[1]
|
Blankenship, R.E. (1992) Origin and Early Evolution of Photosynthesis. Photosynthesis Research, 33, 91-111.
http://link.springer.com/article/10.1007/BF00039173
http://dx.doi.org/10.1007/BF00039173
|
[2]
|
Olson, J.M. and Blankenship, R.E. (2004) Thinking about the Evolution of Photosynthesis. Photosynthesis Research, 80, 373-386. http://www.ncbi.nlm.nih.gov/pubmed/16328834
http://dx.doi.org/10.1023/B:PRES.0000030457.06495.83
|
[3]
|
Von Wettstein, D., Gough, S. and Kannangara, C.G. (1995) Chlorophyll Biosynthesis. The Plant Cell, 7, 1039-1057.
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC160907/pdf/071039.pdf
http://dx.doi.org/10.1105/tpc.7.7.1039
|
[4]
|
Golbeck, J.H. (1993) Shared Thematic Elements in Photochemical Reaction CENTERS. Proceedings of the National Academy of Sciences of the United States of America, 90, 1642-1646.
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC45935/
http://dx.doi.org/10.1073/pnas.90.5.1642
|
[5]
|
Allen, J.P. and Williams, J.C. (1998) Photosynthetic Reaction Centers. FEBS Letters, 438, 5-9.
http://onlinelibrary.wiley.com/doi/10.1016/S0014-5793%2898%2901245-9/epdf
http://dx.doi.org/10.1016/S0014-5793(98)01245-9
|
[6]
|
Nazir, S. and Khan, M.S. (2013) Integration of Novel Chlorophyll Genes from Black Pine into the Chloroplast Genome of Tobacco. Pakistan Journal of Botany, 45, 595-600.
|
[7]
|
Green, B.R., Parson, W.W. and Anderson, J.M. (2004) Photosynthetic Membranes and Their Light-Harvesting Antennas. In: Green, B.R. and Parson, W.W., Eds., Light-Harvesting Antennas in Photosynthesis, Springer, Dordrecht, 1-28.
|
[8]
|
Grimm, B., Porra, R.J., Rüdiger, W., Scheer, H., Melkozernov, A.N. and Blankenship, R.E. (2006) Chlorophylls and Bacteriochlorophylls: Biochemistry, Biophysics, Functions and Applications. In: Grimm, B., Porra, R.J., Rüdiger, W. and Scheer, H., Eds., Advances in Photosynthesis and Respiration, Springer, Dordrecht, 397-412.
https://www.researchgate.net/publication/33027242_Chlorophylls_and_Bacteriochlorophylls_Biochemistry_Biophysics_Functions_and_Applications
http://dx.doi.org/10.1007/1-4020-4516-6
|
[9]
|
Rebeiz, C.A., Ioannides, I.M., Kolossov, V. and Kopetz, K.J. (1999) Chloroplast Biogenesis 80. Proposal of a Unified multibranched Chlorophyll a/b Biosynthetic Pathway. Photosynthetica, 36, 117-128.
http://rd.springer.com/article/10.1023%2FA%3A1007027005903
|
[10]
|
Bauer, C.E., Bolllvar, D.W. and Suzukl, J.Y. (1993) Genetic Analyses of Photopigment Biosynthesis in Eubacteria: A Guiding Light for Algae and Plants. Journal of Bacteriology, 175, 3919-3925.
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC204818/pdf/jbacter00055-0013.pdf
|
[11]
|
Bollivar, D.W., Suzukl, J.Y., Beatty, J.T., Dobrowolskl, J.M. and Bauer, C.E. (1994) Directed Mutational Analysis of Bacteriochlorophyll a Biosynthesis in Rhodobacter capsulatus. Journal of Molecular Biology, 237, 622-640.
|
[12]
|
Castelfranco, P., Walker, C.J. and Welnsteln, J. (1994) Biosynthetic Studies on Chlorophylls: From Protoporphyrin IX to Protochlorophyllide. In: Chadwick, D.J. and Ackrill, K., Eds., The Biosynthesis of the Tetrapyrrole Pigments, Ciba Foundation Symposium 180, John Wiley and Sons, Chichester, England, 194-204.
http://onlinelibrary.wiley.com/doi/10.1002/9780470514535.ch11/summary
|
[13]
|
Burke, D.H., Hearst, J.E. and Sidow, A. (1993) Early Evolution of Photosynthesis: Clues from Nitrogenase and Chlorophyll Iron Proteins. Proceedings of the National Academy of Sciences of the United States of America, 90, 7134-7138.
