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Volumn 2014, Issue , 2014, Pages

The alternative route to heme in the methanogenic archaeon methanosarcina barkeri

Author keywords

[No Author keywords available]

Indexed keywords

ARCHAEAL PROTEIN; HEME; UROPORPHYRINOGEN;

EID: 84893707267     PISSN: 14723646     EISSN: None     Source Type: Journal    
DOI: 10.1155/2014/327637     Document Type: Article
Times cited : (48)

References (28)
  • 1
    • 0034529596 scopus 로고    scopus 로고
    • Tetrapyrroles: The pigments of life
    • DOI 10.1039/b002635m
    • Battersby A. R., Tetrapyrroles: the pigments of life. Natural Product Reports 2000 17 6 507 526 2-s2.0-0034529596 10.1039/b002635m (Pubitemid 32013254)
    • (2000) Natural Product Reports , vol.17 , Issue.6 , pp. 507-526
    • Battersby, A.R.1
  • 2
    • 77952721977 scopus 로고    scopus 로고
    • Structure and function of enzymes in heme biosynthesis
    • 2-s2.0-77952721977 10.1002/pro.405
    • Layer G., Reichelt J., Jahn D., Heinz D. W., Structure and function of enzymes in heme biosynthesis. Protein Science 2010 19 6 1137 1161 2-s2.0-77952721977 10.1002/pro.405
    • (2010) Protein Science , vol.19 , Issue.6 , pp. 1137-1161
    • Layer, G.1    Reichelt, J.2    Jahn, D.3    Heinz, D.W.4
  • 3
    • 79251541167 scopus 로고    scopus 로고
    • A novel pathway for the biosynthesis of heme in Archaea: Genome-based bioinformatic predictions and experimental evidence
    • 175050 10.1155/2010/175050 2-s2.0-79953660218
    • Storbeck S., Rolfes S., Raux-Deery E., Warren M. J., Jahn D., Layer G., A novel pathway for the biosynthesis of heme in Archaea: genome-based bioinformatic predictions and experimental evidence. Archaea 2010 2010 15 175050 10.1155/2010/175050 2-s2.0-79953660218
    • (2010) Archaea , vol.2010 , pp. 15
    • Storbeck, S.1    Rolfes, S.2    Raux-Deery, E.3    Warren, M.J.4    Jahn, D.5    Layer, G.6
  • 4
    • 58149382075 scopus 로고    scopus 로고
    • Genome-based analysis of heme biosynthesis and uptake in prokaryotic systems
    • 2-s2.0-58149382075 10.1021/pr8004309
    • Cavallaro G., Decaria L., Rosato A., Genome-based analysis of heme biosynthesis and uptake in prokaryotic systems. Journal of Proteome Research 2008 7 11 4946 4954 2-s2.0-58149382075 10.1021/pr8004309
    • (2008) Journal of Proteome Research , vol.7 , Issue.11 , pp. 4946-4954
    • Cavallaro, G.1    Decaria, L.2    Rosato, A.3
  • 5
    • 0036667415 scopus 로고    scopus 로고
    • A whole genome view of prokaryotic haem biosynthesis
    • 2-s2.0-0036667415
    • Panek H., O'Brian M. R., A whole genome view of prokaryotic haem biosynthesis. Microbiology 2002 148 8 2273 2282 2-s2.0-0036667415
    • (2002) Microbiology , vol.148 , Issue.8 , pp. 2273-2282
    • Panek, H.1    O'Brian, M.R.2
  • 7
    • 0027145689 scopus 로고
    • L-Methionine methyl is specificially incorporated into the C-2 and C-7 positions of the porphyrin of cytochrome c3 in a strictly anaerobic bacterium, Desulfovibrio vulgaris
    • 3 in a strictly anaerobic bacterium, Desulfovibrio vulgaris. Journal of the American Chemical Society 1993 115 25 12185 12186 2-s2.0-0027145689 (Pubitemid 2004463)
    • (1993) Journal of the American Chemical Society , vol.115 , Issue.25 , pp. 12185-12186
    • Akutsu, H.1    Park, J.-S.2    Sano, S.3
  • 8
    • 33845456591 scopus 로고    scopus 로고
    • Heme biosynthesis in Methanosarcina barkeri via a pathway involving two methylation reactions
    • DOI 10.1128/JB.01349-06
    • Buchenau B., Kahnt J., Heinemann I. U., Jahn D., Thauer R. K., Heme biosynthesis in Methanosarcina barkeri via a pathway involving two methylation reactions. Journal of Bacteriology 2006 188 24 8666 8668 2-s2.0-33845456591 10.1128/JB.01349-06 (Pubitemid 44894068)
    • (2006) Journal of Bacteriology , vol.188 , Issue.24 , pp. 8666-8668
    • Buchenau, B.1    Kahnt, J.2    Heinemann, I.U.3    Jahn, D.4    Thauer, R.K.5
  • 10
    • 66549088091 scopus 로고    scopus 로고
