메뉴 건너뛰기




Volumn 17, Issue 9, 2012, Pages 1232-1245

Environmental heme-based sensor proteins: Implications for understanding bacterial pathogenesis

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CARBON DIOXIDE; COOA PROTEIN; DOSS PROTEIN; DOST PROTEIN; ECDOS PROTEIN; GUANYLATE CYCLASE; HEME; HEME BASED SENSOR PROTEIN; NITRIC OXIDE; OXYGEN; PROTOPORPHYRIN; RCOM PROTEIN; SENSOR OF NITRIC OXIDE; SOLUBLE GUANYLATE CYCLASE; UNCLASSIFIED DRUG;

EID: 84862760868     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2012.4613     Document Type: Review
Times cited : (28)

References (95)
  • 1
    • 78649921851 scopus 로고    scopus 로고
    • Overcoming the heme paradox: Heme toxicity and tolerance in bacterial pathogens
    • Anzaldi LL and Skaar EP. Overcoming the heme paradox: Heme toxicity and tolerance in bacterial pathogens. Infect Immun 78:4977-4989, 2010.
    • (2010) Infect Immun , vol.78 , pp. 4977-4989
    • Anzaldi, L.L.1    Skaar, E.P.2
  • 2
    • 0030597287 scopus 로고    scopus 로고
    • A novel heme protein that acts as a carbon monoxide-dependent transcriptional activator in Rhodospirillum rubrum
    • DOI 10.1006/bbrc.1996.1727
    • Aono S, Nakajima H, Saito K, and Okada M. A novel heme protein that acts as a carbon monoxide-dependent transcriptional activator in Rhodospirillum rubrum. Biochem Biophys Res Commun 228:752-756, 1996. (Pubitemid 26421450)
    • (1996) Biochemical and Biophysical Research Communications , vol.228 , Issue.3 , pp. 752-756
    • Aono, S.1    Nakajima, H.2    Saito, K.3    Okada, M.4
  • 3
    • 0032475847 scopus 로고    scopus 로고
    • Redox-controlled ligand exchange of the heme in the CO-sensing transcriptional activator CooA
    • DOI 10.1074/jbc.273.40.25757
    • Aono S, Ohkubo K, Matsuo T, and Nakajima H. Redoxcontrolled ligand exchange of the heme in the CO-sensing transcriptional activator CooA. J Biol Chem 273:25757-25764, 1998. (Pubitemid 28475801)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.40 , pp. 25757-25764
    • Aono, S.1    Ohkubo, K.2    Matsuo, T.3    Nakajima, H.4
  • 4
    • 34447509223 scopus 로고    scopus 로고
    • Mycobacterial truncated hemoglobins: From genes to functions
    • DOI 10.1016/j.gene.2007.02.043, PII S0378111907001977
    • Ascenzi P, Bolognesi M, Milani M, Guertin M, and Visca P. Mycobacterial truncated hemoglobins: From genes to functions. Gene 398:42-51, 2007. (Pubitemid 47068883)
    • (2007) Gene , vol.398 , Issue.1-2 SPEC. ISSUE , pp. 42-51
    • Ascenzi, P.1    Bolognesi, M.2    Milani, M.3    Guertin, M.4    Visca, P.5
  • 5
    • 42049097209 scopus 로고    scopus 로고
    • Iron oxidation state modulates active site structure in a heme peroxidase
    • DOI 10.1021/bi702337n
    • Badyal SK, Metcalfe CL, Basran J, Efimov I, Moody P C E, and Raven EL. Iron oxidation state modulates active site structure in a heme peroxidase. Biochemistry 47:4403-4409, 2008. (Pubitemid 351522089)
    • (2008) Biochemistry , vol.47 , Issue.15 , pp. 4403-4409
    • Badyal, S.K.1    Metcalfe, C.L.2    Basran, J.3    Efimov, I.4    Moody, P.C.E.5    Raven, E.L.6
  • 6
    • 0036270739 scopus 로고    scopus 로고
    • Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling
    • DOI 10.1046/j.1365-2958.2002.02779.x
    • Betts JC, Lukey PT, Robb LC, McAdam RA, and Duncan K. Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling. Mol Microbiol 43:717-731, 2002. (Pubitemid 34597265)
    • (2002) Molecular Microbiology , vol.43 , Issue.3 , pp. 717-731
    • Betts, J.C.1    Lukey, P.T.2    Robb, L.C.3    McAdam, R.A.4    Duncan, K.5
  • 7
    • 58149382075 scopus 로고    scopus 로고
    • Genome-based analysis of heme biosynthesis and uptake in prokaryotic systems
    • Cavallaro G, Decaria L, and Rosato A. Genome-based analysis of heme biosynthesis and uptake in prokaryotic systems. J Proteome Res 7:4946-4954, 2008.