http://dx.doi.org/10.1073/pnas.90.15.7134
|
[14]
|
Nasrulhaq-Boyce, A., Griffiths, W.T. and Jones, O.T.G. (1987) The Use of Continuous Assays to Characterize the Oxidative Cyclase That Synthesizes the Chlorophyll Isocyclic Ring. Biochemical Journal, 243, 23-29.
http://www.biochemj.org/content/243/1/23
http://dx.doi.org/10.1042/bj2430023
|
[15]
|
Simon, R., Priefer, U. and Pühler, A. (1983) A Broad Host Range Mobilization System for In Vivo Genetic Engineering: Transposon Mutagenesis in Gram Negative Bacteria. Nature Biotechnology, 1, 784-791.
http://www.nature.com/nbt/journal/v1/n9/full/nbt1183-784.html
http://dx.doi.org/10.1038/nbt1183-784
|
[16]
|
Canniffe, D.P., Jackson, P.J., Hollingshead, S., Dickman, M.J. and Hunter, C.N. (2013) 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. Biochemical Journal, 450, 397-405.
http://www.ncbi.nlm.nih.gov/pubmed/23252506
http://dx.doi.org/10.1042/BJ20121723
|
[17]
|
Canniffe D.P., Chidgey J.W. and Hunter, C.N. (2014) Elucidation of the Preferred Routes of C8-Vinyl Reduction in Chlorophyll and Bacteriochlorophyll Biosynthesis. Biochemical Journal, 462, 433-440.
http://dx.doi.org/10.1042/BJ20140163
|
[18]
|
Tripathy, B.C. and Rebeiz, C.A. (1988) Chloroplast Biogenesis 60: Conversion of Divinyl Protochlorophyllide to Monovinyl Protochlorophyllide in Green(Ing) Barley, a Dark Monovinyl/Light Divinyl Plant Species. Plant Physiology, 87, 89-94. http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1054704/
http://dx.doi.org/10.1104/pp.87.1.89
|
[19]
|
Griffiths, W.T. (1991) Protochlorophyllide Photoreduction. In: Scheer, H., Ed., Chlorophylls, CRC Press, Boca Raton, 433-449.
|
[20]
|
Beale, S.I. and Weinstein, J.D. (1991) Biosynthesis of 5-Aminolevulinic Acid in Phototrophic Organisms. In: Scheer, H., Ed., Chlorophylls, CRC Press, Boca Raton, 385-406.
|
[21]
|
Masuda, T. and Takamiya, K. (2004) Novel Insights into the Enzymology, Regulation and Physiological Functions of Light-Dependent Protochlorophyllide Oxidoreductase in Angiosperms. Photosynthesis Research, 81, 1-29.
http://www.ncbi.nlm.nih.gov/pubmed/16328844
http://dx.doi.org/10.1023/B:PRES.0000028392.80354.7c
|
[22]
|
Reinbothe, C., El Bakkouri, M., Buhr, F., Muraki, N., Nomata, J., Kurisu, G., Fujita, Y. and Reinbothe, S. (2010) Chlorophyll Biosynthesis: Spotlight on Protochlorophyllide Reduction. Trends in Plant Science, 15, 614-622.
http://www.sciencedirect.com/science/article/pii/S136013851000155X
http://dx.doi.org/10.1016/j.tplants.2010.07.002
|
[23]
|
Nomata, J., Mizoguchi, T., Tamiaki, H. and Fujita, Y. (2006) 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. The Journal of Biological Chemistry, 281, 15021-15028.
http://dx.doi.org/10.1074/jbc.M601750200
|
[24]
|
Partensky, F., Hess, W.R. and Vaulot, D. (1999) Prochlorococcus, a Marine Photosynthetic Prokaryote of Global Significance. Microbiology and Molecular Biology Reviews, 63, 106-127.
