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Volumn 63, Issue , 2013, Pages 195-272

The globins of cyanobacteria and algae

Author keywords

Chlamydomonas; Cyanobacteria; Haem; Nostoc; Photosynthetic microbe; Reactive oxygen nitrogen species; Synechococcus; Synechocystis; Truncated haemoglobins

Indexed keywords

GLOBIN; HEMOGLOBIN; NITRIC OXIDE;

EID: 84884183812     PISSN: 00652911     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-407693-8.00006-6     Document Type: Chapter
Times cited : (15)

References (185)
  • 1
    • 0042386609 scopus 로고    scopus 로고
    • The relationship between sequence and interaction divergence in proteins
    • Aloy P., Ceulemans H., Stark A., Russell R.B. The relationship between sequence and interaction divergence in proteins. Journal of Molecular Biology 2003, 332:989-998.
    • (2003) Journal of Molecular Biology , vol.332 , pp. 989-998
    • Aloy, P.1    Ceulemans, H.2    Stark, A.3    Russell, R.B.4
  • 2
    • 0346100520 scopus 로고    scopus 로고
    • Peroxynitrite reactivity with amino acids and proteins
    • Alvarez B., Radi R. Peroxynitrite reactivity with amino acids and proteins. Amino Acids 2003, 25:295-311.
    • (2003) Amino Acids , vol.25 , pp. 295-311
    • Alvarez, B.1    Radi, R.2
  • 3
    • 0028022092 scopus 로고
    • Analysis of the sequences within and flanking the cyanoglobin-encoding gene, glbN, of the cyanobacterium Nostoc commune UTEX 584
    • Angeloni S.V., Potts M. Analysis of the sequences within and flanking the cyanoglobin-encoding gene, glbN, of the cyanobacterium Nostoc commune UTEX 584. Gene 1994, 146:133-134.
    • (1994) Gene , vol.146 , pp. 133-134
    • Angeloni, S.V.1    Potts, M.2
  • 5
    • 23844464979 scopus 로고    scopus 로고
    • Characterization of a model system for the study of Nostoc punctiforme akinetes
    • Argueta C., Summers M.L. Characterization of a model system for the study of Nostoc punctiforme akinetes. Archives of Microbiology 2005, 183:338-346.
    • (2005) Archives of Microbiology , vol.183 , pp. 338-346
    • Argueta, C.1    Summers, M.L.2
  • 7
    • 84873807248 scopus 로고    scopus 로고
    • Reactivity of the human hemoglobin "Dark side"
    • Ascenzi P., Leboffe L., Polticelli F. Reactivity of the human hemoglobin "Dark side". IUBMB Life 2013, 65:121-126.
    • (2013) IUBMB Life , vol.65 , pp. 121-126
    • Ascenzi, P.1    Leboffe, L.2    Polticelli, F.3
  • 8
    • 19444377129 scopus 로고    scopus 로고
    • Lifting the lid on Pandora's box: The Bardet-Biedl syndrome
    • Beales P.L. Lifting the lid on Pandora's box: The Bardet-Biedl syndrome. Current Opinion in Genetics & Development 2005, 15:315-323.
    • (2005) Current Opinion in Genetics & Development , vol.15 , pp. 315-323
    • Beales, P.L.1
  • 10
    • 84856503492 scopus 로고    scopus 로고
    • The diversity of cyanobacterial metabolism: Genome analysis of multiple phototrophic microorganisms
    • Beck C., Knoop H., Axmann I.M., Steuer R. The diversity of cyanobacterial metabolism: Genome analysis of multiple phototrophic microorganisms. BMC Genomics 2012, 13:56.
    • (2012) BMC Genomics , vol.13 , pp. 56
    • Beck, C.1    Knoop, H.2    Axmann, I.M.3    Steuer, R.4
  • 12
    • 81855175401 scopus 로고    scopus 로고
    • The diversity of microbial responses to nitric oxide and agents of nitrosative stress: Close cousins but not identical twins
    • Bowman L.A.H., McLean S., Poole R.K., Fukuto J.M. The diversity of microbial responses to nitric oxide and agents of nitrosative stress: Close cousins but not identical twins. Advances in Microbial Physiology 2011, 59:135-219.
    • (2011) Advances in Microbial Physiology , vol.59 , pp. 135-219
    • Bowman, L.A.H.1    McLean, S.2    Poole, R.K.3    Fukuto, J.M.4
  • 15
    • 33749548848 scopus 로고    scopus 로고
    • Prokaryotic photosynthesis and phototrophy illuminated
    • Bryant D.A., Frigaard N.U. Prokaryotic photosynthesis and phototrophy illuminated. Trends in Microbiology 2006, 14:488-496.
    • (2006) Trends in Microbiology , vol.14 , pp. 488-496
    • Bryant, D.A.1    Frigaard, N.U.2
  • 16
    • 0036219963 scopus 로고    scopus 로고
    • Cytoglobin: A novel globin type ubiquitously expressed in vertebrate tissues
    • Burmester T., Ebner B., Weich B., Hankeln T. Cytoglobin: A novel globin type ubiquitously expressed in vertebrate tissues. Molecular Biology and Evolution 2002, 19:416-421.
    • (2002) Molecular Biology and Evolution , vol.19 , pp. 416-421
    • Burmester, T.1    Ebner, B.2    Weich, B.3    Hankeln, T.4
  • 17
  • 18
    • 55549090692 scopus 로고    scopus 로고
    • DNA microarray comparisons of plant factor- and nitrogen deprivation-induced hormogonia reveal decision-making transcriptional regulation patterns in Nostoc punctiforme
    • Campbell E.L., Christman H., Meeks J.C. DNA microarray comparisons of plant factor- and nitrogen deprivation-induced hormogonia reveal decision-making transcriptional regulation patterns in Nostoc punctiforme. Journal of Bacteriology 2008, 190:7382-7391.
    • (2008) Journal of Bacteriology , vol.190 , pp. 7382-7391
    • Campbell, E.L.1    Christman, H.2    Meeks, J.C.3
  • 19
    • 0000283033 scopus 로고
    • Characteristics of hormogonia formation by symbiotic Nostoc spp. in response to the presence of Anthoceros punctatus or its extracellular products
    • Campbell E.L., Meeks J.C. Characteristics of hormogonia formation by symbiotic Nostoc spp. in response to the presence of Anthoceros punctatus or its extracellular products. Applied and Environmental Microbiology 1989, 55:125-131.
    • (1989) Applied and Environmental Microbiology , vol.55 , pp. 125-131
    • Campbell, E.L.1    Meeks, J.C.2
  • 20
    • 34447543003 scopus 로고    scopus 로고
    • Global gene expression patterns of Nostoc punctiforme in steady-state dinitrogen-grown heterocyst-containing cultures and at single time points during the differentiation of akinetes and hormogonia
    • Campbell E.L., Summers M.L., Christman H., Martin M.E., Meeks J.C. Global gene expression patterns of Nostoc punctiforme in steady-state dinitrogen-grown heterocyst-containing cultures and at single time points during the differentiation of akinetes and hormogonia. Journal of Bacteriology 2007, 189:5247-5256.
    • (2007) Journal of Bacteriology , vol.189 , pp. 5247-5256
    • Campbell, E.L.1    Summers, M.L.2    Christman, H.3    Martin, M.E.4    Meeks, J.C.5
  • 21
    • 84855829776 scopus 로고    scopus 로고
    • Global transcription profiles of the nitrogen stress response resulting in heterocyst or hormogonium development in Nostoc punctiforme
    • Christman H.D., Campbell E.L., Meeks J.C. Global transcription profiles of the nitrogen stress response resulting in heterocyst or hormogonium development in Nostoc punctiforme. Journal of Bacteriology 2011, 193:6874-6886.
    • (2011) Journal of Bacteriology , vol.193 , pp. 6874-6886
    • Christman, H.D.1    Campbell, E.L.2    Meeks, J.C.3
  • 24
    • 0033866598 scopus 로고    scopus 로고
    • Structural investigations of the hemoglobin of the cyanobacterium Synechocystis PCC 6803 reveal a unique distal heme pocket
    • Couture M., Das T.K., Savard P.Y., Ouellet Y., Wittenberg J.B., Wittenberg B.A., et al. Structural investigations of the hemoglobin of the cyanobacterium Synechocystis PCC 6803 reveal a unique distal heme pocket. European Journal of Biochemistry 2000, 267:4770-4780.
