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Volumn 196, Issue 1, 2014, Pages 60-69

Corynebacterium glutamicum ArnR controls expression of nitrate reductase operon narKGHJI and nitric oxide (no)-detoxifying enzyme gene hmp in an NO-responsive manner

Author keywords

[No Author keywords available]

Indexed keywords

ARNR PROTEIN; BACTERIAL PROTEIN; CYSTEINE; HMP PROTEIN; NARK PROTEIN; NITRATE REDUCTASE; NITRIC OXIDE; NITRITE; UNCLASSIFIED DRUG;

EID: 84890280939     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.01004-13     Document Type: Article
Times cited : (12)

References (48)
  • 1
    • 0041429540 scopus 로고    scopus 로고
    • Industrial production of amino acids by coryneform bacteria
    • Hermann T. 2003. Industrial production of amino acids by coryneform bacteria. J. Biotechnol. 104:155-172. http://dx.doi.org/10.1016/S0168-1656(03)00149-4.
    • (2003) J. Biotechnol. , vol.104 , pp. 155-172
    • Hermann, T.1
  • 2
    • 0037271033 scopus 로고    scopus 로고
    • Amino acid production processes
    • Ikeda M. 2003. Amino acid production processes. Adv. Biochem. Eng. Biotechnol. 79:1-35. http://dx.doi.org/10.1007/3-540-45989-8_1.
    • (2003) Adv. Biochem. Eng. Biotechnol. , vol.79 , pp. 1-35
    • Ikeda, M.1
  • 3
    • 34547461685 scopus 로고    scopus 로고
    • Anaerobic growth of Corynebacterium glutamicum using nitrate as a terminal electron acceptor
    • Nishimura T, Vertès AA, Shinoda Y, Inui M, Yukawa H. 2007. Anaerobic growth of Corynebacterium glutamicum using nitrate as a terminal electron acceptor. Appl. Microbiol. Biotechnol. 75:889-897. http://dx.doi.org/10.1007/s00253-007-0879-y.
    • (2007) Appl. Microbiol. Biotechnol. , vol.75 , pp. 889-897
    • Nishimura, T.1    Vertès, A.A.2    Shinoda, Y.3    Inui, M.4    Yukawa, H.5
  • 4
    • 34250628080 scopus 로고    scopus 로고
    • Anaerobic growth and potential for amino acid production by nitrate respiration in Corynebacterium glutamicum
    • Takeno S, Ohnishi J, Komatsu T, Masaki T, Sen K, Ikeda M. 2007. Anaerobic growth and potential for amino acid production by nitrate respiration in Corynebacterium glutamicum. Appl. Microbiol. Biotechnol. 75:1173-1182. http://dx.doi.org/10.1007/s00253-007-0926-8.
    • (2007) Appl. Microbiol. Biotechnol. , vol.75 , pp. 1173-1182
    • Takeno, S.1    Ohnishi, J.2    Komatsu, T.3    Masaki, T.4    Sen, K.5    Ikeda, M.6
  • 5
    • 0036225848 scopus 로고    scopus 로고
    • The roles of the polytopic membrane proteins NarK, NarU and NirC in Escherichia coli K-12: two nitrate and three nitrite transporters
    • Clegg S, Yu F, Griffiths L, Cole JA. 2002. The roles of the polytopic membrane proteins NarK, NarU and NirC in Escherichia coli K-12: two nitrate and three nitrite transporters. Mol. Microbiol. 44:143-155. http://dx.doi.org/10.1046/j.1365-2958.2002.02858.x.
    • (2002) Mol. Microbiol. , vol.44 , pp. 143-155
    • Clegg, S.1    Yu, F.2    Griffiths, L.3    Cole, J.A.4
  • 6
    • 84866481440 scopus 로고    scopus 로고
    • Mutational analysis of the respiratory nitrate transporter NarK2 of Mycobacterium tuberculosis
    • Giffin MM, Raab RW, Morganstern M, Sohaskey CD. 2012. Mutational analysis of the respiratory nitrate transporter NarK2 of Mycobacterium tuberculosis. PLoS One 7:e45459. http://dx.doi.org/10.1371/journal.pone.0045459.
