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Volumn 19, Issue 17, 2013, Pages 1999-2012

Analysis of the bacterial response to Ru(CO)3Cl(Glycinate) (CORM-3) and the inactivated compound identifies the role played by the ruthenium compound and reveals sulfur-containing species as a major target of CORM-3 Action

Author keywords

[No Author keywords available]

Indexed keywords

ANTIINFECTIVE AGENT; CARBON MONOXIDE; CORM 3; CYSTEINE; METHIONINE; RUTHENIUM DERIVATIVE; UNCLASSIFIED DRUG;

EID: 84885179456     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2012.5103     Document Type: Article
Times cited : (39)

References (44)
  • 1
    • 0028860781 scopus 로고
    • Expression and characterization of the Escherichia coli fdo locus and a possible physiological role for aerobic formate dehydrogenase
    • Abaibou H, Pommier J, Benoit S, Giordano G, and Mandrandberthelot MA. Expression and characterization of the Escherichia coli fdo locus and a possible physiological role for aerobic formate dehydrogenase. J Bacteriol 177: 7141-7149, 1995.
    • (1995) J Bacteriol , vol.177 , pp. 7141-7149
    • Abaibou, H.1    Pommier, J.2    Benoit, S.3    Giordano, G.4    Mandrandberthelot, M.A.5
  • 2
    • 0036177861 scopus 로고    scopus 로고
    • Quantitative assessment of oxygen availability: Perceived aerobiosis and its effect on flux distribution in the respiratory chain of Escherichia coli
    • Alexeeva S, Hellingwerf KJ, and de Mattos MJT. Quantitative assessment of oxygen availability: perceived aerobiosis and its effect on flux distribution in the respiratory chain of Escherichia coli. J Bacteriol 184: 1402-1406, 2002.
    • (2002) J Bacteriol , vol.184 , pp. 1402-1406
    • Alexeeva, S.1    Hellingwerf, K.J.2    De Mattos, M.J.T.3
  • 7
    • 81855175401 scopus 로고    scopus 로고
    • The diversity of microbial responses to nitric oxide and agents of nitrosative stress: Close cousins but not identical twins
    • edited by Poole RK. London Elsevier
    • Bowman LAH, McLean S, Poole RK, and Fukuto JM. The diversity of microbial responses to nitric oxide and agents of nitrosative stress: close cousins but not identical twins. In: Advances in Microbial Physiology, Vol 59, edited by Poole RK. London: Elsevier, 2011, pp. 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
  • 9
    • 77957167459 scopus 로고    scopus 로고
    • Carbon monoxide in biology microbiology surprising roles for the ''detroit perfume.''
    • Davidge KS, Motterlini R, Mann BE, Wilson JL, and Poole RK. Carbon monoxide in biology and microbiology: surprising roles for the ''Detroit perfume.'' Adv Microb Physiol 56: 85-167, 2009.
    • (2009) Adv Microb Physiol , vol.56 , pp. 85-167
    • Davidge, K.S.1    Motterlini, R.2    Mann, B.E.3    Wilson, J.L.4    Poole, R.K.5
  • 14
    • 3042934967 scopus 로고
    • Tissue sulfhydryl groups
    • Ellman GL. Tissue sulfhydryl groups. Arch Biochem Biophys 82: 70-77, 1959.
    • (1959) Arch Biochem Biophys , vol.82 , pp. 70-77
    • Ellman, G.L.1
  • 16
    • 15444363634 scopus 로고    scopus 로고
    • Transcriptional responses of Escherichia coli to S-nitrosoglutathione under defined chemostat conditions reveal major changes in methionine biosynthesis
    • Flatley J, Barrett J, Pullan ST, Hughes MN, Green J, and Poole RK. Transcriptional responses of Escherichia coli to S-nitrosoglutathione under defined chemostat conditions reveal major changes in methionine biosynthesis. J Biol Chem 280: 10065-10072, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 10065-10072