    • (2000) European Journal of Biochemistry , vol.267 , pp. 4770-4780
    • Couture, M.1    Das, T.K.2    Savard, P.Y.3    Ouellet, Y.4    Wittenberg, J.B.5    Wittenberg, B.A.6
  • 25
    • 0030432481 scopus 로고    scopus 로고
    • Purification and spectroscopic characterization of a recombinant chloroplastic hemoglobin from the green unicellular alga Chlamydomonas eugametos
    • Couture M., Guertin M. Purification and spectroscopic characterization of a recombinant chloroplastic hemoglobin from the green unicellular alga Chlamydomonas eugametos. European Journal of Biochemistry 1996, 242:779-787.
    • (1996) European Journal of Biochemistry , vol.242 , pp. 779-787
    • Couture, M.1    Guertin, M.2
  • 26
    • 77954828486 scopus 로고    scopus 로고
    • Role of heme in the unfolding and assembly of myoglobin
    • Culbertson D.S., Olson J.S. Role of heme in the unfolding and assembly of myoglobin. Biochemistry 2010, 49:6052-6063.
    • (2010) Biochemistry , vol.49 , pp. 6052-6063
    • Culbertson, D.S.1    Olson, J.S.2
  • 27
    • 84870564943 scopus 로고    scopus 로고
    • Algal genomes reveal evolutionary mosaicism and the fate of nucleomorphs
    • Curtis B.A., Tanifuji G., Burki F., Gruber A., Irimia M., Maruyama S., et al. Algal genomes reveal evolutionary mosaicism and the fate of nucleomorphs. Nature 2012, 492:59-65.
    • (2012) Nature , vol.492 , pp. 59-65
    • Curtis, B.A.1    Tanifuji, G.2    Burki, F.3    Gruber, A.4    Irimia, M.5    Maruyama, S.6
  • 28
    • 0033576249 scopus 로고    scopus 로고
    • Identification of the ligands to the ferric heme of Chlamydomonas chloroplast hemoglobin: Evidence for ligation of tyrosine-63 (B10) to the heme
    • Das T.K., Couture M., Lee H.C., Peisach J., Rousseau D.L., Wittenberg B.A., et al. Identification of the ligands to the ferric heme of Chlamydomonas chloroplast hemoglobin: Evidence for ligation of tyrosine-63 (B10) to the heme. Biochemistry 1999, 38:15360-15368.
    • (1999) Biochemistry , vol.38 , pp. 15360-15368
    • Das, T.K.1    Couture, M.2    Lee, H.C.3    Peisach, J.4    Rousseau, D.L.5    Wittenberg, B.A.6
  • 29
    • 0018390275 scopus 로고
    • Chlorophyllin-apomyoglobin complexes
    • Davis R.C., Pearlstein R.M. Chlorophyllin-apomyoglobin complexes. Nature 1979, 280:413-415.
    • (1979) Nature , vol.280 , pp. 413-415
    • Davis, R.C.1    Pearlstein, R.M.2
  • 30
    • 0026589565 scopus 로고
    • On the use of iron octa-alkylporphyrins as models for protoporphyrin IX-containing heme systems in studies employing magnetic circular dichroism spectroscopy
    • Dawson J.H., Kadkhodayan S., Zhuang C., Sono M. On the use of iron octa-alkylporphyrins as models for protoporphyrin IX-containing heme systems in studies employing magnetic circular dichroism spectroscopy. Journal of Inorganic Biochemistry 1992, 45:179-192.
    • (1992) Journal of Inorganic Biochemistry , vol.45 , pp. 179-192
    • Dawson, J.H.1    Kadkhodayan, S.2    Zhuang, C.3    Sono, M.4
  • 32
    • 17144408393 scopus 로고    scopus 로고
    • Structure-function relationships in the growing hexa-coordinate hemoglobin sub-family
    • de Sanctis D., Pesce A., Nardini M., Bolognesi M., Bocedi A., Ascenzi P. Structure-function relationships in the growing hexa-coordinate hemoglobin sub-family. IUBMB Life 2004, 56:643-651.
    • (2004) IUBMB Life , vol.56 , pp. 643-651
    • de Sanctis, D.1    Pesce, A.2    Nardini, M.3    Bolognesi, M.4    Bocedi, A.5    Ascenzi, P.6
  • 33
    • 0027173647 scopus 로고
    • Detection and quantitation of heme-containing proteins by chemiluminescence
    • Dorward D.W. Detection and quantitation of heme-containing proteins by chemiluminescence. Analytical Biochemistry 1993, 209:219-223.
    • (1993) Analytical Biochemistry , vol.209 , pp. 219-223
    • Dorward, D.W.1
  • 34
    • 0030811194 scopus 로고    scopus 로고
    • Expression, purification, and properties of recombinant barley (Hordeum sp.) hemoglobin. Optical spectra and reactions with gaseous ligands
    • Duff S.M., Wittenberg J.B., Hill R.D. Expression, purification, and properties of recombinant barley (Hordeum sp.) hemoglobin. Optical spectra and reactions with gaseous ligands. The Journal of Biological Chemistry 1997, 272:16746-16752.
    • (1997) The Journal of Biological Chemistry , vol.272 , pp. 16746-16752
    • Duff, S.M.1    Wittenberg, J.B.2    Hill, R.D.3
  • 35
    • 0037073478 scopus 로고    scopus 로고
    • The solution structure of the recombinant hemoglobin from the cyanobacterium Synechocystis sp. PCC 6803 in its hemichrome state
    • Falzone C.J., Vu B.C., Scott N.L., Lecomte J.T.J. The solution structure of the recombinant hemoglobin from the cyanobacterium Synechocystis sp. PCC 6803 in its hemichrome state. Journal of Molecular Biology 2002, 324:1015-1029.
    • (2002) Journal of Molecular Biology , vol.324 , pp. 1015-1029
    • Falzone, C.J.1    Vu, B.C.2    Scott, N.L.3    Lecomte, J.T.J.4
  • 37
    • 0002812776 scopus 로고
    • Assimilatory nitrogen metabolism and its regulation
    • Kluwer Academic Publishers, Dordrecht, The Netherlands, D.A. Bryant (Ed.)
    • Flores E., Herrero A. Assimilatory nitrogen metabolism and its regulation. The molecular biology of cyanobacteria 1994, 487-517. Kluwer Academic Publishers, Dordrecht, The Netherlands. D.A. Bryant (Ed.).
    • (1994) The molecular biology of cyanobacteria , pp. 487-517
    • Flores, E.1    Herrero, A.2
  • 38
    • 10444268100 scopus 로고    scopus 로고
    • Globin-coupled sensors, protoglobins, and the last universal common ancestor
    • Freitas T.A., Saito J.A., Hou S., Alam M. Globin-coupled sensors, protoglobins, and the last universal common ancestor. Journal of Inorganic Biochemistry 2005, 99:23-33.
    • (2005) Journal of Inorganic Biochemistry , vol.99 , pp. 23-33
    • Freitas, T.A.1    Saito, J.A.2    Hou, S.3    Alam, M.4
  • 39
    • 32944462917 scopus 로고    scopus 로고
    • The amphibian globin gene repertoire as revealed by the Xenopus genome
    • Fuchs C., Burmester T., Hankeln T. The amphibian globin gene repertoire as revealed by the Xenopus genome. Cytogenetic and Genome Research 2006, 112:296-306.
    • (2006) Cytogenetic and Genome Research , vol.112 , pp. 296-306
    • Fuchs, C.1    Burmester, T.2    Hankeln, T.3
  • 40
    • 2642570165 scopus 로고    scopus 로고
    • Zebrafish reveals different and conserved features of vertebrate neuroglobin gene structure, expression pattern, and ligand binding
    • Fuchs C., Heib V., Kiger L., Haberkamp M., Roesner A., Schmidt M., et al. Zebrafish reveals different and conserved features of vertebrate neuroglobin gene structure, expression pattern, and ligand binding. The Journal of Biological Chemistry 2004, 279:24116-24122.