    • (2008) J Proteome Res , vol.7 , pp. 4946-4954
    • Cavallaro, G.1    Decaria, L.2    Rosato, A.3
  • 8
    • 79958131422 scopus 로고    scopus 로고
    • Blockage of the channel to heme by the E87 side chain in the GAF domain of Mycobacterium tuberculosis DosS confers the unique sensitivity of DosS to oxygen
    • Cho HY, Cho HJ, Kim MH, and Kang BS. Blockage of the channel to heme by the E87 side chain in the GAF domain of Mycobacterium tuberculosis DosS confers the unique sensitivity of DosS to oxygen. FEBS Lett 585:1873-1878, 2011.
    • (2011) FEBS Lett , vol.585 , pp. 1873-1878
    • Cho, H.Y.1    Cho, H.J.2    Kim, M.H.3    Kang, B.S.4
  • 9
    • 67649586805 scopus 로고    scopus 로고
    • Structural insight into the heme-based redox sensing by DosS from Mycobacterium tuberculosis
    • Cho HY, Cho HJ, Kim YM, Oh JI, and Kang BS. Structural insight into the heme-based redox sensing by DosS from Mycobacterium tuberculosis. J Biol Chem 284:13057-13067, 2009.
    • (2009) J Biol Chem , vol.284 , pp. 13057-13067
    • Cho, H.Y.1    Cho, H.J.2    Kim, Y.M.3    Oh, J.I.4    Kang, B.S.5
  • 10
    • 68149175286 scopus 로고    scopus 로고
    • Truncated hemoglobins in Frankia CcI3: Effects of nitrogen source, oxygen concentration, and nitric oxide
    • Coats V C V, Schwintzer C R S C R, and Tjepkema J D T J D. Truncated hemoglobins in Frankia CcI3: Effects of nitrogen source, oxygen concentration, and nitric oxide. Can J Microbiol 55:867-873, 2009.
    • (2009) Can J Microbiol , vol.55 , pp. 867-873
    • Coats, V.C.V.1    Schwintzer, C.R.S.C.R.2    Tjepkema, J.D.T.J.D.3
  • 13
    • 57749120272 scopus 로고    scopus 로고
    • Structural chemistry involved in information detection and transmission by gas sensor heme proteins: Resonance Raman investigation
    • El-Mashtoly SF and Kitagawa T. Structural chemistry involved in information detection and transmission by gas sensor heme proteins: Resonance Raman investigation. Pure Appl Chem 80:2667-2678, 2008.
    • (2008) Pure Appl Chem , vol.80 , pp. 2667-2678
    • El-Mashtoly, S.F.1    Kitagawa, T.2
  • 14
    • 43749101877 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis Rv2540c DNA sequence encodes a bifunctional chorismate synthase
    • Ely F, Nunes J, Schroeder E, Frazzon J, Palma M, Santos D, and Basso L. The Mycobacterium tuberculosis Rv2540c DNA sequence encodes a bifunctional chorismate synthase. BMC Biochem 9:13, 2008.
