorophyllide reductase is the catalytic component containing oxygentolerant Fe-S clusters. FEBS Lett. 2008, 582, 1346-1350.
    • (2008) FEBS Lett , vol.582 , pp. 1346-1350
    • Nomata, J.1    Ogawa, T.2    Kitashima, M.3    Inoue, K.4    Fujita, Y.5
  • 64
    • 84903280941 scopus 로고    scopus 로고
    • Dark-operative protochlorophyllide oxidoreductase generates substrate radicals by an iron-sulphur cluster in bacteriochlorophyll biosynthesis
    • Nomata, J.; Kondo, T.; Mizoguchi, T.; Tamiaki, H.; Itoh, S.; Fujita, Y. Dark-operative protochlorophyllide oxidoreductase generates substrate radicals by an iron-sulphur cluster in bacteriochlorophyll biosynthesis. Sci. Rep. 2014, 4, doi:10.1038/srep05455.
    • (2014) Sci. Rep , pp. 4
    • Nomata, J.1    Kondo, T.2    Mizoguchi, T.3    Tamiaki, H.4    Itoh, S.5    Fujita, Y.6
  • 65
    • 33751079088 scopus 로고    scopus 로고
    • Differential operation of dual protochlorophyllide reductases for chlorophyll biosynthesis in response to environmental oxygen levels in the cyanobacterium Leptolyngbya boryana
    • Yamazaki, S.; Nomata, J.; Fujita, Y. Differential operation of dual protochlorophyllide reductases for chlorophyll biosynthesis in response to environmental oxygen levels in the cyanobacterium Leptolyngbya boryana. Plant Physiol. 2006, 142, 911-922.
    • (2006) Plant Physiol , vol.142 , pp. 911-922
    • Yamazaki, S.1    Nomata, J.2    Fujita, Y.3
  • 66
    • 70349908427 scopus 로고    scopus 로고
    • Oxygen sensitivity of a nitrogenase-like protochlorophyllide reductase from the cyanobacterium Leptolyngbya boryana
    • Yamamoto, H.; Kurumiya, S.; Ohashi, R.; Fujita, Y. Oxygen sensitivity of a nitrogenase-like protochlorophyllide reductase from the cyanobacterium Leptolyngbya boryana. Plant Cell Physiol. 2009, 50, 1663-1673.
    • (2009) Plant Cell Physiol , vol.50 , pp. 1663-1673
    • Yamamoto, H.1    Kurumiya, S.2    Ohashi, R.3    Fujita, Y.4
  • 67
    • 0028226211 scopus 로고
    • Protochlorophyllide reductase is homologous to human carbonyl reductase and pig 20 β-hydroxysteroid dehydrogenase
    • Baker, M.E. Protochlorophyllide reductase is homologous to human carbonyl reductase and pig 20 β-hydroxysteroid dehydrogenase. Biochem. J. 1994, 300, 605-607.
    • (1994) Biochem. J , vol.300 , pp. 605-607
    • Baker, M.E.1
  • 68
    • 0028051740 scopus 로고
    • Structural comparisons lead to the definition of a new superfamily of NAD(P)(H)-accepting oxidoreductases: The single-domain reductases/epimerases/dehydrogenases (the “RED” family)
    • Labesse, G.; Vidal-Cros, A.; Chomilier, J.; Gaudry, M.; Mornon, J.P. Structural comparisons lead to the definition of a new superfamily of NAD(P)(H)-accepting oxidoreductases: The single-domain reductases/epimerases/dehydrogenases (the “RED” family). Biochem. J. 1994, 304, 95-99.
    • (1994) Biochem. J , vol.304 , pp. 95-99
    • Labesse, G.1    Vidal-Cros, A.2    Chomilier, J.3    Gaudry, M.4    Mornon, J.P.5
  • 69
    • 34047267978 scopus 로고    scopus 로고
    • Ultrafast catalytic processes in enzymes
    • Zhong, D. Ultrafast catalytic processes in enzymes. Curr. Opin. Chem. Biol. 2007, 11, 174-181.