|
[25]
|
Islam, M.R., Aikawa, S., Midorikawa, T., Kashino, Y., Satoh, K. and Koike, H. (2008) Slr1923 of Synechocystis sp. PCC6803 Is Essential for Conversion of 3,8-Divinyl(Proto)Chlorophyll(Ide) to 3-Monovinyl(Proto)Chlorophyll(Ide). Plant Physiology, 148, 1068-1081. http://dx.doi.org/10.1104/pp.108.123117
|
[26]
|
Ito, H., Yokono, M., Tanaka, R. and Tanaka, A. (2008) Identification of a Novel Vinyl Reductase Gene Essential for the Biosynthesis of Monovinyl Chlorophyll in Synechocystis sp. PCC6803. The Journal of Biological Chemistry, 283, 9002-9011. http://dx.doi.org/10.1074/jbc.M708369200
|
[27]
|
Ito, H. and Tanaka, A. (2014) Evolution of a New Chlorophyll Metabolic Pathway Driven by the Dynamic Changes in Enzyme Promiscuous Activity. Plant and Cell Physiology, 55, 593-603. http://dx.doi.org/10.1093/pcp/pct203
|
[28]
|
Sousa, F.L., Shavit-Grievink, L., Allen, J.F. and Martin, W.F. (2012) Chlorophyll Biosynthesis Gene Evolution Indicates Photosystem Gene Duplication, Not Photosystem Merger, at the Origin of Oxygenic Photosynthesis. Genome Biology and Evolution, 5, 200-216. http://dx.doi.org/10.1093/gbe/evs127
|
[29]
|
Ogawa, T., Inoue, Y., Kitajima, M. and Shibata, K. (1973) Action Spectra for Biosynthesis of Chlorophylls A and B and Β-Carotene. Photochemistry and Photobiology, 18, 229-235.
http://onlinelibrary.wiley.com/doi/10.1111/j.1751-1097.1973.tb06416.x/abstract
http://dx.doi.org/10.1111/j.1751-1097.1973.tb06416.x
|
[30]
|
Wilks, H.M. and Timko, M.P. (1995) A light-Dependent Complementation System for Analysis of NADPH: Protochlorophyllide Oxidoreductase: Identification and Mutagenesis of Two Conserved Residues That Are Essential for Enzyme Activity. Proceedings of the National Academy of Sciences of the United States of America, 92, 724-728.
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC42692/pdf/pnas01481-0085.pdf
http://dx.doi.org/10.1073/pnas.92.3.724
|
[31]
|
Fujita, Y. (1996) Protochlorophyllide Reduction: A Key Step in the Greening of Plants. Plant and Cell Physiology, 37, 411-421. http://pcp.oxfordjournals.org/content/37/4/411.long
http://dx.doi.org/10.1093/oxfordjournals.pcp.a028962
|
[32]
|
Armstrong, G.A. (1998) Greening in the Dark: Light Independent Protochlorophyllide Biosynthesis from Anoxygenic Photosynthetic Bacteria to Gymnosperms. Journal of Photochemistry and Photobiology B, 43, 87-100.
http://www.sciencedirect.com/science/article/pii/S1011134498000633
http://dx.doi.org/10.1016/S1011-1344(98)00063-3
|
[33]
|
Nomata, J., Kondo, T., Mizoguchi, T., Tamiaki, H., Itoh, S. and Fujita, Y. (2014) Dark-Operative Protochlorophyllide Oxidoreductase Generates Substrate Radicals by an Iron-Sulphur Cluster in Bacteriochlorophyll Biosynthesis. Scientific ReportS, 4, Article Number: 5455. http://www.nature.com/articles/srep05455
http://dx.doi.org/10.1038/srep05455
|
[34]
|
Lebedev, N. and Imko, M.P. (1999) Protochlorophyllide Oxidoreductase B-Catalyzed Protochlorophyllide Photoreduction in Vitro: Insight into the Mechanism of Chlorophyll Formation in Light-Adapted Plants. Proceedings of the National Academy of Sciences of the United States of America, 96, 9954-9959.
http://dx.doi.org/10.1073/pnas.96.17.9954
|
[35]
|
Suzuki, J.Y., Bollivar, D.W. and Bauer, C.E. (1997) Genetic Analysis of Chlorophyll Biosynthesis. Annual Review of Genetics, 31, 61-89. http://www.annualreviews.org/doi/pdf/10.1146/annurev.genet.31.1.61
http://dx.doi.org/10.1146/annurev.genet.31.1.61
|
[36]
|
Sytina, O.A., Heyes, D.J., Hunter, C.N., Alexandre, M.T., van Stokkum, I.H., van Grondelle, R. and Groot, M.L. (2008) Conformational Changes in an Ultrafast Light-Driven Enzyme Determine Catalytic Activity. Nature, 456, 1001-1004.
http://dx.doi.org/10.1038/nature07354
|
[37]
|
Suzuki, J.Y. and Bauer, C.E. (1995) A Prokaryotic Origin for Light-Dependent Chlorophyll Biosynthesis of Plants. Proceedings of the National Academy of Sciences of the United States of America, 92, 3749-3753.