    • (2008) BMC Biochem , vol.9 , pp. 13
    • Ely, F.1    Nunes, J.2    Schroeder, E.3    Frazzon, J.4    Palma, M.5    Santos, D.6    Basso, L.7
  • 15
    • 78349251639 scopus 로고    scopus 로고
    • Reductive stress in microbes: Implications for understanding Mycobacterium tuberculosis disease and persistence
    • Farhana A, Guidry L, Srivastava A, Singh A, Hondalus MK, and Steyn A J C. Reductive stress in microbes: Implications for understanding Mycobacterium tuberculosis disease and persistence. Adv Microb Physiol 57:43-117, 2010.
    • (2010) Adv Microb Physiol , vol.57 , pp. 43-117
    • Farhana, A.1    Guidry, L.2    Srivastava, A.3    Singh, A.4    Hondalus, M.K.5    Steyn, A.J.C.6
  • 16
    • 14844345178 scopus 로고    scopus 로고
    • Ligand binding properties of bacterial hemoglobins and flavohemoglobins
    • DOI 10.1021/bi047389d
    • Farras J, Rechsteiner MP, Herold S, Frey AD, and Kallio PT. Ligand binding properties of bacterial hemoglobins and flavohemoglobins. Biochemistry 44:4125-4134, 2005. (Pubitemid 40358066)
    • (2005) Biochemistry , vol.44 , Issue.10 , pp. 4125-4134
    • Farres, J.1    Rechsteiner, M.P.2    Herold, S.3    Frey, A.D.4    Kallio, P.T.5
  • 17
    • 77955460024 scopus 로고    scopus 로고
    • Reactions of NO and nitrite with heme models and proteins
    • Ford PC. Reactions of NO and nitrite with heme models and proteins. Inorg Chem 49:6226-6239, 2010.
    • (2010) Inorg Chem , vol.49 , pp. 6226-6239
    • Ford, P.C.1
  • 18
    • 0141761124 scopus 로고    scopus 로고
    • The diversity of globincoupled sensors
    • Freitas T A K, Hou S, and Alam M. The diversity of globincoupled sensors. FEBS Lett 552:99-104, 2003.
    • (2003) FEBS Lett , vol.552 , pp. 99-104
    • Freitas, T.A.K.1    Hou, S.2    Alam, M.3
  • 19
    • 0024444665 scopus 로고
    • Redox cycling of myoglobin and ascorbate: A potential protective mechanism against oxidative reperfusion injury in muscle
    • Galaris D, Cadenas E, and Hochstein P. Redox cycling of myoglobin and ascorbate: A potential protective mechanism against oxidative reperfusion injury in muscle. Arch Biochem Biophys 273:497-504, 1989. (Pubitemid 19222002)
    • (1989) Archives of Biochemistry and Biophysics , vol.273 , Issue.2 , pp. 497-504
    • Galaris, D.1    Cadenas, E.2    Hochstein, P.3
  • 20
    • 0034724887 scopus 로고    scopus 로고
    • Steady-state and transient kinetics of Escherichia coli nitricoxide dioxygenase (flavohemoglobin)
    • Gardner AM, Martin LA, Gardner PR, Dou Y, and Olson JS. Steady-state and transient kinetics of Escherichia coli nitricoxide dioxygenase (flavohemoglobin). J Biol Chem 275:12581-12589, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 12581-12589
    • Gardner, A.M.1    Martin, L.A.2    Gardner, P.R.3    Dou, Y.4    Olson, J.S.5
  • 21
    • 84865620563 scopus 로고
    • A haemoprotein with kinase activity encoded by the oxygen sensor of Rhizobium meliloti
    • Gilles-Gonzalez MA, Ditta GS, and Helinski DR. A haemoprotein with kinase activity encoded by the oxygen sensor of Rhizobium meliloti. Biochemistry 47:4403-4409, 1991.