    • (2007) Curr. Opin. Chem. Biol , vol.11 , pp. 174-181
    • Zhong, D.1
  • 70
    • 0028895568 scopus 로고
    • A light-dependent complementation system for analysis of NADPH: Protochlorophyllide oxidoreductase: Identification and mutagenesis of two conserved residues that are essential for enzyme activity
    • Wilks, H.; Timko, M. A light-dependent complementation system for analysis of NADPH: protochlorophyllide oxidoreductase: Identification and mutagenesis of two conserved residues that are essential for enzyme activity. Proc. Natl. Acad. Sci. USA 1995, 92, 724-728.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 724-728
    • Wilks, H.1    Timko, M.2
  • 71
    • 0037143612 scopus 로고    scopus 로고
    • The kinetics and thermodynamics of the photochemistry catalyzed by protochlorophyllide oxidoreductase
    • Heyes, D.; Ruban, A.; Wilks, H.; Hunter, C. Enzymology below 200 K: The kinetics and thermodynamics of the photochemistry catalyzed by protochlorophyllide oxidoreductase. Proc. Natl. Acad. Sci. USA 2002, 99, 11145-11150.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11145-11150
    • Heyes, D.1    Ruban, A.2    Wilks, H.3    Hunter, C.4    Enzymology Below 200, K.5
  • 72
    • 33748750406 scopus 로고    scopus 로고
    • The first catalytic step of the light-driven enzyme protochlorophyllide oxidoreductase proceeds via a charge transfer complex
    • Heyes, D.; Heathcote, P.; Rigby, S.; Palacios, M.; van Grondelle, R.; Hunter, C. The first catalytic step of the light-driven enzyme protochlorophyllide oxidoreductase proceeds via a charge transfer complex. J. Biol. Chem. 2006, 281, 26847-26853.
    • (2006) J. Biol. Chem , vol.281 , pp. 26847-26853
    • Heyes, D.1    Heathcote, P.2    Rigby, S.3    Palacios, M.4    Van Grondelle, R.5    Hunter, C.6
  • 73
  • 74
    • 0032006920 scopus 로고    scopus 로고
    • Cloning of the gene encoding a protochlorophyllide reductase: The physiological significance of the co-existence of light-dependent and -independent protochlorophyllide reduction systems in the cyanobacterium Plectonema boryanum
    • Fujita, Y.; Takagi, H.; Hase, T. Cloning of the gene encoding a protochlorophyllide reductase: The physiological significance of the co-existence of light-dependent and -independent protochlorophyllide reduction systems in the cyanobacterium Plectonema boryanum. Plant Cell Physiol. 1998, 39, 177-185.
    • (1998) Plant Cell Physiol , vol.39 , pp. 177-185
    • Fujita, Y.1    Takagi, H.2    Hase, T.3
  • 75
    • 33845978782 scopus 로고    scopus 로고
    • Photon flux density-dependent gene expression in Synechocystis sp. PCC 6803 is regulated by a small, redox-responsive, LuxR-type regulator
    • Nakamura, K.; Hihara, Y. Photon flux density-dependent gene expression in Synechocystis sp. PCC 6803 is regulated by a small, redox-responsive, LuxR-type regulator. J. Biol. Chem. 2006, 281, 36758-36766.
    • (2006) J. Biol. Chem , vol.281 , pp. 36758-36766
    • Nakamura, K.1    Hihara, Y.2
  • 76
    • 77956627100 scopus 로고    scopus 로고
    • The PedR transcriptional regulator interacts with thioredoxin to connect photosynthesis with gene expression in cyanobacteria
    • Horiuchi, M.; Nakamura, K.; Kojima, K.; Nishiyama, Y.; Hatakeyama, W.; Hisabori, T.; Hihara, Y. The PedR transcriptional regulator interacts with thioredoxin to connect photosynthesis with gene expression in cyanobacteria. Biochem. J. 2010, 431, 135-140.
    • (2010) Biochem. J. , vol.431 , pp. 135-140
    • Horiuchi, M.1    Nakamura, K.2    Kojima, K.3    Nishiyama, Y.4    Hatakeyama, W.5    Hisabori, T.6    Hihara, Y.7
  • 77
    • 68949156528 scopus 로고    scopus 로고
    • Light-dependent and light-independent protochlorophyllide oxidoreductases in the chromatically adapting cyanobacterium Fremyella diplosiphon UTEX 481
    • Shui, J.; Saunders, E.; Needleman, R.; Nappi, M.; Cooper, J.; Hall, L.; Kehoe, D.; Stowe-Evans, E. Light-dependent and light-independent protochlorophyllide oxidoreductases in the chromatically adapting cyanobacterium Fremyella diplosiphon UTEX 481. Plant Cell Physiol. 2009, 50, 1507-1521.
    • (2009) Plant Cell Physiol , vol.50 , pp. 1507-1521
    • Shui, J.1    Saunders, E.2    Needleman, R.3    Nappi, M.4    Cooper, J.5    Hall, L.6    Kehoe, D.7    Stowe-Evans, E.8
  • 78
    • 20444442993 scopus 로고    scopus 로고
    • Identification of a vinyl reductase gene for chlorophyll synthesis in Arabidopsis thaliana and implications for the evolution of Prochlorococcus species
    • Nagata, N.; Tanaka, R.; Satoh, S.; Tanaka, A. Identification of a vinyl reductase gene for chlorophyll synthesis in Arabidopsis thaliana and implications for the evolution of Prochlorococcus species. Plant Cell 2005, 17, 233-240.