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC42039/
http://dx.doi.org/10.1073/pnas.92.9.3749
|
[38]
|
Yang, J. and Cheng, Q. (2004) Origin and Evolution of the Light-Dependent Protochlorophyllide Oxydoreductase (LPOR) Genes. Plant Biology, 6, 537-544. http://www.ncbi.nlm.nih.gov/pubmed/15375724
http://dx.doi.org/10.1055/s-2004-821270
|
[39]
|
Galperin, M.Y., Walker, D.R. and Koonin, E.V. (1998) Analogous Enzymes: Independent Inventions in Enzyme Evolution. Genome Research, 8, 779-790. http://genome.cshlp.org/content/8/8/779.long
http://dx.doi.org/10.1016/j.febslet.2006.10.014
|
[40]
|
Nomata, J., Kitashima, M., Inoue, K. and Fujita, Y. (2006) Nitrogenase Fe Protein Like Fe-Scluster Is Conserved in L-Protein (Bchl) of Dark-Operative Protochlorophyllide Reductase from Rhodobacter capsulatus. FEBS Letters, 580, 6151-6154. http://www.sciencedirect.com/science/article/pii/S0014579306012208
http://dx.doi.org/10.1016/j.febslet.2006.10.014
|
[41]
|
Yang, Z.M. and Bauer, C.E. (1990) Rhodobacter capsulatus Genes Involved in Early Steps of the Bacteriochlorophyll Biosynthetic Pathway. Journal of Bacteriology, 172, 5001-5010. http://jb.asm.org/content/172/9/5001.long
|
[42]
|
Burke, D.H., Alberti, M. and Hearst, J.E. (1993) bchFNBH Bacteriochlorophyll Synthesis Genes of Rhodobacter capsulatus and Identification of the Third Subunit of Light-Independent Protochlorophyllide Reductase in Bacteria and Plants. Journal of Bacteriology, 175, 2414-2422. http://www.ncbi.nlm.nih.gov/pmc/articles/PMC204531/
|
[43]
|
Fujita, Y. and Bauer, C.E. (2000) Reconstitution of Light-Independent Protochlorophyllide Reductase from Purified Bacteriochlorophyll and BchN-BchB Subunits—In Vitro Confirmation of Nitrogenase-Like Features of a Bacteriochlorophyll Biosynthesis Enzyme. The Journal of Biological Chemistry, 275, 23583-23588.
http://www.jbc.org/content/275/31/23583.long
http://dx.doi.org/10.1074/jbc.M002904200
|
[44]
|
Nomata, J., Swem, L.R., Bauer, C.E. and Fujita, Y. (2005) Overexpression and Characterization of Dark-Operative Protochlorophyllide reductase from Rhodobacter capsulatus. Biochimica et Biophysica Acta, 1708, 229-237.
http://www.sciencedirect.com/science/article/pii/S0005272805000794
http://dx.doi.org/10.1016/j.bbabio.2005.02.002
|
[45]
|
Muraki, N., Nomata, J., Ebata, K., Mizoguchi, T., Shiba, T., Tamiaki, H., Kurisu, G. and Fujita, Y. (2010) X-Ray Crystal Structure of the Light-Independent Protochlorophyllide Reductase. Nature, 465, 110-114.
http://www.nature.com/nature/journal/v465/n7294/full/nature08950.html
http://dx.doi.org/10.1038/nature08950
|
[46]
|
Fujita, Y. and Bauer, C.E. (2003) The Light-Independent Protochlorophyllide Reductase: A Nitrogenase-Like Enzyme Catalyzing a Key Reaction for Greening in the Dark. In: Kadish, K., Smith, K.M. and Guilard, R., Eds., Chlorophylls and Bilins: Biosynthesis, Synthesis and Degradation. Academic Press, Amsterdam, 109-156.