    • (2012) PLoS One , vol.7
    • Giffin, M.M.1    Raab, R.W.2    Morganstern, M.3    Sohaskey, C.D.4
  • 7
    • 0032704710 scopus 로고    scopus 로고
    • Prokaryotic nitrate reduction: molecular properties and functional distinction among bacterial nitrate reductases
    • Moreno-Vivián C, Cabello P, Martínez-Luque M, Blasco R, Castillo F. 1999. Prokaryotic nitrate reduction: molecular properties and functional distinction among bacterial nitrate reductases. J. Bacteriol. 181:6573-6584.
    • (1999) J. Bacteriol. , vol.181 , pp. 6573-6584
    • Moreno-Vivián, C.1    Cabello, P.2    Martínez-Luque, M.3    Blasco, R.4    Castillo, F.5
  • 8
    • 0028587191 scopus 로고
    • Nitrate reductases in Escherichia coli
    • Bonnefoy V, Demoss JA. 1994. Nitrate reductases in Escherichia coli. Antonie Van Leeuwenhoek 66:47-56. http://dx.doi.org/10.1007/BF00871632.
    • (1994) Antonie Van Leeuwenhoek , vol.66 , pp. 47-56
    • Bonnefoy, V.1    Demoss, J.A.2
  • 9
    • 0031456471 scopus 로고    scopus 로고
    • Cell biology and molecular basis of denitrification
    • Zumft WG. 1997. Cell biology and molecular basis of denitrification. Microbiol. Mol. Biol. Rev. 61:533-616.
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 533-616
    • Zumft, W.G.1
  • 10
    • 79952370254 scopus 로고    scopus 로고
    • Gene expression profiling of Corynebacterium glutamicum during anaerobic nitrate respiration: induction of the SOS response for cell survival
    • Nishimura T, Teramoto H, Inui M, Yukawa H. 2011. Gene expression profiling of Corynebacterium glutamicum during anaerobic nitrate respiration: induction of the SOS response for cell survival. J. Bacteriol. 193: 1327-1333. http://dx.doi.org/10.1128/JB.01453-10.
    • (2011) J. Bacteriol. , vol.193 , pp. 1327-1333
    • Nishimura, T.1    Teramoto, H.2    Inui, M.3    Yukawa, H.4
  • 11
    • 0030937832 scopus 로고    scopus 로고
    • Nitric oxide and macrophage function
    • MacMicking J, Xie QW, Nathan C. 1997. Nitric oxide and macrophage function. Annu. Rev. Immunol. 15:323-350. http://dx.doi.org/10.1146/annurev.immunol.15.1.323.
    • (1997) Annu. Rev. Immunol. , vol.15 , pp. 323-350
    • MacMicking, J.1    Xie, Q.W.2    Nathan, C.3
  • 12
    • 4844227764 scopus 로고    scopus 로고
    • Antimicrobial reactive oxygen and nitrogen species: concepts and controversies
    • Fang FC. 2004. Antimicrobial reactive oxygen and nitrogen species: concepts and controversies. Nat. Rev. Microbiol. 2:820-832. http://dx.doi.org/10.1038/nrmicro1004.
    • (2004) Nat. Rev. Microbiol. , vol.2 , pp. 820-832
    • Fang, F.C.1
  • 14
    • 0037013239 scopus 로고    scopus 로고
    • Direct evidence for nitric oxide production by a nitric-oxide synthase-like protein from Bacillus subtilis
    • Adak S, Aulak KS, Stuehr DJ. 2002. Direct evidence for nitric oxide production by a nitric-oxide synthase-like protein from Bacillus subtilis. J. Biol. Chem. 277:16167-16171. http://dx.doi.org/10.1074/jbc. M201136200.
    • (2002) J. Biol. Chem. , vol.277 , pp. 16167-16171
    • Adak, S.1    Aulak, K.S.2    Stuehr, D.J.3
  • 16
    • 45549109686 scopus 로고    scopus 로고
    • Nitric oxide homeostasis in Salmonella typhimurium: roles of respiratory nitrate reductase and flavohemoglobin
    • Gilberthorpe NJ, Poole RK. 2008. Nitric oxide homeostasis in Salmonella typhimurium: roles of respiratory nitrate reductase and flavohemoglobin. J. Biol. Chem. 283:11146-11154. http://dx.doi.org/10.1074/jbc. M708019200.