    • (2005) Plant Cell , vol.17 , pp. 233-240
    • Nagata, N.1    Tanaka, R.2    Satoh, S.3    Tanaka, A.4
  • 79
    • 34047246478 scopus 로고    scopus 로고
    • Characterization of a plant-like protochlorophyllide a divinyl reductase in green sulfur bacteria
    • Chew, A.G.; Bryant, D.A. Characterization of a plant-like protochlorophyllide a divinyl reductase in green sulfur bacteria. J. Biol. Chem. 2007, 282, 2967-2975.
    • (2007) J. Biol. Chem , vol.282 , pp. 2967-2975
    • Chew, A.G.1    Bryant, D.A.2
  • 80
    • 84874037609 scopus 로고    scopus 로고
    • Identification of an 8-vinyl reductase involved in bacteriochlorophyll biosynthesis in Rhodobacter sphaeroides and evidence for the existence of a third distinct class of the enzyme
    • Canniffe, D.P.; Jackson, P.J.; Hollingshead, S.; Dickman, M.J.; Hunter, C.N. Identification of an 8-vinyl reductase involved in bacteriochlorophyll biosynthesis in Rhodobacter sphaeroides and evidence for the existence of a third distinct class of the enzyme. Biochem. J. 2013, 450, 397-405.
    • (2013) Biochem. J. , vol.450 , pp. 397-405
    • Canniffe, D.P.1    Jackson, P.J.2    Hollingshead, S.3    Dickman, M.J.4    Hunter, C.N.5
  • 81
    • 57749097479 scopus 로고    scopus 로고
    • Slr1923 of Synechocystis sp. PCC6803 is essential for conversion of 3,8-divinyl(proto)chlorophyll(ide) to 3-monovinyl(proto)chlorophyll(ide)
    • Islam, M.R.; Aikawa, S.; Midorikawa, T.; Kashino, Y.; Satoh, K.; Koike, H. Slr1923 of Synechocystis sp. PCC6803 is essential for conversion of 3,8-divinyl(proto)chlorophyll(ide) to 3-monovinyl(proto)chlorophyll(ide). Plant Physiol. 2008, 148, 1068-1081.
    • (2008) Plant Physiol , vol.148 , pp. 1068-1081
    • Islam, M.R.1    Aikawa, S.2    Midorikawa, T.3    Kashino, Y.4    Satoh, K.5    Koike, H.6
  • 82
    • 44049092613 scopus 로고    scopus 로고
    • Identification of a novel vinyl reductase gene essential for the biosynthesis of monovinyl chlorophyll in Synechocystis sp. PCC 6803
    • Ito, H.; Yokono, M.; Tanaka, R.; Tanaka, A. Identification of a novel vinyl reductase gene essential for the biosynthesis of monovinyl chlorophyll in Synechocystis sp. PCC 6803. J. Biol. Chem. 2008, 283, 9002-9011.
    • (2008) J. Biol. Chem , vol.283 , pp. 9002-9011
    • Ito, H.1    Yokono, M.2    Tanaka, R.3    Tanaka, A.4
  • 83
    • 84899079315 scopus 로고    scopus 로고
    • Evolution of a new chlorophyll metabolic pathway driven by the dynamic changes in enzyme promiscuous activity
    • Ito, H.; Tanaka, A. Evolution of a new chlorophyll metabolic pathway driven by the dynamic changes in enzyme promiscuous activity. Plant Cell Physiol. 2014, 55, 593-603.
    • (2014) Plant Cell Physiol , vol.55 , pp. 593-603
    • Ito, H.1    Tanaka, A.2
  • 85
    • 33744959925 scopus 로고    scopus 로고
    • A second nitrogenase-like enzyme for bacteriochlorophyll biosynthesis—reconstitution of chlorophyllide a reductase with purified X-protein (BchX) and YZ-protein (BchY-BchZ) from Rhodobacter capsulatus
    • Nomata, J.; Mizoguchi, T.; Tamiaki, H.; Fujita, Y. A second nitrogenase-like enzyme for bacteriochlorophyll biosynthesis—reconstitution of chlorophyllide a reductase with purified X-protein (BchX) and YZ-protein (BchY-BchZ) from Rhodobacter capsulatus. J. Biol. Chem. 2006, 281, 15021-15028.
    • (2006) J. Biol. Chem. , vol.281 , pp. 15021-15028
    • Nomata, J.1    Mizoguchi, T.2    Tamiaki, H.3    Fujita, Y.4
  • 86
    • 84901607004 scopus 로고    scopus 로고
    • Reconstitution of a sequential reaction of two nitrogenase-like enzymes in the bacteriochlorophyll biosynthetic pathway of Rhodobacter capsulatus
    • Yamamoto, H.; Kato, M.; Yamanashi, K.; Fujita, Y. Reconstitution of a sequential reaction of two nitrogenase-like enzymes in the bacteriochlorophyll biosynthetic pathway of Rhodobacter capsulatus. Biochem. Biophys. Res. Commun. 2014, 448, 200-205.