    • (2004) The Journal of Biological Chemistry , vol.279 , pp. 24116-24122
    • Fuchs, C.1    Heib, V.2    Kiger, L.3    Haberkamp, M.4    Roesner, A.5    Schmidt, M.6
  • 41
    • 0026815409 scopus 로고
    • The early genetic response to light in the green unicellular alga Chlamydomonas eugametos grown under light dark cycles involves genes that represent direct responses to light and photosynthesis
    • Gagné G., Guertin M. The early genetic response to light in the green unicellular alga Chlamydomonas eugametos grown under light dark cycles involves genes that represent direct responses to light and photosynthesis. Plant Molecular Biology 1992, 18:429-445.
    • (1992) Plant Molecular Biology , vol.18 , pp. 429-445
    • Gagné, G.1    Guertin, M.2
  • 42
    • 10644291828 scopus 로고    scopus 로고
    • Nitric oxide dioxygenase function and mechanism of flavohemoglobin, hemoglobin, myoglobin and their associated reductases
    • Gardner P.R. Nitric oxide dioxygenase function and mechanism of flavohemoglobin, hemoglobin, myoglobin and their associated reductases. Journal of Inorganic Biochemistry 2005, 99:247-266.
    • (2005) Journal of Inorganic Biochemistry , vol.99 , pp. 247-266
    • Gardner, P.R.1
  • 43
    • 84877806490 scopus 로고    scopus 로고
    • Hemoglobin, a nitric-oxide dioxygenase
    • Gardner P.R. Hemoglobin, a nitric-oxide dioxygenase. Scientifica 2012, 2012. 10.6064/2012/683729.
    • (2012) Scientifica , vol.2012
    • Gardner, P.R.1
  • 44
    • 0034724887 scopus 로고    scopus 로고
    • Steady-state and transient kinetics of Escherichia coli nitric-oxide dioxygenase (flavohemoglobin). The B10 tyrosine hydroxyl is essential for dioxygen binding and catalysis
    • Gardner A.M., Martin L.A., Gardner P.R., Dou Y., Olson J.S. Steady-state and transient kinetics of Escherichia coli nitric-oxide dioxygenase (flavohemoglobin). The B10 tyrosine hydroxyl is essential for dioxygen binding and catalysis. The Journal of Biological Chemistry 2000, 275:12581-12589.
    • (2000) The Journal of Biological Chemistry , vol.275 , pp. 12581-12589
    • Gardner, A.M.1    Martin, L.A.2    Gardner, P.R.3    Dou, Y.4    Olson, J.S.5
  • 46
    • 0009695370 scopus 로고
    • The oxidation of myoglobin to metmyoglobin by oxygen. III. Kinetic studies in the presence of carbon monoxide, and at different hydrogen-ion concentrations with considerations regarding the stability of oxymyoglobin
    • George P., Stratmann C.J. The oxidation of myoglobin to metmyoglobin by oxygen. III. Kinetic studies in the presence of carbon monoxide, and at different hydrogen-ion concentrations with considerations regarding the stability of oxymyoglobin. Biochemistry Journal 1954, 57:568-573.
    • (1954) Biochemistry Journal , vol.57 , pp. 568-573
    • George, P.1    Stratmann, C.J.2
  • 48
    • 61849150615 scopus 로고    scopus 로고
    • The new chemical biology of nitrite reactions with hemoglobin: R-state catalysis, oxidative denitrosylation, and nitrite reductase/anhydrase
    • Gladwin M.T., Grubina R., Doyle M.P. The new chemical biology of nitrite reactions with hemoglobin: R-state catalysis, oxidative denitrosylation, and nitrite reductase/anhydrase. Accounts of Chemical Research 2009, 42:157-167.
    • (2009) Accounts of Chemical Research , vol.42 , pp. 157-167
    • Gladwin, M.T.1    Grubina, R.2    Doyle, M.P.3
  • 49
    • 0025766849 scopus 로고
    • Transgenic expression of aminoglycoside adenine transferase in the chloroplast: A selectable marker of site-directed transformation of chlamydomonas
    • Goldschmidt-Clermont M. Transgenic expression of aminoglycoside adenine transferase in the chloroplast: A selectable marker of site-directed transformation of chlamydomonas. Nucleic Acids Research 1991, 19:4083-4089.
    • (1991) Nucleic Acids Research , vol.19 , pp. 4083-4089
    • Goldschmidt-Clermont, M.1
  • 50
    • 77955686486 scopus 로고    scopus 로고
    • RNA-Seq analysis of sulfur-deprived Chlamydomonas cells reveals aspects of acclimation critical for cell survival
    • Gonzalez-Ballester D., Casero D., Cokus S., Pellegrini M., Merchant S.S., Grossman A.R. RNA-Seq analysis of sulfur-deprived Chlamydomonas cells reveals aspects of acclimation critical for cell survival. The Plant Cell 2010, 22:2058-2084.
    • (2010) The Plant Cell , vol.22 , pp. 2058-2084
    • Gonzalez-Ballester, D.1    Casero, D.2    Cokus, S.3    Pellegrini, M.4    Merchant, S.S.5    Grossman, A.R.6
  • 52
    • 78650251773 scopus 로고    scopus 로고
    • Phylogenomic analysis of the Chlamydomonas genome unmasks proteins potentially involved in photosynthetic function and regulation
    • Grossman A.R., Karpowicz S.J., Heinnickel M., Dewez D., Hamel B., Dent R., et al. Phylogenomic analysis of the Chlamydomonas genome unmasks proteins potentially involved in photosynthetic function and regulation. Photosynthesis Research 2010, 106:3-17.
    • (2010) Photosynthesis Research , vol.106 , pp. 3-17
    • Grossman, A.R.1    Karpowicz, S.J.2    Heinnickel, M.3    Dewez, D.4    Hamel, B.5    Dent, R.6
  • 53
    • 33845674111 scopus 로고    scopus 로고
    • Influence of the protein matrix on intramolecular histidine ligation in ferric and ferrous hexacoordinate hemoglobins
    • Halder P., Trent J.T., Hargrove M.S. Influence of the protein matrix on intramolecular histidine ligation in ferric and ferrous hexacoordinate hemoglobins. Proteins 2007, 66:172-182.
    • (2007) Proteins , vol.66 , pp. 172-182
    • Halder, P.1    Trent, J.T.2    Hargrove, M.S.3
  • 55
    • 0033729233 scopus 로고    scopus 로고
    • A flash photolysis method to characterize hexacoordinate hemoglobin kinetics
    • Hargrove M.S. A flash photolysis method to characterize hexacoordinate hemoglobin kinetics. Biophysical Journal 2000, 79:2733-2738.
    • (2000) Biophysical Journal , vol.79 , pp. 2733-2738
    • Hargrove, M.S.1
  • 62
    • 0035486999 scopus 로고    scopus 로고
    • A globin-coupled oxygen sensor from the facultatively alkaliphilic Bacillus halodurans C-125
    • Hou S., Belisle C., Lam S., Piatibratov M., Sivozhelezov V., Takami H., et al. A globin-coupled oxygen sensor from the facultatively alkaliphilic Bacillus halodurans C-125. Extremophiles 2001, 5:351-354.
    • (2001) Extremophiles , vol.5 , pp. 351-354
    • Hou, S.1    Belisle, C.2    Lam, S.3    Piatibratov, M.4    Sivozhelezov, V.5    Takami, H.6
  • 65
    • 33846519418 scopus 로고    scopus 로고
    • Covalent heme attachment in Synechocystis hemoglobin is required to prevent ferrous heme dissociation
    • Hoy J.A., Smagghe B.J., Halder P., Hargrove M.S. Covalent heme attachment in Synechocystis hemoglobin is required to prevent ferrous heme dissociation. Protein Science 2007, 16:250-260.
    • (2007) Protein Science , vol.16 , pp. 250-260
    • Hoy, J.A.1    Smagghe, B.J.2    Halder, P.3    Hargrove, M.S.4
  • 68
    • 33744521045 scopus 로고    scopus 로고
    • Two flagellar genes, AGG2 and AGG3, mediate orientation to light in Chlamydomonas
    • Iomini C., Li L., Mo W., Dutcher S.K., Piperno G. Two flagellar genes, AGG2 and AGG3, mediate orientation to light in Chlamydomonas. Current Biology 2006, 16:1147-1153.
    • (2006) Current Biology , vol.16 , pp. 1147-1153
    • Iomini, C.1    Li, L.2    Mo, W.3    Dutcher, S.K.4    Piperno, G.5
  • 69
    • 0024974873 scopus 로고
    • Protozoan myoglobin from Paramecium caudatum. Its unusual amino acid sequence
    • Iwaasa H., Takagi T., Shikama K. Protozoan myoglobin from Paramecium caudatum. Its unusual amino acid sequence. Journal of Molecular Biology 1989, 208:355-358.