    • (2008) J. Biol. Chem. , vol.283 , pp. 11146-11154
    • Gilberthorpe, N.J.1    Poole, R.K.2
  • 17
    • 79953298366 scopus 로고    scopus 로고
    • Iron-containing transcription factors and their roles as sensors
    • Fleischhacker AS, Kiley PJ. 2011. Iron-containing transcription factors and their roles as sensors. Curr. Opin. Chem. Biol. 15:335-341. http://dx.doi.org/10.1016/j.cbpa.2011.01.006.
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 335-341
    • Fleischhacker, A.S.1    Kiley, P.J.2
  • 18
    • 77950862348 scopus 로고    scopus 로고
    • There's NO stopping NsrR, a global regulator of the bacterial NO stress response
    • Tucker NP, Le Brun NE, Dixon R, Hutchings MI. 2010. There's NO stopping NsrR, a global regulator of the bacterial NO stress response. Trends Microbiol. 18:149-156. http://dx.doi.org/10.1016/j.tim.2009.12.009.
    • (2010) Trends Microbiol. , vol.18 , pp. 149-156
    • Tucker, N.P.1    Le Brun, N.E.2    Dixon, R.3    Hutchings, M.I.4
  • 19
    • 42549123126 scopus 로고    scopus 로고
    • ArnR, a novel transcriptional regulator, represses expression of the narKGHJI operon in Corynebacterium glutamicum
    • Nishimura T, Teramoto H, Vertès AA, Inui M, Yukawa H. 2008. ArnR, a novel transcriptional regulator, represses expression of the narKGHJI operon in Corynebacterium glutamicum. J. Bacteriol. 190:3264-3273. http://dx.doi.org/10.1128/JB.01801-07.
    • (2008) J. Bacteriol. , vol.190 , pp. 3264-3273
    • Nishimura, T.1    Teramoto, H.2    Vertès, A.A.3    Inui, M.4    Yukawa, H.5
  • 22
    • 0032564409 scopus 로고    scopus 로고
    • Nitrosative stress: metabolic pathway involving the flavohemoglobin
    • Hausladen A, Gow AJ, Stamler JS. 1998. Nitrosative stress: metabolic pathway involving the flavohemoglobin. Proc. Natl. Acad. Sci. U. S. A. 95:14100-14105. http://dx.doi.org/10.1073/pnas.95.24.14100.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 14100-14105
    • Hausladen, A.1    Gow, A.J.2    Stamler, J.S.3
  • 23
    • 84858964958 scopus 로고    scopus 로고
    • Protection from nitrosative stress: a central role for microbial flavohemoglobin
    • Forrester MT, Foster MW. 2012. Protection from nitrosative stress: a central role for microbial flavohemoglobin. Free Radic. Biol. Med. 52: 1620-1633. http://dx.doi.org/10.1016/j.freeradbiomed.2012.01.028.
    • (2012) Free Radic. Biol. Med. , vol.52 , pp. 1620-1633
    • Forrester, M.T.1    Foster, M.W.2
  • 24
    • 0033017012 scopus 로고    scopus 로고
    • Anoxic function for the Escherichia coli flavohaemoglobin (Hmp): reversible binding of nitric oxide and reduction to nitrous oxide
    • Kim SO, Orii Y, Lloyd D, Hughes MN, Poole RK. 1999. Anoxic function for the Escherichia coli flavohaemoglobin (Hmp): reversible binding of nitric oxide and reduction to nitrous oxide. FEBS Lett. 445:389-394. http://dx.doi.org/10.1016/S0014-5793(99)00157-X.
    • (1999) FEBS Lett. , vol.445 , pp. 389-394
    • Kim, S.O.1    Orii, Y.2    Lloyd, D.3    Hughes, M.N.4    Poole, R.K.5
  • 25
    • 0035863151 scopus 로고    scopus 로고
    • Escherichia coli flavohaemoglobin (Hmp) with equistoichiometric FAD and haem contents has a low affinity for dioxygen in the absence or presence of nitric oxide
    • Mills CE, Sedelnikova S, Søballe B, Hughes MN, Poole RK. 2001. Escherichia coli flavohaemoglobin (Hmp) with equistoichiometric FAD and haem contents has a low affinity for dioxygen in the absence or presence of nitric oxide. Biochem. J. 353:207-213. http://dx.doi.org/10.1042/0264-6021:3530207.