    • (2014) Biochem. Biophys. Res. Commun , vol.448 , pp. 200-205
    • Yamamoto, H.1    Kato, M.2    Yamanashi, K.3    Fujita, Y.4
  • 87
    • 84899732857 scopus 로고    scopus 로고
    • Chlorophyllide a oxidoreductase works as one of the divinyl reductases specifically involved in bacteriochlorophyll a biosynthesis
    • Harada, J.; Mizoguchi, T.; Tsukatani, Y.; Yokono, M.; Tanaka, A.; Tamiaki, H. Chlorophyllide a oxidoreductase works as one of the divinyl reductases specifically involved in bacteriochlorophyll a biosynthesis. J. Biol. Chem. 2014, 289, 12716-12726.
    • (2014) J. Biol. Chem , vol.289 , pp. 12716-12726
    • Harada, J.1    Mizoguchi, T.2    Tsukatani, Y.3    Yokono, M.4    Tanaka, A.5    Tamiaki, H.6
  • 88
    • 57749205180 scopus 로고    scopus 로고
    • Growth arrest of Synechocystis sp. PCC 6803 by superoxide generated from heterologously expressed Rhodobacter sphaeroides chlorophyllide a reductase
    • Kim, E.J.; Kim, J.S.; Rhee, H.J.; Lee, J.K. Growth arrest of Synechocystis sp. PCC 6803 by superoxide generated from heterologously expressed Rhodobacter sphaeroides chlorophyllide a reductase. FEBS Lett. 2009, 583, 219-223.
    • (2009) FEBS Lett , vol.583 , pp. 219-223
    • Kim, E.J.1    Kim, J.S.2    Rhee, H.J.3    Lee, J.K.4
  • 89
    • 80054705660 scopus 로고    scopus 로고
    • Heme oxygenase isoform is essential for aerobic growth in the cyanobacterium Synechocystis sp. PCC 6803: Modes of differential operation of two isoforms/enzymes to adapt to low oxygen environments in cyanobacteria
    • Aoki, R.; Goto, T.; Fujita, Y. A heme oxygenase isoform is essential for aerobic growth in the cyanobacterium Synechocystis sp. PCC 6803: Modes of differential operation of two isoforms/enzymes to adapt to low oxygen environments in cyanobacteria. Plant Cell Physiol. 2011, 52, 1744-1756.
    • (2011) Plant Cell Physiol , vol.52 , pp. 1744-1756
    • Aoki, R.1    Goto, T.2    Fujita, Y.A.3
  • 90
    • 0032127571 scopus 로고    scopus 로고
    • Phytobilin biosynthesis: Cloning and expression of a gene encoding soluble ferredoxin-dependent heme oxygenase from Synechocystis sp. PCC 6803
    • Cornejo, J.; Willows, R.D.; Beale, S.I. Phytobilin biosynthesis: Cloning and expression of a gene encoding soluble ferredoxin-dependent heme oxygenase from Synechocystis sp. PCC 6803. Plant J. 1998, 15, 99-107.
    • (1998) Plant J , vol.15 , pp. 99-107
    • Cornejo, J.1    Willows, R.D.2    Beale, S.I.3
  • 91
    • 0033905732 scopus 로고    scopus 로고
    • Phytobilin biosynthesis: The Synechocystis sp. PCC 6803 heme oxygenase-encoding ho1 gene complements a phytochrome-deficient Arabidopsis thalianna hy1 mutant
    • Willows, R.D.; Mayer, S.M.; Foulk, M.S.; DeLong, A.; Hanson, K.; Chory, J.; Beale, S.I. Phytobilin biosynthesis: The Synechocystis sp. PCC 6803 heme oxygenase-encoding ho1 gene complements a phytochrome-deficient Arabidopsis thalianna hy1 mutant. Plant Mol. Biol. 2000, 43, 113-120.
    • (2000) Plant Mol. Biol , vol.43 , pp. 113-120
    • Willows, R.D.1    Mayer, S.M.2    Foulk, M.S.3    Delong, A.4    Hanson, K.5    Chory, J.6    Beale, S.I.7
  • 92
    • 14044256465 scopus 로고    scopus 로고
    • Protein expressed by the ho2 gene of the cyanobacterium Synechocystis sp. PCC 6803 is a true heme oxygenase. Properties of the heme and enzyme complex
    • Zhang, X.; Migita, C.T.; Sato, M.; Sasahara, M.; Yoshida, T. Protein expressed by the ho2 gene of the cyanobacterium Synechocystis sp. PCC 6803 is a true heme oxygenase. Properties of the heme and enzyme complex. FEBS J. 2005, 272, 1012-1022.