    • Flatley, J.1    Barrett, J.2    Pullan, S.T.3    Hughes, M.N.4    Green, J.5    Poole, R.K.6
  • 18
    • 45549109686 scopus 로고    scopus 로고
    • Nitric oxide homeostasis in Salmonella typhimurium - Roles of respiratory nitrate reductase and flavohemoglobin
    • Gilberthorpe NJ, and Poole RK. Nitric oxide homeostasis in Salmonella typhimurium - roles of respiratory nitrate reductase and flavohemoglobin. J Biol Chem 283: 11146-11154, 2008.
    • (2008) J Biol Chem , vol.283 , pp. 11146-11154
    • Gilberthorpe, N.J.1    Poole, R.K.2
  • 19
    • 67650543887 scopus 로고    scopus 로고
    • Severe zinc depletion of Escherichia coli roles for high affinity zinc binding by ZinT, zinc transport and zinc-independent proteins
    • Graham AI, Hunt S, Stokes SL, Bramall N, Bunch J, Cox AG, McLeod CW, and Poole RK. Severe zinc depletion of Escherichia coli roles for high affinity zinc binding by ZinT, zinc transport and zinc-independent proteins. J Biol Chem 284: 18377-18389, 2009.
    • (2009) J Biol Chem , vol.284 , pp. 18377-18389
    • Graham, A.I.1    Hunt, S.2    Stokes, S.L.3    Bramall, N.4    Bunch, J.5    Cox, A.G.6    McLeod, C.W.7    Poole, R.K.8
  • 20
    • 84855243112 scopus 로고    scopus 로고
    • Dynamics of a starvation-to-surfeit shift: A transcriptomic and modelling analysis of the bacterial response to zinc reveals transient behaviour of the fur and SoxS regulators
    • Graham AI, Sanguinetti G, Bramall N, McLeod CW, and Poole RK. Dynamics of a starvation-to-surfeit shift: a transcriptomic and modelling analysis of the bacterial response to zinc reveals transient behaviour of the Fur and SoxS regulators. Microbiology 158: 284-292, 2012.
    • (2012) Microbiology , vol.158 , pp. 284-292
    • Graham, A.I.1    Sanguinetti, G.2    Bramall, N.3    McLeod, C.W.4    Poole, R.K.5
  • 21
    • 41949119905 scopus 로고    scopus 로고
    • Determination of the Escherichia coli S-nitrosoglutathione response network using integrated biochemical and systems analysis
    • Jarboe LR, Hyduke DR, Tran LM, Chou KJY, and Liao JC. Determination of the Escherichia coli S-nitrosoglutathione response network using integrated biochemical and systems analysis. J Biol Chem 283: 5148-5157, 2008.
    • (2008) J Biol Chem , vol.283 , pp. 5148-5157
    • Jarboe, L.R.1    Hyduke, D.R.2    Tran, L.M.3    Chou, K.J.Y.4    Liao, J.C.5
  • 22
    • 34047228780 scopus 로고    scopus 로고
    • Metal carbonyls as pharmaceuticals Ru(CO)3Cl(glycinate), a CO-releasing molecule with an extensive aqueous solution chemistry
    • Johnson TR, Mann BE, Teasdale IP, Adams H, Foresti R, Green CJ, and Motterlini R. Metal carbonyls as pharmaceuticals Ru(CO)3Cl(glycinate), a CO-releasing molecule with an extensive aqueous solution chemistry. Dalton Trans 1500-1508, 2007.
    • (2007) Dalton Trans , pp. 1500-1508
    • Johnson, T.R.1    Mann, B.E.2    Teasdale, I.P.3    Adams, H.4    Foresti, R.5    Green, C.J.6    Motterlini, R.7
  • 24
    • 50449147866 scopus 로고
    • Transduction of linked genetic characters of the host by bacteriophage-PL
    • Lennox ES. Transduction of linked genetic characters of the host by bacteriophage-PL. Virology 1: 190-206, 1955.
    • (1955) Virology , vol.1 , pp. 190-206
    • Lennox, E.S.1
  • 25
    • 33748053969 scopus 로고    scopus 로고
    • The housekeeping dipeptide permease is the Escherichia coli heme transporter and functions with two optional peptide binding proteins