    • (1989) Journal of Molecular Biology , vol.208 , pp. 355-358
    • Iwaasa, H.1    Takagi, T.2    Shikama, K.3
  • 70
    • 0025281025 scopus 로고
    • Protozoan hemoglobin from Tetrahymena pyriformis. Isolation, characterization, and amino acid sequence
    • Iwaasa H., Takagi T., Shikama K. Protozoan hemoglobin from Tetrahymena pyriformis. Isolation, characterization, and amino acid sequence. The Journal of Biological Chemistry 1990, 265:8603-8609.
    • (1990) The Journal of Biological Chemistry , vol.265 , pp. 8603-8609
    • Iwaasa, H.1    Takagi, T.2    Shikama, K.3
  • 71
    • 0031904598 scopus 로고    scopus 로고
    • Conservation of the conformation of the porphyrin macrocycle in hemoproteins
    • Jentzen W., Ma J.G., Shelnutt J.A. Conservation of the conformation of the porphyrin macrocycle in hemoproteins. Biophysical Journal 1998, 74:753-763.
    • (1998) Biophysical Journal , vol.74 , pp. 753-763
    • Jentzen, W.1    Ma, J.G.2    Shelnutt, J.A.3
  • 73
    • 0030606607 scopus 로고    scopus 로고
    • Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions
    • Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., et al. Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions. DNA Research 1996, 3:109-136.
    • (1996) DNA Research , vol.3 , pp. 109-136
    • Kaneko, T.1    Sato, S.2    Kotani, H.3    Tanaka, A.4    Asamizu, E.5    Nakamura, Y.6
  • 74
    • 13244259056 scopus 로고    scopus 로고
    • Diversity and evolutionary history of plastids and their hosts
    • Keeling P.J. Diversity and evolutionary history of plastids and their hosts. American Journal of Botany 2004, 91:1481-1493.
    • (2004) American Journal of Botany , vol.91 , pp. 1481-1493
    • Keeling, P.J.1
  • 75
    • 0001149591 scopus 로고
    • Haemoglobin in protozoa
    • Keilin D., Ryley J.F. Haemoglobin in protozoa. Nature 1953, 172:451-452.
    • (1953) Nature , vol.172 , pp. 451-452
    • Keilin, D.1    Ryley, J.F.2
  • 76
    • 79957794175 scopus 로고    scopus 로고
    • Electron transfer function versus oxygen delivery: A comparative study for several hexacoordinated globins across the animal kingdom
    • Kiger L., Tilleman L., Geuens E., Hoogewijs D., Lechauve C., Moens L., et al. Electron transfer function versus oxygen delivery: A comparative study for several hexacoordinated globins across the animal kingdom. PLoS One 2011, 6:e20478.
    • (2011) PLoS One , vol.6
    • Kiger, L.1    Tilleman, L.2    Geuens, E.3    Hoogewijs, D.4    Lechauve, C.5    Moens, L.6
  • 77
    • 70349309436 scopus 로고    scopus 로고
    • Cytochrome c biogenesis: Mechanisms for covalent modifications and trafficking of heme and for heme-iron redox control
    • Kranz R.G., Richard-Fogal C., Taylor J.-S., Frawley E.R. Cytochrome c biogenesis: Mechanisms for covalent modifications and trafficking of heme and for heme-iron redox control. Microbiology and Molecular Biology Reviews 2009, 73:510-528.
    • (2009) Microbiology and Molecular Biology Reviews , vol.73 , pp. 510-528
    • Kranz, R.G.1    Richard-Fogal, C.2    Taylor, J.-S.3    Frawley, E.R.4
  • 78
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. Journal of Applied Crystallography 1991, 24:946-950.
    • (1991) Journal of Applied Crystallography , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 79
  • 81
  • 82
    • 0001165867 scopus 로고    scopus 로고
    • Nuclear magnetic resonance of hemoproteins
    • Academic Press, Burlington, MA
    • La Mar G.N., Satterlee J.D., de Ropp J.S. Nuclear magnetic resonance of hemoproteins. The porphyrin handbook 2000, Vol. 5:185-298. Academic Press, Burlington, MA.
    • (2000) The porphyrin handbook , vol.5 , pp. 185-298
    • La Mar, G.N.1    Satterlee, J.D.2    de Ropp, J.S.3
  • 85
    • 76149101303 scopus 로고    scopus 로고
    • The Chlamydomonas reinhardtii BBSome is an IFT cargo required for export of specific signaling proteins from flagella
    • Lechtreck K.F., Johnson E.C., Sakai T., Cochran D., Ballif B.A., Rush J., et al. The Chlamydomonas reinhardtii BBSome is an IFT cargo required for export of specific signaling proteins from flagella. The Journal of Cell Biology 2009, 187:1117-1132.
    • (2009) The Journal of Cell Biology , vol.187 , pp. 1117-1132
    • Lechtreck, K.F.1    Johnson, E.C.2    Sakai, T.3    Cochran, D.4    Ballif, B.A.5    Rush, J.6
  • 86
    • 0035967512 scopus 로고    scopus 로고
    • Binding of ferric heme by the recombinant globin from the cyanobacterium Synechocystis sp. PCC 6803
    • Lecomte J.T.J., Scott N.L., Vu B.C., Falzone C.J. Binding of ferric heme by the recombinant globin from the cyanobacterium Synechocystis sp. PCC 6803. Biochemistry 2001, 40:6541-6552.
    • (2001) Biochemistry , vol.40 , pp. 6541-6552
    • Lecomte, J.T.J.1    Scott, N.L.2    Vu, B.C.3    Falzone, C.J.4
  • 87
    • 22844442344 scopus 로고    scopus 로고
    • Structural and dynamic properties of Synechocystis sp. PCC 6803 Hb revealed by reconstitution with Zn-protoporphyrin IX
    • Lecomte J.T.J., Vu B.C., Falzone C.J. Structural and dynamic properties of Synechocystis sp. PCC 6803 Hb revealed by reconstitution with Zn-protoporphyrin IX. Journal of Inorganic Biochemistry 2005, 99:1585-1592.
    • (2005) Journal of Inorganic Biochemistry , vol.99 , pp. 1585-1592
    • Lecomte, J.T.J.1    Vu, B.C.2    Falzone, C.J.3
  • 88
    • 20444476656 scopus 로고    scopus 로고
    • Structural divergence and distant relationships in proteins: Evolution of the globins
    • Lecomte J.T.J., Vuletich D.A., Lesk A.M. Structural divergence and distant relationships in proteins: Evolution of the globins. Current Opinion in Structural Biology 2005, 15:290-301.
    • (2005) Current Opinion in Structural Biology , vol.15 , pp. 290-301
    • Lecomte, J.T.J.1    Vuletich, D.A.2    Lesk, A.M.3
  • 89
    • 84867795031 scopus 로고    scopus 로고
    • Characterization of the mechanism and magnitude of cytoglobin-mediated nitrite reduction and nitric oxide generation under anaerobic conditions
    • Li H., Hemann C., Abdelghany T.M., El-Mahdy M.A., Zweier J.L. Characterization of the mechanism and magnitude of cytoglobin-mediated nitrite reduction and nitric oxide generation under anaerobic conditions. The Journal of Biological Chemistry 2012, 287:36623-36633.
    • (2012) The Journal of Biological Chemistry , vol.287 , pp. 36623-36633
    • Li, H.1    Hemann, C.2    Abdelghany, T.M.3    El-Mahdy, M.A.4    Zweier, J.L.5
  • 90
    • 0033214084 scopus 로고    scopus 로고
    • Studies on nitric oxide (NO) formation by the green alga Scenedesmus obliquus and the diazotrophic cyanobacterium Anabaena doliolum
    • Mallick N., Rai L.C., Mohn F.H., Soeder C.J. Studies on nitric oxide (NO) formation by the green alga Scenedesmus obliquus and the diazotrophic cyanobacterium Anabaena doliolum. Chemosphere 1999, 39:1601-1610.