    • (2005) FEBS J , vol.272 , pp. 1012-1022
    • Zhang, X.1    Migita, C.T.2    Sato, M.3    Sasahara, M.4    Yoshida, T.5
  • 93
    • 15544367847 scopus 로고    scopus 로고
    • Crystal structure of dimeric heme oxygenase-2 from Synechocystis sp. PCC 6803 in complex with heme
    • Sugishima, M.; Hagiwara, Y.; Zhang, X.; Yoshida, T.; Migita, C.T.; Fukuyama, K. Crystal structure of dimeric heme oxygenase-2 from Synechocystis sp. PCC 6803 in complex with heme. Biochemistry 2005, 44, 4257-4266.
    • (2005) Biochemistry , vol.44 , pp. 4257-4266
    • Sugishima, M.1    Hagiwara, Y.2    Zhang, X.3    Yoshida, T.4    Migita, C.T.5    Fukuyama, K.6
  • 94
    • 9644264176 scopus 로고    scopus 로고
    • Crystal structure of heme oxygenase-1 from cyanobacterium Synechocystis sp. PCC 6803 in complex with heme
    • Sugishima, M.; Migita, C.T.; Zhang, X.; Yoshida, T.; Fukuyama, K. Crystal structure of heme oxygenase-1 from cyanobacterium Synechocystis sp. PCC 6803 in complex with heme. Eur. J. Biochem. 2004, 271, 4517-4525.
    • (2004) Eur. J. Biochem , vol.271 , pp. 4517-4525
    • Sugishima, M.1    Migita, C.T.2    Zhang, X.3    Yoshida, T.4    Fukuyama, K.5
  • 95
    • 76149126413 scopus 로고    scopus 로고
    • Heme oxygenase 2 of the cyanobacterium Synechocystis sp. PCC 6803 is induced under a microaerobic atmosphere and is required for microaerobic growth at high light intensity
    • Yilmaz, M.; Kang, I.; Beale, S.I. Heme oxygenase 2 of the cyanobacterium Synechocystis sp. PCC 6803 is induced under a microaerobic atmosphere and is required for microaerobic growth at high light intensity. Photosynth. Res. 2010, 103, 47-59.
    • (2010) Photosynth. Res , vol.103 , pp. 47-59
    • Yilmaz, M.1    Kang, I.2    Beale, S.I.3
  • 96
    • 5444249703 scopus 로고    scopus 로고
    • Characterization of a heme oxygenase of Clostridium tetani and its possible role in oxygen tolerance
    • Brüggemann, H.; Bauer, R.; Raffestin, S.; Gottschalk, G. Characterization of a heme oxygenase of Clostridium tetani and its possible role in oxygen tolerance. Arch. Microbiol. 2004, 182, 259-263.
    • (2004) Arch. Microbiol , vol.182 , pp. 259-263
    • Brüggemann, H.1    Bauer, R.2    Raffestin, S.3    Gottschalk, G.4
  • 98
    • 84859773974 scopus 로고    scopus 로고
    • MarR-type transcriptional regulator ChlR activates expression of tetrapyrrole biosynthesis genes in response to low-oxygen conditions in cyanobacteria
    • Aoki, R.; Takeda, T.; Omata, T.; Ihara, K.; Fujita, Y. MarR-type transcriptional regulator ChlR activates expression of tetrapyrrole biosynthesis genes in response to low-oxygen conditions in cyanobacteria. J. Biol. Chem. 2012, 287, 13500-13507.
    • (2012) J. Biol. Chem , vol.287 , pp. 13500-13507
    • Aoki, R.1    Takeda, T.2    Omata, T.3    Ihara, K.4    Fujita, Y.5
  • 99
    • 84902440208 scopus 로고    scopus 로고
    • ChlR protein of Synechococcus sp. PCC 7002 is a transcription activator that uses an oxygen-sensitive [4Fe-4S] cluster to control genes involved in pigment biosynthesis
    • Ludwig, M.; Pandelia, M.E.; Chew, C.Y.; Zhang, B.; Golbeck, J.H.; Krebs, C.; Bryant, D.A. ChlR protein of Synechococcus sp. PCC 7002 is a transcription activator that uses an oxygen-sensitive [4Fe-4S] cluster to control genes involved in pigment biosynthesis. J. Biol. Chem. 2014, 289, 16624-16639.
    • (2014) J. Biol. Chem , vol.289 , pp. 16624-16639
    • Ludwig, M.1    Pandelia, M.E.2    Chew, C.Y.3    Zhang, B.4    Golbeck, J.H.5    Krebs, C.6    Bryant, D.A.7
  • 100
    • 84899826805 scopus 로고    scopus 로고
    • Transcriptional regulators ChlR and CnfR are essential for diazotrophic growth in nonheterocystous cyanobacteria
    • Tsujimoto, R.; Kamiya, N.; Fujita, Y. Transcriptional regulators ChlR and CnfR are essential for diazotrophic growth in nonheterocystous cyanobacteria. Proc. Natl. Acad. Sci. USA 2014, 111, 6762-6767.