    • Letoffe S, Delepelaire P, and Wandersman C. The housekeeping dipeptide permease is the Escherichia coli heme transporter and functions with two optional peptide binding proteins. Proc Natl Acad Sci U S A 103: 12891-12896, 2006.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 12891-12896
    • Letoffe, S.1    Delepelaire, P.2    Wandersman, C.3
  • 26
    • 77956673882 scopus 로고    scopus 로고
    • Carbon monoxide an essential signalling molecule
    • edited by Jaouen E and Metzler-Nolte N. Berlin Springer Verlog
    • Mann BE. Carbon monoxide: an essential signalling molecule. In: Medicinal Organometallic Chemistry, edited by Jaouen E and Metzler-Nolte N. Berlin: Springer-Verlog, 2010, pp. 247-285.
    • (2010) Medicinal Organometallic Chemistry , pp. 247-285
    • Mann, B.E.1
  • 28
    • 84861624301 scopus 로고    scopus 로고
    • Sulfite species enhance carbon monoxide release from CO-releasing molecules: Implications for the deoxymyoglobin assay of activity
    • McLean S, Mann BE, and Poole RK. Sulfite species enhance carbon monoxide release from CO-releasing molecules: implications for the deoxymyoglobin assay of activity. Anal Biochem 427: 36-40, 2012.
    • (2012) Anal Biochem , vol.427 , pp. 36-40
    • McLean, S.1    Mann, B.E.2    Poole, R.K.3
  • 31
    • 0037147266 scopus 로고    scopus 로고
    • Cysteine is exported from the Escherichia coli cytoplasm by CydDC, an ATP-binding cassette-type transporter required for cytochrome assembly
    • Pittman MS, Corker H, Wu GH, Binet MB, Moir AJG, and Poole RK. Cysteine is exported from the Escherichia coli cytoplasm by CydDC, an ATP-binding cassette-type transporter required for cytochrome assembly. J Biol Chem 277: 49841-49849, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 49841-49849
    • Pittman, M.S.1    Corker, H.2    Wu, G.H.3    Binet, M.B.4    Moir, A.J.G.5    Poole, R.K.6
  • 32
    • 0036033555 scopus 로고    scopus 로고
    • A third envelope stress signal transduction pathway in Escherichia coli
    • Raffa RG, and Raivio TL. A third envelope stress signal transduction pathway in Escherichia coli. Mol Microbiol 45: 1599-1611, 2002.
    • (2002) Mol Microbiol , vol.45 , pp. 1599-1611
    • Raffa, R.G.1    Raivio, T.L.2
  • 35
    • 33751008680 scopus 로고    scopus 로고
    • Probabilistic inference of transcription factor concentrations and genespecific regulatory activities
    • Sanguinetti G, Lawrence ND, and Rattray M. Probabilistic inference of transcription factor concentrations and genespecific regulatory activities. Bioinformatics 22: 2775-2781, 2006.
    • (2006) Bioinformatics , vol.22 , pp. 2775-2781
    • Sanguinetti, G.1    Lawrence, N.D.2    Rattray, M.3
  • 36
    • 84869090746 scopus 로고    scopus 로고
    • New insights into the chemistry of fac-[Ru(CO)3]2 + fragments in biologically relevant conditions: The CO releasing activity of [Ru(CO)3 Cl2(1,3-thiazole)], and the X-ray crystal structure of its adduct with Lysozyme
    • Santos MFA, Seixas JD, Coelho AC, Mukhopadhyay A, Reis PM, Romao CC, and Santos-Silva T. New insights into the chemistry of fac-[Ru(CO)3]2 + fragments in biologically relevant conditions: the CO releasing activity of [Ru(CO)3 Cl2(1,3-thiazole)], and the X-ray crystal structure of its adduct with Lysozyme. J Inorg Biochem 117: 285, 2012.
    • (2012) J Inorg Biochem , vol.117 , pp. 285
    • Santos, M.F.A.1    Seixas, J.D.2    Coelho, A.C.3    Mukhopadhyay, A.4    Reis, P.M.5    Romao, C.C.6    Santos-Silva, T.7