    • (1991) Biochemistry , vol.47 , pp. 4403-4409
    • Gilles-Gonzalez, M.A.1    Ditta, G.S.2    Helinski, D.R.3
  • 22
    • 10444268892 scopus 로고    scopus 로고
    • Heme-based sensors: Defining characteristics, recent developments, and regulatory hypotheses
    • DOI 10.1016/j.jinorgbio.2004.11.006, PII S0162013404003502, Heme-Diatomic Interactions, Part 1
    • Gilles-Gonzalez MA and Gonzalez G. Heme-based sensors: Defining characteristics, recent developments, and regulatory hypotheses. J Inorg Biochem 99:1-22, 2005. (Pubitemid 39642968)
    • (2005) Journal of Inorganic Biochemistry , vol.99 , Issue.1 , pp. 1-22
    • Gilles-Gonzalez, M.-A.1    Gonzalez, G.2
  • 23
    • 0027219226 scopus 로고
    • Regulation of the kinase activity of heme protein FixL from the two- component system FixL/FixJ of Rhizobium meliloti
    • Gilles-Gonzalez MA and Gonzalez G. Regulation of the kinase activity of heme protein FixL from the two-component system FixL/FixJ of Rhizobium meliloti. J Biol Chem 268:16293-16297, 1993. (Pubitemid 23229929)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.22 , pp. 16293-16297
    • Gilles-Gonzalez, M.A.1    Gonzalez, G.2
  • 24
    • 0942298565 scopus 로고    scopus 로고
    • Signal transduction by heme-containing PAS-domain proteins
    • DOI 10.1152/japplphysiol.00941.2003
    • Gilles-Gonzalez MA and Gonzalez G. Signal transduction by heme-containing PAS-domain proteins. J Appl Physiol 96:774-783, 2004. (Pubitemid 38140186)
    • (2004) Journal of Applied Physiology , vol.96 , Issue.2 , pp. 774-783
    • Gilles-Gonzalez, M.-A.1    Gonzalez, G.2
  • 25
    • 0028949951 scopus 로고
    • Kinase activity of oxygen sensor FixL depends on the spin state of its heme iron
    • Gilles-Gonzalez MA, Gonzalez G, and Perutz MF. Kinase activity of oxygen sensor FixL depends on the spin state of its heme iron. Biochemistry 34:232-236, 1995.
    • (1995) Biochemistry , vol.34 , pp. 232-236
    • Gilles-Gonzalez, M.A.1    Gonzalez, G.2    Perutz, M.F.3
  • 26
    • 0028241788 scopus 로고
    • Heme-based sensors, exemplified by the kinase FixL, are a new class of heme protein with distinctive ligand binding and autoxidation
    • DOI 10.1021/bi00192a011
    • Gilles-Gonzalez MA, Gonzalez G, Perutz MF, Kiger L, Marden MC, and Poyart C. Heme-based sensors, exemplified by the kinase FixL, are a new class of heme protein with distinctive ligand binding and autoxidation. Biochemistry 33:8067-8073, 1994. (Pubitemid 24223828)
    • (1994) Biochemistry , vol.33 , Issue.26 , pp. 8067-8073
    • Gilles-Gonzalez, M.A.1    Gonzalez, G.2    Perutz, M.F.3
  • 27
    • 0027482489 scopus 로고
    • The reaction of ascorbic acid with different heme iron redox states of myoglobin. Antioxidant and prooxidant aspects
    • DOI 10.1016/0014-5793(93)80651-A
    • Giulivi C and Cadenas E. The reaction of ascorbic acid with different heme iron redox states of myoglobin: Antioxidant and prooxidant aspects. FEBS Lett 332:287-290, 1993. (Pubitemid 23305342)
    • (1993) FEBS Letters , vol.332 , Issue.3 , pp. 287-290
    • Giulivi, C.1    Cadenas, E.2
  • 29
    • 0001951589 scopus 로고    scopus 로고
    • Chemistry of free radicals and related 'reactive species'
    • Halliwell B and Gutteridge JMC, eds. Oxford University Press
    • Halliwell B. Chemistry of free radicals and related 'reactive species'. In: Free Radicals in Biology and Medicine, Halliwell B and Gutteridge JMC, eds. Oxford University Press, 2008, p. 30-78.