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 6762-6767
    • Tsujimoto, R.1    Kamiya, N.2    Fujita, Y.3
  • 101
    • 33645858540 scopus 로고    scopus 로고
    • Regulation of virulence by members of the MarR/SlyA family
    • Ellison, D.W.; Miller, V.L. Regulation of virulence by members of the MarR/SlyA family. Curr. Opin. Microbiol. 2006, 9, 153-159.
    • (2006) Curr. Opin. Microbiol , vol.9 , pp. 153-159
    • Ellison, D.W.1    Miller, V.L.2
  • 102
    • 79951505770 scopus 로고    scopus 로고
    • Molecular mechanisms of ligand-mediated attenuation of DNA binding by MarR family transcriptional regulators
    • Perera, I.C.; Grove, A. Molecular mechanisms of ligand-mediated attenuation of DNA binding by MarR family transcriptional regulators. J. Mol. Cell Biol. 2010, 2, 243-254.
    • (2010) J. Mol. Cell Biol , vol.2 , pp. 243-254
    • Perera, I.C.1    Grove, A.2
  • 103
    • 69949138465 scopus 로고    scopus 로고
    • Crystal structures of the reduced, sulfenic acid, and mixed disulfide forms of SarZ, a redox active global regulator in Staphylococcus aureus
    • Poor, C.B.; Chen, P.R.; Duguid, E.; Rice, P.A.; He, C. Crystal structures of the reduced, sulfenic acid, and mixed disulfide forms of SarZ, a redox active global regulator in Staphylococcus aureus. J. Biol. Chem. 2009, 284, 23517-23524.
    • (2009) J. Biol. Chem. , vol.284 , pp. 23517-23524
    • Poor, C.B.1    Chen, P.R.2    Duguid, E.3    Rice, P.A.4    He, C.5
  • 105
    • 0024869570 scopus 로고
    • Influence of light on accumulation of photosynthesis-specific transcripts in the cyanobacterium Synechocystis 6803
    • Mohamed, A.; Jansson, C. Influence of light on accumulation of photosynthesis-specific transcripts in the cyanobacterium Synechocystis 6803. Plant Mol. Biol. 1989, 13, 693-700.
    • (1989) Plant Mol. Biol , vol.13 , pp. 693-700
    • Mohamed, A.1    Jansson, C.2
  • 106
    • 57449108112 scopus 로고    scopus 로고
    • Low-oxygen induction of normally cryptic psbA genes in cyanobacteria
    • Summerfield, T.C.; Toepel, J.; Sherman, L.A. Low-oxygen induction of normally cryptic psbA genes in cyanobacteria. Biochemistry 2008, 47, 12939-12941.
    • (2008) Biochemistry , vol.47 , pp. 12939-12941
    • Summerfield, T.C.1    Toepel, J.2    Sherman, L.A.3
  • 107
    • 2342447248 scopus 로고    scopus 로고
    • Variation in sulfide tolerance of photosystem II in phylogenetically diverse cyanobacteria from sulfidic habitats
    • Miller, S.R.; Bebout, B.M. Variation in sulfide tolerance of photosystem II in phylogenetically diverse cyanobacteria from sulfidic habitats. Appl. Environ. Microbiol. 2004, 70, 736-744.
    • (2004) Appl. Environ. Microbiol , vol.70 , pp. 736-744
    • Miller, S.R.1    Bebout, B.M.2
  • 108
    • 84892668033 scopus 로고    scopus 로고
    • A novel “oxygen-induced” greening process in a cyanobacterial mutant lacking the transcriptional activator ChlR involved in low-oxygen adaptation of tetrapyrrole biosynthesis
    • Aoki, R.; Hiraide, Y.; Yamakawa, H.; Fujita, Y. A novel “oxygen-induced” greening process in a cyanobacterial mutant lacking the transcriptional activator ChlR involved in low-oxygen adaptation of tetrapyrrole biosynthesis. J. Biol. Chem. 2014, 289, 1841-1851.
    • (2014) J. Biol. Chem , vol.289 , pp. 1841-1851
    • Aoki, R.1    Hiraide, Y.2    Yamakawa, H.3    Fujita, Y.4
  • 109
    • 79951491190 scopus 로고    scopus 로고
    • Gene expression under low oxygen conditions in the cyanobacterium Synechocystis sp. PCC 6803 demonstrates Hik31-dependent and-independent responses
    • Summerfield, T.C.; Nagarajan, S.; Sherman, L. Gene expression under low oxygen conditions in the cyanobacterium Synechocystis sp. PCC 6803 demonstrates Hik31-dependent and-independent responses. Microbiology 2012, 157, 301-312.