    • (1999) Chemosphere , vol.39 , pp. 1601-1610
    • Mallick, N.1    Rai, L.C.2    Mohn, F.H.3    Soeder, C.J.4
  • 91
    • 34447281313 scopus 로고    scopus 로고
    • Myoglobin with chlorophyllous chromophores: Influence on protein stability
    • Markovic D., Proll S., Bubenzer C., Scheer H. Myoglobin with chlorophyllous chromophores: Influence on protein stability. Biochimica et Biophysica Acta 2007, 1767:897-904.
    • (2007) Biochimica et Biophysica Acta , vol.1767 , pp. 897-904
    • Markovic, D.1    Proll, S.2    Bubenzer, C.3    Scheer, H.4
  • 92
    • 0035707917 scopus 로고    scopus 로고
    • An overview of the genome of Nostoc punctiforme, a multicellular, symbiotic cyanobacterium
    • Meeks J.C., Elhai J., Thiel T., Potts M., Larimer F., Lamerdin J., et al. An overview of the genome of Nostoc punctiforme, a multicellular, symbiotic cyanobacterium. Photosynthesis Research 2001, 70:85-106.
    • (2001) Photosynthesis Research , vol.70 , pp. 85-106
    • Meeks, J.C.1    Elhai, J.2    Thiel, T.3    Potts, M.4    Larimer, F.5    Lamerdin, J.6
  • 94
    • 2442538228 scopus 로고    scopus 로고
    • Cyanide binding to truncated hemoglobins: A crystallographic and kinetic study
    • Milani M., Ouellet Y., Ouellet H., Guertin M., Boffi A., Antonini G., et al. Cyanide binding to truncated hemoglobins: A crystallographic and kinetic study. Biochemistry 2004, 43:5213-5221.
    • (2004) Biochemistry , vol.43 , pp. 5213-5221
    • Milani, M.1    Ouellet, Y.2    Ouellet, H.3    Guertin, M.4    Boffi, A.5    Antonini, G.6
  • 102
    • 41149121750 scopus 로고    scopus 로고
    • Exploring the molecular basis of heme coordination in human neuroglobin
    • Nadra A.D., Marti M.A., Pesce A., Bolognesi M., Estrin D.A. Exploring the molecular basis of heme coordination in human neuroglobin. Proteins 2008, 71:695-705.
    • (2008) Proteins , vol.71 , pp. 695-705
    • Nadra, A.D.1    Marti, M.A.2    Pesce, A.3    Bolognesi, M.4    Estrin, D.A.5
  • 103
    • 34447530237 scopus 로고    scopus 로고
    • Protein fold and structure in the truncated (2/2) globin family
    • Nardini M., Pesce A., Milani M., Bolognesi M. Protein fold and structure in the truncated (2/2) globin family. Gene 2007, 398:2-11.
    • (2007) Gene , vol.398 , pp. 2-11
    • Nardini, M.1    Pesce, A.2    Milani, M.3    Bolognesi, M.4
  • 104
    • 78650169950 scopus 로고    scopus 로고
    • Structural and functional diversification of the light-harvesting complexes in photosynthetic eukaryotes
    • Neilson J.A.D., Durnford D.G. Structural and functional diversification of the light-harvesting complexes in photosynthetic eukaryotes. Photosynthesis Research 2010, 106:57-71.
    • (2010) Photosynthesis Research , vol.106 , pp. 57-71
    • Neilson, J.A.D.1    Durnford, D.G.2
  • 105
    • 79955762558 scopus 로고    scopus 로고
    • Chemical reactivity of Synechococcus sp. PCC 7002 and Synechocystis sp. PCC 6803 hemoglobins: Covalent heme attachment and bishistidine coordination
    • Nothnagel H.J., Preimesberger M.R., Pond M.P., Winer B.Y., Adney E.M., Lecomte J.T.J. Chemical reactivity of Synechococcus sp. PCC 7002 and Synechocystis sp. PCC 6803 hemoglobins: Covalent heme attachment and bishistidine coordination. Journal of Biological Inorganic Chemistry 2011, 16:539-552.
    • (2011) Journal of Biological Inorganic Chemistry , vol.16 , pp. 539-552
    • Nothnagel, H.J.1    Preimesberger, M.R.2    Pond, M.P.3    Winer, B.Y.4    Adney, E.M.5    Lecomte, J.T.J.6
  • 106
    • 0019765115 scopus 로고
    • Stopped-flow, rapid mixing measurements of ligand binding to hemoglobin and red cells
    • Academic Press, New York
    • Olson J.S. Stopped-flow, rapid mixing measurements of ligand binding to hemoglobin and red cells. Methods in Enzymology 1981, Vol. 76:631-651. Academic Press, New York.
    • (1981) Methods in Enzymology , vol.76 , pp. 631-651
    • Olson, J.S.1
  • 107
    • 0029894282 scopus 로고    scopus 로고
    • Kinetic pathways and barriers for ligand binding to myoglobin
    • Olson J.S., Phillips G.N. Kinetic pathways and barriers for ligand binding to myoglobin. The Journal of Biological Chemistry 1996, 271:17593-17596.
    • (1996) The Journal of Biological Chemistry , vol.271 , pp. 17593-17596
    • Olson, J.S.1    Phillips, G.N.2
  • 109
    • 34547953953 scopus 로고    scopus 로고
    • Ligand pathways in myoglobin: A review of Trp cavity mutations
    • Olson J.S., Soman J., Phillips G.N. Ligand pathways in myoglobin: A review of Trp cavity mutations. IUBMB Life 2007, 59:552-562.
    • (2007) IUBMB Life , vol.59 , pp. 552-562
    • Olson, J.S.1    Soman, J.2    Phillips, G.N.3
  • 110
    • 0025026058 scopus 로고
    • Comparison of the structures of globins and phycocyanins: Evidence for evolutionary relationship
    • Pastore A., Lesk A.M. Comparison of the structures of globins and phycocyanins: Evidence for evolutionary relationship. Proteins 1990, 8:133-155.
    • (1990) Proteins , vol.8 , pp. 133-155
    • Pastore, A.1    Lesk, A.M.2
  • 111
    • 0034213366 scopus 로고    scopus 로고
    • A novel two-over-two α-helical sandwich fold is characteristic of the truncated hemoglobin family
    • Pesce A., Couture M., Dewilde S., Guertin M., Yamauchi K., Ascenzi P., et al. A novel two-over-two α-helical sandwich fold is characteristic of the truncated hemoglobin family. The EMBO Journal 2000, 19:2424-2434.
    • (2000) The EMBO Journal , vol.19 , pp. 2424-2434
    • Pesce, A.1    Couture, M.2    Dewilde, S.3    Guertin, M.4    Yamauchi, K.5    Ascenzi, P.6
  • 112
    • 48849090525 scopus 로고    scopus 로고
    • Reactions of ferrous neuroglobin and cytoglobin with nitrite under anaerobic conditions
    • Petersen M.G., Dewilde S., Fago A. Reactions of ferrous neuroglobin and cytoglobin with nitrite under anaerobic conditions. Journal of Inorganic Biochemistry 2008, 102:1777-1782.
    • (2008) Journal of Inorganic Biochemistry , vol.102 , pp. 1777-1782
    • Petersen, M.G.1    Dewilde, S.2    Fago, A.3
  • 114
    • 0019209443 scopus 로고
    • Structure and refinement of oxymyoglobin at 1.6Å resolution
    • Phillips S.E. Structure and refinement of oxymyoglobin at 1.6Å resolution. Journal of Molecular Biology 1980, 142:531-554.
    • (1980) Journal of Molecular Biology , vol.142 , pp. 531-554
    • Phillips, S.E.1
  • 115
    • 77956271750 scopus 로고    scopus 로고
    • Light-dependent electrogenic activity of cyanobacteria
    • Pisciotta J.M., Zou Y., Baskakov I.V. Light-dependent electrogenic activity of cyanobacteria. PLoS One 2010, 5:e10821.
    • (2010) PLoS One , vol.5
    • Pisciotta, J.M.1    Zou, Y.2    Baskakov, I.V.3
  • 116
    • 84864274190 scopus 로고    scopus 로고
    • Influence of heme post-translational modification and distal ligation on the backbone dynamics of a monomeric hemoglobin
    • Pond M.P., Majumdar A., Lecomte J.T.J. Influence of heme post-translational modification and distal ligation on the backbone dynamics of a monomeric hemoglobin. Biochemistry 2012, 51:5733-5747.