  • 37
    • 79551692596 scopus 로고    scopus 로고
    • CORM-3 reactivity toward proteins: The crystal structure of a Ru(II) dicarbonyl-lysozyme complex
    • Santos-Silva T, Mukhopadhyay A, Seixas JD, Bernardes GJL, Romao CC, and Romao MJ. CORM-3 reactivity toward proteins: the crystal structure of a Ru(II) dicarbonyl-lysozyme complex. J Am Chem Soc 133: 1192-1195, 2011.
    • (2011) J Am Chem Soc , vol.133 , pp. 1192-1195
    • Santos-Silva, T.1    Mukhopadhyay, A.2    Seixas, J.D.3    Gjl, B.4    Romao, C.C.5    Romao, M.J.6
  • 38
    • 79955822396 scopus 로고    scopus 로고
    • PhotoCORMs: Light-triggered release of carbon monoxide from the coordination sphere of transition metal complexes for biological applications
    • Schatzschneider U. PhotoCORMs: light-triggered release of carbon monoxide from the coordination sphere of transition metal complexes for biological applications. Inorg Chim Acta 374: 19-23, 2011.
    • (2011) Inorg Chim Acta , vol.374 , pp. 19-23
    • Schatzschneider, U.1
  • 39
    • 77953298121 scopus 로고    scopus 로고
    • Compensations for diminished terminal oxidase activity in Escherichia coli cytochrome bd-II mediated respiration and glutamate metabolism
    • Shepherd M, Sanguinetti G, Cook GM, and Poole RK. Compensations for diminished terminal oxidase activity in Escherichia coli cytochrome bd-II mediated respiration and glutamate metabolism. J Biol Chem 285: 18464-18472, 2010.
    • (2010) J Biol Chem , vol.285 , pp. 18464-18472
    • Shepherd, M.1    Sanguinetti, G.2    Cook, G.M.3    Poole, R.K.4
  • 40
    • 84867333665 scopus 로고    scopus 로고
    • A role for reactive oxygen species in the antibacterial properties of carbon monoxide-releasing molecules
    • Tavares AFN, Nobre LS, and Saraiva LM. A role for reactive oxygen species in the antibacterial properties of carbon monoxide-releasing molecules. FEMS Microbiol Lett 336: 1-10, 2012.
    • (2012) FEMS Microbiol Lett , vol.336 , pp. 1-10
    • Tavares, A.F.N.1    Nobre, L.S.2    Saraiva, L.M.3
  • 41
    • 79960671726 scopus 로고    scopus 로고
    • Reactive oxygen species mediate bactericidal killing elicited by carbon monoxide-releasing molecules
    • Tavares AFN, Teixeira M, Romao CC, Seixas JD, Nobre LS, and Saraiva LM. Reactive oxygen species mediate bactericidal killing elicited by carbon monoxide-releasing molecules. J Biol Chem 286: 26708-26717, 2011.
    • (2011) J Biol Chem , vol.286 , pp. 26708-26717
    • Tavares, A.F.N.1    Teixeira, M.2    Romao, C.C.3    Seixas, J.D.4    Nobre, L.S.5    Saraiva, L.M.6
  • 42
    • 0020356013 scopus 로고
    • Superoxide dismutase-inhibitable reduction of cytochrome-c by the alloxan radical: Implications for alloxan cytotoxicity
    • Winterbourn CC. Superoxide dismutase-inhibitable reduction of cytochrome-c by the alloxan radical: implications for alloxan cytotoxicity. Biochem J 207: 609-612, 1982.
    • (1982) Biochem J , vol.207 , pp. 609-612
    • Winterbourn, C.C.1
  • 44
    • 0037776519 scopus 로고
    • Transduction and recombination study of linkage relationships among the genes controlling tryptophan synthesis in Escherichia coli
    • Yanofsky C, and Lennox ES. Transduction and recombination study of linkage relationships among the genes controlling tryptophan synthesis in Escherichia coli. Virology 8: 425-447, 1959.
    • (1959) Virology , vol.8 , pp. 425-447
    • Yanofsky, C.1    Lennox, E.S.2


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