    • (2001) Biochem. J. , vol.353 , pp. 207-213
    • Mills, C.E.1    Sedelnikova, S.2    Søballe, B.3    Hughes, M.N.4    Poole, R.K.5
  • 27
    • 4644247295 scopus 로고    scopus 로고
    • Metabolic analysis of Corynebacterium glutamicum during lactate and succinate productions under oxygen deprivation conditions
    • Inui M, Murakami S, Okino S, Kawaguchi H, Vertès AA, Yukawa H. 2004. Metabolic analysis of Corynebacterium glutamicum during lactate and succinate productions under oxygen deprivation conditions. J. Mol. Microbiol. Biotechnol. 7:182-196. http://dx.doi.org/10.1159/000079827.
    • (2004) J. Mol. Microbiol. Biotechnol. , vol.7 , pp. 182-196
    • Inui, M.1    Murakami, S.2    Okino, S.3    Kawaguchi, H.4    Vertès, A.A.5    Yukawa, H.6
  • 28
    • 25444479070 scopus 로고    scopus 로고
    • Metabolic engineering of Corynebacterium glutamicum for fuel ethanol production under oxygen-deprivation conditions
    • Inui M, Kawaguchi H, Murakami S, Vertès AA, Yukawa H. 2004. Metabolic engineering of Corynebacterium glutamicum for fuel ethanol production under oxygen-deprivation conditions. J. Mol. Microbiol. Biotechnol. 8:243-254. http://dx.doi.org/10.1159/000086705.
    • (2004) J. Mol. Microbiol. Biotechnol. , vol.8 , pp. 243-254
    • Inui, M.1    Kawaguchi, H.2    Murakami, S.3    Vertès, A.A.4    Yukawa, H.5
  • 29
    • 0003903343 scopus 로고
    • Molecular cloning: a laboratory manual, 2nd ed
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Sambrook J, Fritsch EF, Maniatis T. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1989)
    • Sambrook, J.1    Fritsch, E.F.2    Maniatis, T.3
  • 30
    • 78650066340 scopus 로고    scopus 로고
    • Antisense-RNA-mediated plasmid copy number control in pCG1-family plasmids, pCGR2 and pCG1, in Corynebacterium glutamicum
    • Okibe N, Suzuki N, Inui M, Yukawa H. 2010. Antisense-RNA-mediated plasmid copy number control in pCG1-family plasmids, pCGR2 and pCG1, in Corynebacterium glutamicum. Microbiology 156:3609-3623. http://dx.doi.org/10.1099/mic.0.043745-0.
    • (2010) Microbiology , vol.156 , pp. 3609-3623
    • Okibe, N.1    Suzuki, N.2    Inui, M.3    Yukawa, H.4
  • 31
    • 0027289448 scopus 로고
    • Presence of mrr- and mcr-like restriction systems in coryneform bacteria
    • Vertès AA, Inui M, Kobayashi M, Kurusu Y, Yukawa H. 1993. Presence of mrr- and mcr-like restriction systems in coryneform bacteria. Res. Microbiol. 144:181-185. http://dx.doi.org/10.1016/0923-2508(93)90043-2.
    • (1993) Res. Microbiol. , vol.144 , pp. 181-185
    • Vertès, A.A.1    Inui, M.2    Kobayashi, M.3    Kurusu, Y.4    Yukawa, H.5
  • 32
    • 0017184389 scopus 로고
    • Arapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • BradfordMM.1976.Arapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254. http://dx.doi.org/10.1016/0003-2697(76)90527-3.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 33
    • 14644387541 scopus 로고    scopus 로고
    • Nitric oxide and nitrosative stress tolerance in bacteria
    • Poole RK. 2005. Nitric oxide and nitrosative stress tolerance in bacteria. Biochem. Soc. Trans. 33:176-180. http://dx.doi.org/10.1042/BST0330176.