    • (2012) Biochemistry , vol.51 , pp. 5733-5747
    • Pond, M.P.1    Majumdar, A.2    Lecomte, J.T.J.3
  • 118
    • 84862541571 scopus 로고    scopus 로고
    • Electron self-exchange and self-amplified posttranslational modification in the hemoglobins from Synechocystis sp. PCC 6803 and Synechococcus sp. PCC 7002
    • Preimesberger M.R., Pond M.P., Majumdar A., Lecomte J.T.J. Electron self-exchange and self-amplified posttranslational modification in the hemoglobins from Synechocystis sp. PCC 6803 and Synechococcus sp. PCC 7002. Journal of Biological Inorganic Chemistry 2012, 17:599-609.
    • (2012) Journal of Biological Inorganic Chemistry , vol.17 , pp. 599-609
    • Preimesberger, M.R.1    Pond, M.P.2    Majumdar, A.3    Lecomte, J.T.J.4
  • 120
    • 33746697712 scopus 로고    scopus 로고
    • Myoglobin with modified tetrapyrrole chromophores: Binding specificity and photochemistry
    • Pröll S., Wilhelm B., Robert B., Scheer H. Myoglobin with modified tetrapyrrole chromophores: Binding specificity and photochemistry. Biochimica et Biophysica Acta 2006, 1757:750-763.
    • (2006) Biochimica et Biophysica Acta , vol.1757 , pp. 750-763
    • Pröll, S.1    Wilhelm, B.2    Robert, B.3    Scheer, H.4
  • 121
    • 0015477354 scopus 로고
    • Intermediate hemichrome formation after oxidation of three unstable hemoglobins (Freiburg, Riverdale-Bronx and Koln)
    • Rachmilewitz E.A., Harari E. Intermediate hemichrome formation after oxidation of three unstable hemoglobins (Freiburg, Riverdale-Bronx and Koln). Hämatologie und Bluttransfusion 1972, 10:241-250.
    • (1972) Hämatologie und Bluttransfusion , vol.10 , pp. 241-250
    • Rachmilewitz, E.A.1    Harari, E.2
  • 122
    • 0015807484 scopus 로고
    • Hemichrome formation during in vitro oxidation of Hb Köln
    • Rachmilewitz E.A., White J.M. Hemichrome formation during in vitro oxidation of Hb Köln. Nature: New Biology 1973, 241:115-117.
    • (1973) Nature: New Biology , vol.241 , pp. 115-117
    • Rachmilewitz, E.A.1    White, J.M.2
  • 124
    • 33745618402 scopus 로고    scopus 로고
    • Evolution of the Isd11-IscS complex reveals a single α-proteobacterial endosymbiosis for all eukaryotes
    • Richards T.A., van der Giezen M. Evolution of the Isd11-IscS complex reveals a single α-proteobacterial endosymbiosis for all eukaryotes. Molecular Biology and Evolution 2006, 23:1341-1344.
    • (2006) Molecular Biology and Evolution , vol.23 , pp. 1341-1344
    • Richards, T.A.1    van der Giezen, M.2
  • 127
    • 0036010191 scopus 로고    scopus 로고
    • Nitric oxide production mediated by nitrate reductase in the green alga Chlamydomonas reinhardtii: An alternative NO production pathway in photosynthetic organisms
    • Sakihama Y., Nakamura S., Yamasaki H. Nitric oxide production mediated by nitrate reductase in the green alga Chlamydomonas reinhardtii: An alternative NO production pathway in photosynthetic organisms. Plant & Cell Physiology 2002, 43:290-297.
    • (2002) Plant & Cell Physiology , vol.43 , pp. 290-297
    • Sakihama, Y.1    Nakamura, S.2    Yamasaki, H.3
  • 129
    • 7344236514 scopus 로고
    • Ueber die Atmungsfarbstoffe von Paramecium
    • (Tokyo), Fujii Jubilee Volume
    • Sato, T., & Tamiya, H. (1937). Ueber die Atmungsfarbstoffe von Paramecium. Cytologia (Tokyo), Fujii Jubilee Volume, pp. 1133-1138.
    • (1937) Cytologia , pp. 1133-1138
    • Sato, T.1    Tamiya, H.2
  • 130
    • 84055190273 scopus 로고    scopus 로고
    • Structure and dynamics of Mycobacterium tuberculosis truncated hemoglobin N: Insights from NMR spectroscopy and molecular dynamics simulations
    • Savard P.Y., Daigle R., Morin S., Sebilo A., Meindre F., Lague P., et al. Structure and dynamics of Mycobacterium tuberculosis truncated hemoglobin N: Insights from NMR spectroscopy and molecular dynamics simulations. Biochemistry 2011, 50:11121-11130.
    • (2011) Biochemistry , vol.50 , pp. 11121-11130
    • Savard, P.Y.1    Daigle, R.2    Morin, S.3    Sebilo, A.4    Meindre, F.5    Lague, P.6
  • 131
    • 0037018935 scopus 로고    scopus 로고
    • The hemoglobin of the cyanobacterium Synechococcus sp. PCC 7002: Evidence for hexacoordination and covalent adduct formation in the ferric recombinant protein
    • Scott N.L., Falzone C.J., Vuletich D.A., Zhao J., Bryant D.A., Lecomte J.T.J. The hemoglobin of the cyanobacterium Synechococcus sp. PCC 7002: Evidence for hexacoordination and covalent adduct formation in the ferric recombinant protein. Biochemistry 2002, 41:6902-6910.
    • (2002) Biochemistry , vol.41 , pp. 6902-6910
    • Scott, N.L.1    Falzone, C.J.2    Vuletich, D.A.3    Zhao, J.4    Bryant, D.A.5    Lecomte, J.T.J.6
  • 133
    • 0034022487 scopus 로고    scopus 로고
    • Cloning, expression, purification, and preliminary characterization of a putative hemoglobin from the cyanobacterium Synechocystis sp. PCC 6803
    • Scott N.L., Lecomte J.T.J. Cloning, expression, purification, and preliminary characterization of a putative hemoglobin from the cyanobacterium Synechocystis sp. PCC 6803. Protein Science 2000, 9:587-597.
    • (2000) Protein Science , vol.9 , pp. 587-597
    • Scott, N.L.1    Lecomte, J.T.J.2
  • 134
    • 77955669608 scopus 로고    scopus 로고
    • Functional and structural characterization of the 2/2 hemoglobin from Synechococcus sp. PCC 7002
    • Scott N.L., Xu Y., Shen G., Vuletich D.A., Falzone C.J., Li Z., et al. Functional and structural characterization of the 2/2 hemoglobin from Synechococcus sp. PCC 7002. Biochemistry 2010, 49:7000-7011.
    • (2010) Biochemistry , vol.49 , pp. 7000-7011
    • Scott, N.L.1    Xu, Y.2    Shen, G.3    Vuletich, D.A.4    Falzone, C.J.5    Li, Z.6
  • 137
    • 33344467539 scopus 로고    scopus 로고
    • 2 bonding in myoglobin and hemoglobin: A new molecular paradigm
    • 2 bonding in myoglobin and hemoglobin: A new molecular paradigm. Progress in Biophysics and Molecular Biology 2006, 91:83-162.
    • (2006) Progress in Biophysics and Molecular Biology , vol.91 , pp. 83-162
    • Shikama, K.1
  • 139
    • 30744469606 scopus 로고    scopus 로고
    • Slow ligand binding kinetics dominate ferrous hexacoordinate hemoglobin reactivities and reveal differences between plants and other species
    • Smagghe B.J., Sarath G., Ross E., Hilbert J.L., Hargrove M.S. Slow ligand binding kinetics dominate ferrous hexacoordinate hemoglobin reactivities and reveal differences between plants and other species. Biochemistry 2006, 45:561-570.
    • (2006) Biochemistry , vol.45 , pp. 561-570
    • Smagghe, B.J.1    Sarath, G.2    Ross, E.3    Hilbert, J.L.4    Hargrove, M.S.5
  • 140
    • 44349180793 scopus 로고    scopus 로고
    • NO dioxygenase activity in hemoglobins is ubiquitous in vitro, but limited by reduction in vivo
    • Smagghe B.J., Trent J.T., Hargrove M.S. NO dioxygenase activity in hemoglobins is ubiquitous in vitro, but limited by reduction in vivo. PLoS One 2008, 3:e2039.