https://www.researchgate.net/publication/277670730_The_Light-Independent_Protochlorophyllide_Reductase_A_Nitrogenase-Like_Enzyme_Catalyzing_a_Key_Reaction_for_Greening_in_the_Dark
http://dx.doi.org/10.1016/b978-0-08-092387-1.50010-2
|
[47]
|
Nomata, J., Ogawa, T., Kitashima, M., Inoue, K. and Fujita, Y. (2008) Loss of Oocytes Due to Conditional Ablation of Murine Double Minute 2 (Mdm2) Gene Is p53-Dependent and Results in Female Sterility. FEBS Letters, 582, 1346-1350. http://linkinghub.elsevier.com/retrieve/pii/S0014-5793(08)00247-0
http://dx.doi.org/10.1016/j.febslet.2008.03.018
|
[48]
|
Xiong, J., Inoue, K. and Bauer, C.E. (1998) Tracking Molecular Evolution of Photosynthesis by Characterization of a Major Photosynthesis Gene Cluster from Heliobacillus mobilis. Proceedings of the National Academy of Sciences of the United States of America, 95, 14851-14856. http://www.ncbi.nlm.nih.gov/pmc/articles/PMC24539/
http://dx.doi.org/10.1073/pnas.95.25.14851
|
[49]
|
Watzlich, D., Brocker, M.J., Uliczka, F., Ribbe, M., Virus, S., Jahn, D., et al. (2009) Chimeric Nitrogenase-Like Enzymes of (Bacterio) Chlorophyll Biosynthesis. The Journal of Biological Chemistry, 284, 15530-15540.
http://www.jbc.org/content/284/23/15530.full
http://dx.doi.org/10.1074/jbc.M901331200
|
[50]
|
Ohyama, K., Kohchi, T., Sano, T. and Yamada, Y. (1988) Newly Identified Groups of Genes in Chloroplasts. Trends in Biochemical Sciences, 13, 19-22. http://www.cell.com/trends/biochemical-sciences/abstract/0968-0004(88)90013-8
http://dx.doi.org/10.1016/0968-0004(88)90013-8
|
[51]
|
Suzuki, J.Y. and Bauer, C.E. (1992) Light-Independent Chlorophyll Biosynthesis: lnvolvement of the Chloroplast Gene chlL (frxC). Plant Cell, 4, 929-940. http://www.ncbi.nlm.nih.gov/pmc/articles/PMC160185/pdf/040929.pdf
http://dx.doi.org/10.1105/tpc.4.8.929
|
[52]
|
Yamada, K., Matsuda, M., Fujita, Y., Matsubara, H. and Sugai, M. (1992) A frxC Homologue Exists in the Chloroplast DNAs from Various Pteridophytes and Gymnosperms. Plant and Cell Physiology, 33, 325-327.
http://pcp.oxfordjournals.org/content/33/3/325.abstract
|
[53]
|
Burke, D.H., Raubeson, L.A., Alberti, M., Hearst, J.E., Jordan, E.T., Kirch, S.A., Valinski, A.E.C., Conant, D.S. and Stein, D.B. (1993) The chlL (frxC) Gene: Phylogenetic Distribution in Vascular Plants and DNA Sequence from Polystichum acrostichoides (Pteridophyta) and Synechococcus sp. 7002 (Cyanobacteria). Plant Systematics and Evolution, 187, 89-102. http://rd.springer.com/article/10.1007%2FBF00994092
http://dx.doi.org/10.1007/BF00994092
|
[54]
|
Ji, H.W., Tang, C.Q., Li, L.B. and Kuang, T.Y. (2001) Photosynthesis Development in Dark-Grown Lotus (Nelumbo nucifera) Seedlings. Acta Botanica Sinica, 43, 1129-1133.
|
[55]
|
Chen, M. (2014) Chlorophyll Modifications and Their Spectral Extension in Oxygenic Photosynthesis. Annual Review of Biochemistry, 83, 19-41. http://dx.doi.org/10.1146/annurev-biochem-072711-162943
|
[56]
|
Kusumi, J., Sato, A. and Tachida, H. (2006) Relaxation of Functional Constraint on Light-Independent Protochlorophyllide Oxidoreductase in Thuja. Molecular Biology and Evolution, 23, 941-948.
http://mbe.oxfordjournals.org/content/23/5/941.full
http://dx.doi.org/10.1093/molbev/msj097
|
[57]
|
Fujita, Y., Takahashi, Y., Kohchi, T., Ozeki, H., Ohyama, K. and Matsubara, H. (1989) Identification of a Novel nifH-Like (frxC) Protein in Chloroplasts of the Liverwort Marchantia polymorpha. Plant Molecular Biology, 13, 551-561.