    • Functional characterization of the early steps of tetrapyrrole biosynthesis and modification in Desulfovibrio vulgaris Hildenborough
    • 2-s2.0-66549088091 10.1042/BJ20090151
    • Lobo S. A. L., Brindley A., Warren M. J., Saraiva L. M., Functional characterization of the early steps of tetrapyrrole biosynthesis and modification in Desulfovibrio vulgaris Hildenborough. Biochemical Journal 2009 420 2 317 325 2-s2.0-66549088091 10.1042/BJ20090151
    • (2009) Biochemical Journal , vol.420 , Issue.2 , pp. 317-325
    • Lobo, S.A.L.1    Brindley, A.2    Warren, M.J.3    Saraiva, L.M.4
  • 13
    • 22844435319 scopus 로고    scopus 로고
    • 4]-dependent NirA from Mycobacterium tuberculosis is a sulfite reductase with a covalent Cys-Tyr bond in the active site
    • DOI 10.1074/jbc.M502560200
    • Schnell R., Sandalova T., Hellman U., Lindqvist Y., Schneider G., Siroheme- and [Fe4-S4]-dependent NirA from Mycobacterium tuberculosis is a sulfite reductase with a covalent Cys-Tyr bond in the active site. Journal of Biological Chemistry 2005 280 29 27319 27328 2-s2.0-22844435319 10.1074/jbc.M502560200 (Pubitemid 41040773)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.29 , pp. 27319-27328
    • Schnell, R.1    Sandalova, T.2    Hellman, U.3    Lindqvist, Y.4    Schneider, G.5
  • 14
    • 84858701614 scopus 로고    scopus 로고
    • The radical SAM enzyme AlbA catalyzes thioether bond formation in subtilosin A
    • 2-s2.0-84858701614 10.1038/nchembio.798
    • Flühe L., Knappe T. A., Gattner M. J., Schäfer A., Burghaus O., Linne U., Marahiel M. A., The radical SAM enzyme AlbA catalyzes thioether bond formation in subtilosin A. Nature Chemical Biology 2012 8 4 350 357 2-s2.0-84858701614 10.1038/nchembio.798
    • (2012) Nature Chemical Biology , vol.8 , Issue.4 , pp. 350-357
    • Flühe, L.1    Knappe, T.A.2    Gattner, M.J.3    Schäfer, A.4    Burghaus, O.5    Linne, U.6    Marahiel, M.A.7
  • 15
    • 0023899855 scopus 로고
    • Rapid colorimetric micromethod for the quantitation of complexed iron in biological samples
    • 2-s2.0-0023899855
    • Fish W. W., Rapid colorimetric micromethod for the quantitation of complexed iron in biological samples. Methods in Enzymology 1988 158 357 364 2-s2.0-0023899855
    • (1988) Methods in Enzymology , vol.158 , pp. 357-364
    • Fish, W.W.1
  • 16
    • 0020776388 scopus 로고
    • Semi-micro methods for analysis of labile sulfide and of labile sulfide plus sulfane sulfur in unusually stable iron-sulfur proteins
    • 2-s2.0-0020776388
    • Beinert H., Semi-micro methods for analysis of labile sulfide and of labile sulfide plus sulfane sulfur in unusually stable iron-sulfur proteins. Analytical Biochemistry 1983 131 2 373 378 2-s2.0-0020776388
    • (1983) Analytical Biochemistry , vol.131 , Issue.2 , pp. 373-378
    • Beinert, H.1
  • 17
    • 73249146193 scopus 로고    scopus 로고
    • Unusual diheme conformation of the heme-degrading protein from Mycobacterium tuberculosis
    • 2-s2.0-73249146193 10.1016/j.jmb.2009.11.025
    • Chim N., Iniguez A., Nguyen T. Q., Goulding C. W., Unusual diheme conformation of the heme-degrading protein from Mycobacterium tuberculosis. Journal of Molecular Biology 2010 395 3 595 608 2-s2.0-73249146193 10.1016/j.jmb.2009.11.025
    • (2010) Journal of Molecular Biology , vol.395 , Issue.3 , pp. 595-608
    • Chim, N.1    Iniguez, A.2    Nguyen, T.Q.3    Goulding, C.W.4
  • 18
    • 33745905288 scopus 로고    scopus 로고
    • Porphyrin profiles in blood, urine and faeces by HPLC/electrospray ionization tandem mass spectrometry
    • DOI 10.1002/bmc.656
    • Danton M., Lim C. K., Porphyrin profiles in blood, urine and faeces by HPLC/electrospray ionization tandem mass spectrometry. Biomedical Chromatography 2006 20 6-7 612 621 2-s2.0-33745905288 10.1002/bmc.656 (Pubitemid 44043406)
    • (2006) Biomedical Chromatography , vol.20 , Issue.6-7 , pp. 612-621
    • Danton, M.1    Lim, C.K.2
  • 20
    • 1542717685 scopus 로고
    • The structures and chemistrty of isobacteriochlorins from Desulphovibrio gigas