    • (2008) PLoS One , vol.3
    • Smagghe, B.J.1    Trent, J.T.2    Hargrove, M.S.3
  • 141
    • 84874674226 scopus 로고    scopus 로고
    • The global response of Nostoc punctiforme ATCC 29133 to UVA stress, assessed in a Temporal DNA microarray study
    • Soule T., Gao Q.J., Stout V., Garcia-Pichel F. The global response of Nostoc punctiforme ATCC 29133 to UVA stress, assessed in a Temporal DNA microarray study. Photochemistry and Photobiology 2013, 89:415-423.
    • (2013) Photochemistry and Photobiology , vol.89 , pp. 415-423
    • Soule, T.1    Gao, Q.J.2    Stout, V.3    Garcia-Pichel, F.4
  • 144
    • 84855960615 scopus 로고    scopus 로고
    • Analysis of raphidophyte assimilatory nitrate reductase reveals unique domain architecture incorporating a 2/2 hemoglobin
    • Stewart J.J., Coyne K.J. Analysis of raphidophyte assimilatory nitrate reductase reveals unique domain architecture incorporating a 2/2 hemoglobin. Plant Molecular Biology 2011, 77:565-575.
    • (2011) Plant Molecular Biology , vol.77 , pp. 565-575
    • Stewart, J.J.1    Coyne, K.J.2
  • 145
    • 83455221752 scopus 로고    scopus 로고
    • Hydroxylamine reduction to ammonium by plant and cyanobacterial hemoglobins
    • Sturms R., Dispirito A.A., Fulton D.B., Hargrove M.S. Hydroxylamine reduction to ammonium by plant and cyanobacterial hemoglobins. Biochemistry 2011, 50:10829-10835.
    • (2011) Biochemistry , vol.50 , pp. 10829-10835
    • Sturms, R.1    Dispirito, A.A.2    Fulton, D.B.3    Hargrove, M.S.4
  • 146
    • 79955859483 scopus 로고    scopus 로고
    • Plant and cyanobacterial hemoglobins reduce nitrite to nitric oxide under anoxic conditions
    • Sturms R., Dispirito A.A., Hargrove M.S. Plant and cyanobacterial hemoglobins reduce nitrite to nitric oxide under anoxic conditions. Biochemistry 2011, 50:3873-3878.
    • (2011) Biochemistry , vol.50 , pp. 3873-3878
    • Sturms, R.1    Dispirito, A.A.2    Hargrove, M.S.3
  • 149
    • 80054076084 scopus 로고    scopus 로고
    • Hell's Gate globin I: An acid and thermostable bacterial hemoglobin resembling mammalian neuroglobin
    • Teh A.-H., Saito J.A., Baharuddin A., Tuckerman J.R., Newhouse J.S., Kanbe M., et al. Hell's Gate globin I: An acid and thermostable bacterial hemoglobin resembling mammalian neuroglobin. FEBS Letters 2011, 585:3250-3258.
    • (2011) FEBS Letters , vol.585 , pp. 3250-3258
    • Teh, A.-H.1    Saito, J.A.2    Baharuddin, A.3    Tuckerman, J.R.4    Newhouse, J.S.5    Kanbe, M.6
  • 150
    • 0030067617 scopus 로고    scopus 로고
    • Spectroscopical and functional characterization of the hemoglobin of Nostoc commune UTEX 584 (Cyanobacteria)
    • Thorsteinsson M.V., Bevan D.R., Ebel R.E., Weber R.E., Potts M. Spectroscopical and functional characterization of the hemoglobin of Nostoc commune UTEX 584 (Cyanobacteria). Biochimica et Biophysica Acta 1996, 1292:133-139.
    • (1996) Biochimica et Biophysica Acta , vol.1292 , pp. 133-139
    • Thorsteinsson, M.V.1    Bevan, D.R.2    Ebel, R.E.3    Weber, R.E.4    Potts, M.5
  • 151
    • 0033573859 scopus 로고    scopus 로고
    • A cyanobacterial hemoglobin with unusual ligand binding kinetics and stability properties
    • Thorsteinsson M.V., Bevan D.R., Potts M., Dou Y., Eich R.F., Hargrove M.S., et al. A cyanobacterial hemoglobin with unusual ligand binding kinetics and stability properties. Biochemistry 1999, 38:2117-2126.
    • (1999) Biochemistry , vol.38 , pp. 2117-2126
    • Thorsteinsson, M.V.1    Bevan, D.R.2    Potts, M.3    Dou, Y.4    Eich, R.F.5    Hargrove, M.S.6
  • 152
    • 84863513471 scopus 로고    scopus 로고
    • Nitrite reductase activity of nonsymbiotic hemoglobins from Arabidopsis thaliana
    • Tiso M., Tejero J., Kenney C., Frizzell S., Gladwin M.T. Nitrite reductase activity of nonsymbiotic hemoglobins from Arabidopsis thaliana. Biochemistry 2012, 51:5285-5292.
    • (2012) Biochemistry , vol.51 , pp. 5285-5292
    • Tiso, M.1    Tejero, J.2    Kenney, C.3    Frizzell, S.4    Gladwin, M.T.5
  • 153
    • 34249978500 scopus 로고    scopus 로고
    • Bardet-Biedl syndrome: Beyond the cilium
    • Tobin J.L., Beales P.L. Bardet-Biedl syndrome: Beyond the cilium. Pediatric Nephrology 2007, 22:926-936.
    • (2007) Pediatric Nephrology , vol.22 , pp. 926-936
    • Tobin, J.L.1    Beales, P.L.2
  • 154
    • 0037117726 scopus 로고    scopus 로고
    • A comparative resonance Raman analysis of heme-binding PAS domains: Heme iron coordination structures of the BjFixL, AxPDEA1, EcDos, and MtDos proteins
    • Tomita T., Gonzalez G., Chang A.L., Ikeda-Saito M., Gilles-Gonzalez M.A. A comparative resonance Raman analysis of heme-binding PAS domains: Heme iron coordination structures of the BjFixL, AxPDEA1, EcDos, and MtDos proteins. Biochemistry 2002, 41:4819-4826.
    • (2002) Biochemistry , vol.41 , pp. 4819-4826
    • Tomita, T.1    Gonzalez, G.2    Chang, A.L.3    Ikeda-Saito, M.4    Gilles-Gonzalez, M.A.5
  • 156
    • 0037205447 scopus 로고    scopus 로고
    • A ubiquitously expressed human hexacoordinate hemoglobin
    • Trent J.T., Hargrove M.S. A ubiquitously expressed human hexacoordinate hemoglobin. The Journal of Biological Chemistry 2002, 277:19538-19545.
    • (2002) The Journal of Biological Chemistry , vol.277 , pp. 19538-19545
    • Trent, J.T.1    Hargrove, M.S.2
  • 157
    • 3843100441 scopus 로고    scopus 로고
    • Crystallographic analysis of Synechocystis cyanoglobin reveals the structural changes accompanying ligand binding in a hexacoordinate hemoglobin
    • Trent J.T., Kundu S., Hoy J.A., Hargrove M.S. Crystallographic analysis of Synechocystis cyanoglobin reveals the structural changes accompanying ligand binding in a hexacoordinate hemoglobin. Journal of Molecular Biology 2004, 341:1097-1108.
    • (2004) Journal of Molecular Biology , vol.341 , pp. 1097-1108
    • Trent, J.T.1    Kundu, S.2    Hoy, J.A.3    Hargrove, M.S.4
  • 159
    • 84865620451 scopus 로고    scopus 로고
    • How do heme-protein sensors exclude oxygen? Lessons learned from cytochrome c', Nostoc puntiforme heme nitric oxide/oxygen-binding domain, and soluble guanylyl cyclase
    • Tsai A.L., Martin E., Berka V., Olson J.S. How do heme-protein sensors exclude oxygen? Lessons learned from cytochrome c', Nostoc puntiforme heme nitric oxide/oxygen-binding domain, and soluble guanylyl cyclase. Antioxidants & Redox Signaling 2012, 17:1246-1263.
    • (2012) Antioxidants & Redox Signaling , vol.17 , pp. 1246-1263
    • Tsai, A.L.1    Martin, E.2    Berka, V.3    Olson, J.S.4
  • 160
    • 80052419041 scopus 로고    scopus 로고
    • Peroxynitrite formation and function in plants
    • Vandelle E., Delledonne M. Peroxynitrite formation and function in plants. Plant Science 2011, 181:534-539.