http://link.springer.com/article/10.1007%2FBF00027315
http://dx.doi.org/10.1007/BF00027315
|
[58]
|
Liu, X.Q., Xu, H. and Huang, C. (1993) Chloroplast ChlB Gene Is Required for Light-Independent Chlorophyll Accumulation in Chlamydomonas reinhardtii. Plant Molecular Biology, 23, 297-308.
http://www.ncbi.nlm.nih.gov/pubmed/8219066
http://dx.doi.org/10.1007/BF00029006
|
[59]
|
Page, C.C., Moser, C.C., Chen, X. and Dutton, P.L. (1999) Natural Engineering Principles of Electron Tunneling in Biological Oxidation-Reduction. Nature, 402, 47-52.
http://www.nature.com/nature/journal/v402/n6757/full/402047a0.html
|
[60]
|
Brocker, M.J., Schomburg, S., Heinz, D.W., Jahn, D., Schubert, W.-D. and Moser, J. (2010) Crystal Structure of the Nitrogenase-Like Dark Operative Protochlorophyllide Oxidoreductase Catalytic Complex (ChlN/ChlB)2. The Journal of Biological Chemistry, 285, 27336-27345. http://www.jbc.org/content/285/35/27336.long
http://dx.doi.org/10.1074/jbc.M110.126698
|
[61]
|
Moser, J., Lange, C., Krausze, J., Rebelein, J., Schubert, W.D., Ribbe, M.W., Heinz, D.W. and Jahn, D. (2013) Structure of ADP-Aluminium Fluoride-Stabilized Protochlorophyllide Oxidoreductase Complex. Proceedings of the National Academy of Sciences of the United States of America, 110, 2094-2098.
http://dx.doi.org/10.1073/pnas.1218303110
|
[62]
|
Tsukatani, Y., Yamamoto, H., Harada, J., Yoshitomi, T., Nomata, J., Kasahara, M., Mizoguchi, T., Fujitam, Y and Tamiaki, H. (2013) An Unexpectedly Branched Biosynthetic Pathway for Bacteriochlorophyll β Capable of Absorbing Near-Infrared Light. Scientific Reports, 3, 1217-1223. http://dx.doi.org/10.1038/srep01217
|
[63]
|
Hanada, S., Takaichi, S., Matsuura, K. and Nakamura, K. (2002) Roseiflexus castenholzii gen. nov., sp. nov., a Thermophilic, Filamentous, Photosynthetic Bacterium Which Lacks Chlorosomes. International Journal of Systematic and Evolutionary Microbiology, 52, 187-193. http://dx.doi.org/10.1099/00207713-52-1-187
|
[64]
|
Tsukatani, Y., Arada, J., Nomata, J., Yamamoto, H., Fujita, Y., Mizoguchi, T. and Tamiaki, H. (2015) Rhodobacter sphaeroides Mutants Overexpressing Chlorophyllide α Oxidoreductase of Blastochloris viridis Elucidate Functions of Enzymes in Late Bacteriochlorophyll Biosynthetic Pathways. Scientific Reports, 5, Article Number: 9741.
http://www.nature.com/articles/srep09741
http://dx.doi.org/10.1038/srep09741
|
[65]
|
Burke, D.H., Alberti, M. and Hearst, J.E. (1993) The Rhodobacter capsulatus Chlorin Reductase-Encoding Locus, bchA, Consists of Three Genes, bchX, bchY, and bchZ. Journal of Bacteriology, 175, 2407-2413.
http://www.ncbi.nlm.nih.gov/pubmed/8468299
|
[66]
|
Yamazaki, S., Nomata, J. and Fujita, Y. (2006) Differential Operation of Dual Protochlorophyllide Reductases for Chlorophyll Biosynthesis in Response to Environmental Oxygen Levels in the Cyanobacterium Leptolyngbyaboryana. Plant Physiology, 142, 911-922. http://dx.doi.org/10.1104/pp.106.086090
|
[67]
|
Shui, J., Saunders, E., Needleman, R., Nappi, M., Cooper, J., Hall, L., Kehoe, D. and Stowe-Evans, E. (2009) Light-Dependent and Light-Independent Protochlorophyllide Oxidoreductases in the Chromatically Adapting Cyanobacterium Fremyella diplosiphon UTEX 481. Plant and Cell Physiology, 50, 1507-1521.