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 176-180
    • Poole, R.K.1
  • 35
    • 0027989421 scopus 로고
    • Aerobic-anaerobic gene regulation in Escherichia coli: control by the ArcAB and Fnr regulons
    • Gunsalus RP, Park SJ. 1994. Aerobic-anaerobic gene regulation in Escherichia coli: control by the ArcAB and Fnr regulons. Res. Microbiol. 145: 437-450. http://dx.doi.org/10.1016/0923-2508(94)90092-2.
    • (1994) Res. Microbiol. , vol.145 , pp. 437-450
    • Gunsalus, R.P.1    Park, S.J.2
  • 36
    • 0024989737 scopus 로고
    • FNR and its role in oxygen-regulated gene expression in Escherichia coli
    • Spiro S, Guest JR. 1990. FNR and its role in oxygen-regulated gene expression in Escherichia coli. FEMS Microbiol. Rev. 6:399-428.
    • (1990) FEMS Microbiol. Rev. , vol.6 , pp. 399-428
    • Spiro, S.1    Guest, J.R.2
  • 37
    • 0344153756 scopus 로고    scopus 로고
    • Phylogeny of the bacterial superfamily of Crp-Fnr transcription regulators: exploiting the metabolic spectrum by controlling alternative gene programs
    • Körner H, Sofia HJ, Zumft WG. 2003. Phylogeny of the bacterial superfamily of Crp-Fnr transcription regulators: exploiting the metabolic spectrum by controlling alternative gene programs. FEMS Microbiol. Rev. 27:559-592. http://dx.doi.org/10.1016/S0168-6445(03)00066-4.
    • (2003) FEMS Microbiol. Rev. , vol.27 , pp. 559-592
    • Körner, H.1    Sofia, H.J.2    Zumft, W.G.3
  • 38
    • 78650720288 scopus 로고    scopus 로고
    • Regulation of the nitrate reductase operon narKGHJI by the cAMPdependent regulator GlxR in Corynebacterium glutamicum
    • Nishimura T, Teramoto H, Toyoda K, Inui M, Yukawa H. 2011. Regulation of the nitrate reductase operon narKGHJI by the cAMPdependent regulator GlxR in Corynebacterium glutamicum. Microbiology 157:21-28. http://dx.doi.org/10.1099/mic.0.044552-0.
    • (2011) Microbiology , vol.157 , pp. 21-28
    • Nishimura, T.1    Teramoto, H.2    Toyoda, K.3    Inui, M.4    Yukawa, H.5
  • 39
    • 0344780881 scopus 로고    scopus 로고
    • Nitrate and nitrite control of respiratory nitrate reduction in denitrifying Pseudomonas stutzeri by a two-component regulatory system homologous to NarXL of Escherichia coli
    • Härtig E, Schiek U, Vollack KU, Zumft WG. 1999. Nitrate and nitrite control of respiratory nitrate reduction in denitrifying Pseudomonas stutzeri by a two-component regulatory system homologous to NarXL of Escherichia coli. J. Bacteriol. 181:3658-3665.
    • (1999) J. Bacteriol. , vol.181 , pp. 3658-3665
    • Härtig, E.1    Schiek, U.2    Vollack, K.U.3    Zumft, W.G.4
  • 40
    • 34249818178 scopus 로고    scopus 로고
    • The anaerobic regulatory network required for Pseudomonas aeruginosa nitrate respiration
    • Schreiber K, Krieger R, Benkert B, Eschbach M, Arai H, Schobert M, Jahn D. 2007. The anaerobic regulatory network required for Pseudomonas aeruginosa nitrate respiration. J. Bacteriol. 189:4310-4314. http://dx.doi.org/10.1128/JB.00240-07.
    • (2007) J. Bacteriol. , vol.189 , pp. 4310-4314
    • Schreiber, K.1    Krieger, R.2    Benkert, B.3    Eschbach, M.4    Arai, H.5    Schobert, M.6    Jahn, D.7
  • 42
    • 28844486003 scopus 로고    scopus 로고
    • The AraC-type regulator RipA represses aconitase and other iron proteins from Corynebacterium under iron limitation and is itself repressed by DtxR
    • Wennerhold J, Krug A, Bott M. 2005. The AraC-type regulator RipA represses aconitase and other iron proteins from Corynebacterium under iron limitation and is itself repressed by DtxR. J. Biol. Chem. 280:40500-40508. http://dx.doi.org/10.1074/jbc. M508693200.