    • (2011) Plant Science , vol.181 , pp. 534-539
    • Vandelle, E.1    Delledonne, M.2
  • 162
    • 79551530357 scopus 로고    scopus 로고
    • Phylogenetic relationships of 3/3 and 2/2 hemoglobins in Archaeplastida genomes to bacterial and other eukaryote hemoglobins
    • Vinogradov S.N., Fernandez I., Hoogewijs D., Arredondo-Peter R. Phylogenetic relationships of 3/3 and 2/2 hemoglobins in Archaeplastida genomes to bacterial and other eukaryote hemoglobins. Molecular Plant 2011, 4:42-58.
    • (2011) Molecular Plant , vol.4 , pp. 42-58
    • Vinogradov, S.N.1    Fernandez, I.2    Hoogewijs, D.3    Arredondo-Peter, R.4
  • 166
    • 44049108195 scopus 로고    scopus 로고
    • Diversity of globin function: Enzymatic, transport, storage, and sensing
    • Vinogradov S.N., Moens L. Diversity of globin function: Enzymatic, transport, storage, and sensing. The Journal of Biological Chemistry 2008, 283:8773-8777.
    • (2008) The Journal of Biological Chemistry , vol.283 , pp. 8773-8777
    • Vinogradov, S.N.1    Moens, L.2
  • 168
    • 34447575504 scopus 로고
    • Red, brown and green pigments in leguminous root nodules
    • Virtanen A.I., Laine T. Red, brown and green pigments in leguminous root nodules. Nature 1946, 1157:25-26.
    • (1946) Nature , vol.1157 , pp. 25-26
    • Virtanen, A.I.1    Laine, T.2
  • 169
    • 44349088799 scopus 로고    scopus 로고
    • Ultrafast heme-residue bond formation in six-coordinate heme proteins: Implications for functional ligand exchange
    • Vos M.H., Battistoni A., Lechauve C., Marden M.C., Kiger L., Desbois A., et al. Ultrafast heme-residue bond formation in six-coordinate heme proteins: Implications for functional ligand exchange. Biochemistry 2008, 47:5718-5723.
    • (2008) Biochemistry , vol.47 , pp. 5718-5723
    • Vos, M.H.1    Battistoni, A.2    Lechauve, C.3    Marden, M.C.4    Kiger, L.5    Desbois, A.6
  • 172
    • 1542298190 scopus 로고    scopus 로고
    • Characterization of the heme-histidine cross-link in cyanobacterial hemoglobins from Synechocystis sp. PCC 6803 and Synechococcus sp. PCC 7002
    • Vu B.C., Vuletich D.A., Kuriakose S.A., Falzone C.J., Lecomte J.T.J. Characterization of the heme-histidine cross-link in cyanobacterial hemoglobins from Synechocystis sp. PCC 6803 and Synechococcus sp. PCC 7002. Journal of Biological Inorganic Chemistry 2004, 9:183-194.
    • (2004) Journal of Biological Inorganic Chemistry , vol.9 , pp. 183-194
    • Vu, B.C.1    Vuletich, D.A.2    Kuriakose, S.A.3    Falzone, C.J.4    Lecomte, J.T.J.5
  • 173
    • 33646341657 scopus 로고    scopus 로고
    • A phylogenetic and structural analysis of truncated hemoglobins
    • Vuletich D.A., Lecomte J.T.J. A phylogenetic and structural analysis of truncated hemoglobins. Journal of Molecular Evolution 2006, 62:196-210.
    • (2006) Journal of Molecular Evolution , vol.62 , pp. 196-210
    • Vuletich, D.A.1    Lecomte, J.T.J.2
  • 174
    • 33747403852 scopus 로고    scopus 로고
    • Modulation of Chlamydomonas reinhardtii flagellar motility by redox poise
    • Wakabayashi K., King S.M. Modulation of Chlamydomonas reinhardtii flagellar motility by redox poise. The Journal of Cell Biology 2006, 173:743-754.
    • (2006) The Journal of Cell Biology , vol.173 , pp. 743-754
    • Wakabayashi, K.1    King, S.M.2
  • 175
    • 0022486777 scopus 로고
    • Primary sequence of a dimeric bacterial haemoglobin from Vitreoscilla
    • Wakabayashi S., Matsubara H., Webster D.A. Primary sequence of a dimeric bacterial haemoglobin from Vitreoscilla. Nature 1986, 322:481-483.
    • (1986) Nature , vol.322 , pp. 481-483
    • Wakabayashi, S.1    Matsubara, H.2    Webster, D.A.3
  • 176
    • 34548126843 scopus 로고    scopus 로고
    • Fluorescent and luminescent probes for measurement of oxidative and nitrosative species in cells and tissues: progress, pitfalls, and prospects
    • Wardman P. Fluorescent and luminescent probes for measurement of oxidative and nitrosative species in cells and tissues: progress, pitfalls, and prospects. Free Radical Biology & Medicine 2007, 43:995-1022.
    • (2007) Free Radical Biology & Medicine , vol.43 , pp. 995-1022
    • Wardman, P.1
  • 178
    • 0001540685 scopus 로고
    • Generation of superoxide radicals during the autoxidation of mammalian oxyhemoglobin
    • Wever R., Oudega B., Van Gelder B.F. Generation of superoxide radicals during the autoxidation of mammalian oxyhemoglobin. Biochimica et Biophysica Acta-Enzymology 1973, 302:475-478.
    • (1973) Biochimica et Biophysica Acta-Enzymology , vol.302 , pp. 475-478
    • Wever, R.1    Oudega, B.2    Van Gelder, B.F.3
  • 179
    • 0037059826 scopus 로고    scopus 로고
    • Truncated hemoglobins: A new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes and plants
    • Wittenberg J.B., Bolognesi M., Wittenberg B.A., Guertin M. Truncated hemoglobins: A new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes and plants. The Journal of Biological Chemistry 2002, 277:871-874.
    • (2002) The Journal of Biological Chemistry , vol.277 , pp. 871-874
    • Wittenberg, J.B.1    Bolognesi, M.2    Wittenberg, B.A.3    Guertin, M.4
  • 180
    • 0019886577 scopus 로고
    • Solution properties of synthetic chlorophyllide- and bacteriochlorophyllide-apomyoglobin complexes
    • Wright K.A., Boxer S.G. Solution properties of synthetic chlorophyllide- and bacteriochlorophyllide-apomyoglobin complexes. Biochemistry 1981, 20:7546-7556.
    • (1981) Biochemistry , vol.20 , pp. 7546-7556
    • Wright, K.A.1    Boxer, S.G.2
  • 182
    • 0034673016 scopus 로고    scopus 로고
    • 1H NMR study of the heme cavity and folding topology of the abbreviated chain 118-residue globin from the cyanobacterium Nostoc commune
    • 1H NMR study of the heme cavity and folding topology of the abbreviated chain 118-residue globin from the cyanobacterium Nostoc commune. Biochemistry 2000, 39:1389-1399.
    • (2000) Biochemistry , vol.39 , pp. 1389-1399
    • Yeh, D.C.1    Thorsteinsson, M.V.2    Bevan, D.R.3    Potts, M.4    La Mar, G.N.5
  • 184
    • 77954746068 scopus 로고    scopus 로고
    • Structure and properties of a bis-histidyl ligated globin from Caenorhabditis elegans
    • Yoon J., Herzik M.A., Winter M.B., Tran R., Olea C., Marletta M.A. Structure and properties of a bis-histidyl ligated globin from Caenorhabditis elegans. Biochemistry 2010, 13:5662-5670.
    • (2010) Biochemistry , vol.13 , pp. 5662-5670
    • Yoon, J.1    Herzik, M.A.2    Winter, M.B.3    Tran, R.4    Olea, C.5    Marletta, M.A.6
  • 185
    • 65649147891 scopus 로고    scopus 로고
    • Mechanistic insights into Bardet-Biedl syndrome, a model ciliopathy
    • Zaghloul N.A., Katsanis N. Mechanistic insights into Bardet-Biedl syndrome, a model ciliopathy. The Journal of Clinical Investigation 2009, 119:428-437.
    • (2009) The Journal of Clinical Investigation , vol.119 , pp. 428-437
    • Zaghloul, N.A.1    Katsanis, N.2


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