    • (2012) Microbiology , vol.157 , pp. 301-312
    • Summerfield, T.C.1    Nagarajan, S.2    Sherman, L.3
  • 111
    • 0015364291 scopus 로고
    • Nitrogenase of Klebsiella pneumoniae. Purification and properties of the component proteins
    • Eady, R.R.; Smith, B.E.; Cook, K.A.; Postgate, J.R. Nitrogenase of Klebsiella pneumoniae. Purification and properties of the component proteins. Biochem. J. 1972, 128, 655-675.
    • (1972) Biochem. J. , vol.128 , pp. 655-675
    • Eady, R.R.1    Smith, B.E.2    Cook, K.A.3    Postgate, J.R.4
  • 113
    • 84865236206 scopus 로고    scopus 로고
    • Single-cell confocal spectrometry of a filamentous cyanobacterium Nostoc at room and cryogenic temperature. Diversity and differentiation of pigment systems in 311 cells
    • Sugiura, K.; Itoh, S. Single-cell confocal spectrometry of a filamentous cyanobacterium Nostoc at room and cryogenic temperature. Diversity and differentiation of pigment systems in 311 cells. Plant Cell Physiol. 2012, 53, 1492-1506.
    • (2012) Plant Cell Physiol , vol.53 , pp. 1492-1506
    • Sugiura, K.1    Itoh, S.2
  • 114
    • 33845522034 scopus 로고    scopus 로고
    • Identification of the glycosyl transferase required for synthesis of the principal glycolipid characteristic of heterocysts of Anabaena sp. Strain PCC 7120. FEMS Microbiol
    • Awai, K.; Wolk, C.P. Identification of the glycosyl transferase required for synthesis of the principal glycolipid characteristic of heterocysts of Anabaena sp. strain PCC 7120. FEMS Microbiol. Lett. 2007, 266, 98-102.
    • (2007) Lett , vol.266 , pp. 98-102
    • Awai, K.1    Wolk, C.P.2
  • 115
    • 0037863804 scopus 로고    scopus 로고
    • Cytochrome c oxidase genes required for nitrogenase activity and diazotrophic growth in Anabaena sp. PCC 7120
    • Valladares, A.; Herrero, A.; Pils, D.; Schmetterer, G.; Flores, E. Cytochrome c oxidase genes required for nitrogenase activity and diazotrophic growth in Anabaena sp. PCC 7120. Mol. Microbiol. 2003, 47, 1239-1249.
    • (2003) Mol. Microbiol. , vol.47 , pp. 1239-1249
    • Valladares, A.1    Herrero, A.2    Pils, D.3    Schmetterer, G.4    Flores, E.5
  • 116
    • 0016155416 scopus 로고
    • Nitrogenase activity and photosynthesis in Plectonema boryanum
    • Weare, N.M.; Benemann, J.R. Nitrogenase activity and photosynthesis in Plectonema boryanum. J. Bacteriol. 1974, 119, 258-265.
    • (1974) J. Bacteriol , vol.119 , pp. 258-265
    • Weare, N.M.1    Benemann, J.R.2
  • 118
    • 0037052458 scopus 로고    scopus 로고
    • Life and the evolution of Earth’s atmosphere
    • Kasting, J.F.; Siefert, J.L. Life and the evolution of Earth’s atmosphere. Science 2002, 296, 1066-1068.
    • (2002) Science , vol.296 , pp. 1066-1068
    • Kasting, J.F.1    Siefert, J.L.2
  • 120
    • 0242608621 scopus 로고    scopus 로고
    • Pathways of oxidative damage
    • Imlay, J.A. Pathways of oxidative damage. Annu. Rev. Microbiol. 2003, 57, 395-418.
    • (2003) Annu. Rev. Microbiol , vol.57 , pp. 395-418
    • Imlay, J.A.1
  • 121
    • 33645065589 scopus 로고    scopus 로고
    • Iron-sulphur clusters and the problem with oxygen
    • Imlay, J.A. Iron-sulphur clusters and the problem with oxygen. Mol. Microbiol. 2006, 59, 1073-1082.
    • (2006) Mol. Microbiol , vol.59 , pp. 1073-1082
    • Imlay, J.A.1
  • 122
    • 23844554290 scopus 로고    scopus 로고
    • Biosynthetic pathways, gene replacement and the antiquity of life
    • Raymond, J.; Blankenship, R.E. Biosynthetic pathways, gene replacement and the antiquity of life. Geobiology 2004, 2, 199-203.
    • (2004) Geobiology , vol.2 , pp. 199-203
    • Raymond, J.1    Blankenship, R.E.2
  • 123
    • 0031666414 scopus 로고    scopus 로고
    • Analogous enzymes: Independent inventions in enzyme evolution
    • Galperin, M.Y.; Walker, D.R.; Koonin, E.V. Analogous enzymes: Independent inventions in enzyme evolution. Genome Res. 1998, 8, 779-790.