    • (2005) J. Biol. Chem. , vol.280 , pp. 40500-40508
    • Wennerhold, J.1    Krug, A.2    Bott, M.3
  • 43
    • 77956549301 scopus 로고    scopus 로고
    • RosR (Cg1324), a hydrogen peroxide-sensitive MarR-type transcriptional regulator of Corynebacterium glutamicum
    • Bussmann M, Baumgart M, Bott M. 2010. RosR (Cg1324), a hydrogen peroxide-sensitive MarR-type transcriptional regulator of Corynebacterium glutamicum. J. Biol. Chem. 285:29305-29318. http://dx.doi.org/10.1074/jbc. M110.156372.
    • (2010) J. Biol. Chem. , vol.285 , pp. 29305-29318
    • Bussmann, M.1    Baumgart, M.2    Bott, M.3
  • 44
    • 85044710067 scopus 로고    scopus 로고
    • Dissimilatory metabolism of nitrogen oxides in bacteria: comparative reconstruction of transcriptional networks
    • Rodionov DA, Dubchak IL, Arkin AP, Alm EJ, Gelfand MS. 2005. Dissimilatory metabolism of nitrogen oxides in bacteria: comparative reconstruction of transcriptional networks. PLoS Comput. Biol. 1:e55. http://dx.doi.org/10.1371/journal.pcbi.0010055.
    • (2005) PLoS Comput. Biol. , vol.1
    • Rodionov, D.A.1    Dubchak, I.L.2    Arkin, A.P.3    Alm, E.J.4    Gelfand, M.S.5
  • 45
    • 78649728803 scopus 로고    scopus 로고
    • Nitric oxide-sensitive and -insensitive interaction of Bacillus subtilis NsrR with a ResDE-controlled promoter
    • Kommineni S, Yukl E, Hayashi T, Delepine J, Geng H, Moënne-Loccoz P, Nakano MM. 2010. Nitric oxide-sensitive and -insensitive interaction of Bacillus subtilis NsrR with a ResDE-controlled promoter. Mol. Microbiol. 78:1280-1293. http://dx.doi.org/10.1111/j.1365-2958.2010.07407.x.
    • (2010) Mol. Microbiol. , vol.78 , pp. 1280-1293
    • Kommineni, S.1    Yukl, E.2    Hayashi, T.3    Delepine, J.4    Geng, H.5    Moënne-Loccoz, P.6    Nakano, M.M.7
  • 46
    • 58149136356 scopus 로고    scopus 로고
    • Functional analysis of NsrR, a nitric oxide-sensing Rrf2 repressor in Neisseria gonorrhoeae
    • Isabella VM, Lapek JD, Jr, Kennedy EM, Clark VL. 2009. Functional analysis of NsrR, a nitric oxide-sensing Rrf2 repressor in Neisseria gonorrhoeae. Mol. Microbiol. 71:227-239. http://dx.doi.org/10.1111/j.1365-2958.2008.06522.x.
    • (2009) Mol. Microbiol. , vol.71 , pp. 227-239
    • Isabella, V.M.1    Lapek, J.D.2    Kennedy, E.M.3    Clark, V.L.4
  • 48
    • 57449099080 scopus 로고    scopus 로고
    • Transcription factor NsrR from Bacillus subtilis senses nitric oxide with a 4Fe-4S cluster (dagger)
    • Yukl ET, Elbaz MA, Nakano MM, Moënne-Loccoz P. 2008. Transcription factor NsrR from Bacillus subtilis senses nitric oxide with a 4Fe-4S cluster (dagger). Biochemistry 47:13084-13092. http://dx.doi.org/10.1021/bi801342x.
    • (2008) Biochemistry , vol.47 , pp. 13084-13092
    • Yukl, E.T.1    Elbaz, M.A.2    Nakano, M.M.3    Moënne-Loccoz, P.4


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