    • 2-s2.0-1542717685
    • Battersby A. R., Jones K., McDonald E., Robinson J. A., Morris H. R., The structures and chemistrty of isobacteriochlorins from Desulphovibrio gigas. Tetrahedron Letters 1977 18 25 2213 2216 2-s2.0-1542717685
    • (1977) Tetrahedron Letters , vol.18 , Issue.25 , pp. 2213-2216
    • Battersby, A.R.1    Jones, K.2    McDonald, E.3    Robinson, J.A.4    Morris, H.R.5
  • 23
    • 77951953046 scopus 로고    scopus 로고
    • A purified mutant HemA protein from Salmonella enterica serovar Typhimurium lacks bound heme and is defective for heme-mediated regulation in vivo
    • 2-s2.0-77951953046 10.1111/j.1574-6968.2010.01967.x
    • Jones A. M., Elliott T., A purified mutant HemA protein from Salmonella enterica serovar Typhimurium lacks bound heme and is defective for heme-mediated regulation in vivo. FEMS Microbiology Letters 2010 307 1 41 47 2-s2.0-77951953046 10.1111/j.1574-6968.2010.01967.x
    • (2010) FEMS Microbiology Letters , vol.307 , Issue.1 , pp. 41-47
    • Jones, A.M.1    Elliott, T.2
  • 24
    • 21144441269 scopus 로고    scopus 로고
    • Glutamyl-tRNA reductase of Chlorobium vibrioforme is a dissociable homodimer that contains one tightly bound heme per subunit
    • DOI 10.1128/JB.187.13.4444-4450.2005
    • Srivastava A., Beale S. I., Glutamyl-tRNA reductase of Chlorobium vibrioforme is a dissociable homodimer that contains one tightly bound heme per subunit. Journal of Bacteriology 2005 187 13 4444 4450 2-s2.0-21144441269 10.1128/JB.187.13.4444-4450.2005 (Pubitemid 40880954)
    • (2005) Journal of Bacteriology , vol.187 , Issue.13 , pp. 4444-4450
    • Srivastava, A.1    Beale, S.I.2
  • 25
    • 55649122540 scopus 로고    scopus 로고
    • Differential regulation of human ALAS1 mRNA and protein levels by heme and cobalt protoporphyrin
    • 2-s2.0-55649122540 10.1007/s11010-008-9888-0
    • Zheng J., Shan Y., Lambrecht R. W., Donohue S. E., Bonkovsky H. L., Differential regulation of human ALAS1 mRNA and protein levels by heme and cobalt protoporphyrin. Molecular and Cellular Biochemistry 2008 319 1-2 153 161 2-s2.0-55649122540 10.1007/s11010-008-9888-0
    • (2008) Molecular and Cellular Biochemistry , vol.319 , Issue.1-2 , pp. 153-161
    • Zheng, J.1    Shan, Y.2    Lambrecht, R.W.3    Donohue, S.E.4    Bonkovsky, H.L.5
  • 26
    • 38449083833 scopus 로고    scopus 로고
    • Haeme-regulated degradation of δ-aminolevulinate synthase 1 in rat liver mitochondria
    • DOI 10.1093/jb/mvm159
    • Yoshino K., Munakata H., Kuge O., Ito A., Ogishima T., Haeme-regulated degradation of δ -aminolevulinate synthase 1 in rat liver mitochondria. Journal of Biochemistry 2007 142 4 453 458 2-s2.0-38449083833 10.1093/jb/mvm159 (Pubitemid 351197678)
    • (2007) Journal of Biochemistry , vol.142 , Issue.4 , pp. 453-458
    • Yoshino, K.1    Munakata, H.2    Kuge, O.3    Ito, A.4    Ogishima, T.5
  • 27
    • 0035282866 scopus 로고    scopus 로고
    • Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: Functional characterization using new analysis and information visualization methods
    • Sofia H. J., Chen G., Hetzler B. G., Reyes-Spindola J. F., Miller N. E., Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods. Nucleic Acids Research 2001 29 5 1097 1106 2-s2.0-0035282866 (Pubitemid 32186195)
    • (2001) Nucleic Acids Research , vol.29 , Issue.5 , pp. 1097-1106
    • Sofia, H.J.1    Chen, G.2    Hetzler, B.G.3    Reyes-Spindola, J.F.4    Miller, N.E.5
  • 28
    • 84866011930 scopus 로고    scopus 로고
    • Identification and function of auxiliary iron-sulfur clusters in radical SAM enzymes
    • 10.1016/j.bbapap.2012.07.009
    • Lanz N. D., Booker S. J., Identification and function of auxiliary iron-sulfur clusters in radical SAM enzymes. Biochimica et Biophysica Acta 2012 1824 11 1196 1212 10.1016/j.bbapap.2012.07.009
    • (2012) Biochimica et Biophysica Acta , vol.1824 , Issue.11 , pp. 1196-1212
    • Lanz, N.D.1    Booker, S.J.2


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