    • (1998) Genome Res , vol.8 , pp. 779-790
    • Galperin, M.Y.1    Walker, D.R.2    Koonin, E.V.3
  • 125
    • 84888615834 scopus 로고    scopus 로고
    • Characterization of bcib: A ferredoxin-dependent 8-vinyl-protochlorophyllide reductase from the green sulfur bacterium Chloroherpeton thalassium
    • Saunders, A.H.; Golbeck, J.H.; Bryant, D.A. Characterization of bcib: A ferredoxin-dependent 8-vinyl-protochlorophyllide reductase from the green sulfur bacterium Chloroherpeton thalassium. Biochemistry 2013, 52, 8442-8451.
    • (2013) Biochemistry , vol.52 , pp. 8442-8451
    • Saunders, A.H.1    Golbeck, J.H.2    Bryant, D.A.3
  • 127
    • 79955565417 scopus 로고    scopus 로고
    • Fatty acid production in genetically modified cyanobacteria
    • Liu, X.; Sheng, J.; Curtiss, R. Fatty acid production in genetically modified cyanobacteria. Proc. Natl. Acad. Sci. USA 2011, 108, 6899-6904.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 6899-6904
    • Liu, X.1    Sheng, J.2    Curtiss, R.3
  • 128
    • 79959523740 scopus 로고    scopus 로고
    • Algae: The scum solution
    • Savage, N. Algae: The scum solution. Nature 2011, 474, S15-S16.
    • (2011) Nature , vol.474 , pp. S15-S16
    • Savage, N.1
  • 129
    • 84901846248 scopus 로고    scopus 로고
    • Metabolic design for cyanobacterial chemical synthesis
    • Oliver, J.W.; Atsumi, S. Metabolic design for cyanobacterial chemical synthesis. Photosynth. Res. 2014, 120, 249-261.
    • (2014) Photosynth. Res , vol.120 , pp. 249-261
    • Oliver, J.W.1    Atsumi, S.2
  • 130
    • 34247610894 scopus 로고    scopus 로고
    • Promoting R&D in photobiological hydrogen production utilizing mariculture-raised cyanobacteria
    • Sakurai, H.; Masukawa, H. Promoting R&D in photobiological hydrogen production utilizing mariculture-raised cyanobacteria. Mar. Biotechnol. 2007, 9, 128-145.
    • (2007) Mar. Biotechnol , vol.9 , pp. 128-145
    • Sakurai, H.1    Masukawa, H.2
  • 131
    • 77955508046 scopus 로고    scopus 로고
    • Feasibility study of large-scale photobiological hydrogen production utilizing mariculture-raised cyanobacteria
    • Sakurai, H.; Masukawa, H.; Kitashima, M.; Inoue, K. A feasibility study of large-scale photobiological hydrogen production utilizing mariculture-raised cyanobacteria. Adv. Exp. Med. Biol. 2010, 675, 291-303.
    • (2010) Adv. Exp. Med. Biol , vol.675 , pp. 291-303
    • Sakurai, H.1    Masukawa, H.2    Kitashima, M.3    Inoue, K.A.4
  • 132
    • 84864002936 scopus 로고    scopus 로고
    • Genetic engineering of cyanobacteria to enhance biohydrogen production from sunlight and water
    • Masukawa, H.; Kitashima, M.; Inoue, K.; Sakurai, H.; Hausinger, R.P. Genetic engineering of cyanobacteria to enhance biohydrogen production from sunlight and water. AmBio 2012, 41, 169-173.
    • (2012) Ambio , vol.41 , pp. 169-173
    • Masukawa, H.1    Kitashima, M.2    Inoue, K.3    Sakurai, H.4    Hausinger, R.P.5
  • 133
    • 84884648088 scopus 로고    scopus 로고
    • Metabolic engineering of cyanobacteria for the production of hydrogen from water
    • Rögner, M. Metabolic engineering of cyanobacteria for the production of hydrogen from water. Biochem. Soc. Trans. 2013, 41, 1254-1259.
    • (2013) Biochem. Soc. Trans , vol.41 , pp. 1254-1259
    • Rögner, M.1
  • 134
    • 84925010268 scopus 로고    scopus 로고
    • Development of a highly-frequent in vivo transposon mutagenesis system for Synechocystis sp. PCC 6803 and Synechococcus elongatus PCC 7942
    • Watabe, K.; Mimuro, M.; Tsuchiya, T. Development of a highly-frequent in vivo transposon mutagenesis system for Synechocystis sp. PCC 6803 and Synechococcus elongatus PCC 7942. Plant Cell Physiol. 2014, 55, 2017-2026.
    • (2014) Plant Cell Physiol , vol.55 , pp. 2017-2026
    • Watabe, K.1    Mimuro, M.2    Tsuchiya, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.