http://pcp.oxfordjournals.org/content/50/8/1507.long
http://dx.doi.org/10.1093/pcp/pcp095
|
[68]
|
Tamiaki, H., Teramura, M. and Tsukatani, Y. (2015) Reduction Processes in Biosynthesis of Chlorophyll Molecules: Chemical Implication of Enzymatically Regio- and Stereoselective Hydrogenations in the Late Stages of Their Biosynthetic Pathway. Bulletin of the Chemical Society of Japan, 89, 161-173.
https://www.jstage.jst.go.jp/article/bcsj/advpub/0/advpub_20150307/_article
http://dx.doi.org/10.1246/bcsj.20150307
|
[69]
|
Wittenberg, J.B., Appleby, C.A., Bergersen, F.J. and Turner, G.L. (1877) Leghemoglobin: The Role of Hemoglobin in the Nitrogen-Fixing Legume Root Nodule. Annals of the New York Academy of Sciences, 244, 28-34.
http://dx.doi.org/10.1111/j.1749-6632.1975.tb41519.x
|
[70]
|
Cheng, Q. (2008) Perspectives in Biological Nitrogen Fixation Research. Journal of Integrative Plant Biology, 50, 784-796. http://www.ncbi.nlm.nih.gov/pubmed/18713389
http://dx.doi.org/10.1111/j.1744-7909.2008.00700.x
|
[71]
|
Cheng, Q, Zhang, Y., Sun, W.L., Liu, G.X., Li, M.Z., Li, Y.N., Yan, Y.L. and Lin, M. (2014) How Prokaryotic Microbes Fix Nitrogen? Current Trends in Microbiology, 9, 19-34.
http://www.researchtrends.net/tia/abstract.asp?in=0&vn=9&tid=41&aid=5573&pub=2014&type
|
[72]
|
Yates, M.G. (1992) The Enzymology of Molybdenum-Dependent Nitrogen Fixation. In: Stacey, G., Burris, R.H. and Evans, H.J, Eds., Biological Nitrogen Fixation, Chapman and Hall, New York, 685-735.
|
[73]
|
Igarashi, R.Y. and Seefeldt, L.C. (2003) Nitrogen Fixation: The Mechanism of the Mo-Dependent Nitrogenase. Critical Reviews in Biochemistry and Molecular Biology, 38, 351-384. http://dx.doi.org/10.1080/10409230391036766
|
[74]
|
Kim, C.-H. and Rees, D.C. (1992) Structural Models for the Metal Centers in the Nitrogenase Molybdenum-Iron Protein. Science, 257, 1677-1682. http://www.sciencemag.org/content/257/5077/1677.long
http://dx.doi.org/10.1126/science.1529354
|
[75]
|
Raymond, J., Siefert, J.L., Staples, C.R. and Blankenship, R.E. (2004) The Natural History of Nitrogen Fixation. Molecular Biology and Evolution, 21, 541-554. http://mbe.oxfordjournals.org/content/21/3/541.full.pdf+html
http://dx.doi.org/10.1093/molbev/msh047
|
[76]
|
Fujita, Y., Takagi H. and Hase T. (1998) Cloning of the Gene Encoding a Protochlorophyllide Reductase: The Physiological Significance of Co-Existence of Light-Dependent and -Independent Protochlorophyllide Reduction Systems in the Cyanobacterium Pleconema boryanum. Plant and Cell Physiology, 39, 177-185.
http://dx.doi.org/10.1093/oxfordjournals.pcp.a029355
|
[77]
|
Yamamoto, H., Nomata, J. and Fujita, Y. (2008) Functional Expression of Nitrogenase-Like Protochlorophyllide Reductase from Rhodobacter capsulatus in Escherichia coli. Photochemical & Photobiological Sciences, 7, 1238-1242.
http://pubs.rsc.org/en/content/articlepdf/2008/pp/b802427h
http://dx.doi.org/10.1039/b802427h
|
[78]
|
Tamura, K., Stecher, G., Peterson, D., Filipski, A. and Kumar, S. (2013) MEGA6 Molecular Evolutionary Genetics Analysis Version 6.0. Molecular Biology and Evolution, 30, 2725-2729. http://www.kumarlab.net
http://dx.doi.org/10.1093/molbev/mst197
|