    • (2008) Free Radicals in Biology and Medicine , pp. 30-78
    • Halliwell, B.1
  • 30
    • 0030051489 scopus 로고    scopus 로고
    • Characterization of a CO-responsive transcriptional activator from Rhodospirillum rubrum
    • DOI 10.1074/jbc.271.1.120
    • He Y, Shelver D, Kerby RL, and Roberts GP. Characterization of a CO-responsive transcriptional activator from Rhodospirillum rubrum. J Biol Chem 271:120-123, 1996. (Pubitemid 26026566)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.1 , pp. 120-123
    • He, Y.1    Shelver, D.2    Kerby, R.L.3    Roberts, G.P.4
  • 31
    • 78649647277 scopus 로고    scopus 로고
    • DosS responds to a reduced electron transport system to induce the Mycobacterium tuberculosis DosR regulon
    • Honaker RW, Dhiman RK, Narayanasamy P, Crick DC, and Voskuil MI. DosS responds to a reduced electron transport system to induce the Mycobacterium tuberculosis DosR regulon. J Bacteriol 192:6447-6455, 2010.
    • (2010) J Bacteriol , vol.192 , pp. 6447-6455
    • Honaker, R.W.1    Dhiman, R.K.2    Narayanasamy, P.3    Crick, D.C.4    Voskuil, M.I.5
  • 32
    • 67651202584 scopus 로고    scopus 로고
    • Unique roles of DosT and DosS in DosR regulon induction and Mycobacterium tuberculosis dormancy
    • Honaker RW, Leistikow RL, Bartek IL, and Voskuil MI. Unique roles of DosT and DosS in DosR regulon induction and Mycobacterium tuberculosis dormancy. Infect Immun 77:3258-3263, 2009.
    • (2009) Infect Immun , vol.77 , pp. 3258-3263
    • Honaker, R.W.1    Leistikow, R.L.2    Bartek, I.L.3    Voskuil, M.I.4
  • 33
    • 0025619730 scopus 로고
    • Metabolism and energy generation in homoacetogenic clostridia
    • Hugenholtz J and Ljungdahl LG. Metabolism and energy generation in homoacetogenic clostridia. FEMS Microbiol Lett 87:383-389, 1990.
    • (1990) FEMS Microbiol Lett , vol.87 , pp. 383-389
    • Hugenholtz, J.1    Ljungdahl, L.G.2
  • 34
    • 67649631300 scopus 로고    scopus 로고
    • DevS oxy complex stability identifies this heme protein as a gas sensor in Mycobacterium tuberculosis dormancy
    • Ioanoviciu A, Meharenna YT, Poulos TL, and Ortiz de Montellano PR. DevS oxy complex stability identifies this heme protein as a gas sensor in Mycobacterium tuberculosis dormancy. Biochemistry 48:5839-5848, 2009.
    • (2009) Biochemistry , vol.48 , pp. 5839-5848
    • Ioanoviciu, A.1    Meharenna, Y.T.2    Poulos, T.L.3    Ortiz De Montellano, P.R.4
  • 35
    • 34147117736 scopus 로고    scopus 로고
    • DevS, a heme-containing two-component oxygen sensor of Mycobacterium tuberculosis
    • DOI 10.1021/bi602422p
    • Ioanoviciu A, Yukl ET, Moenne-Loccoz P, and De Montellano P R O. DevS, a heme-containing two-component oxygen sensor of Mycobacterium tuberculosis. Biochemistry 46:4250-4260, 2007. (Pubitemid 46559392)
    • (2007) Biochemistry , vol.46 , Issue.14 , pp. 4250-4260
    • Ioanovichi, A.1    Yukl, E.T.2    Moenne-Loccoz, P.3    Ortiz De Montellano, P.R.4
  • 36
    • 50149095403 scopus 로고    scopus 로고
    • Arg97 at the heme-distal side of the isolated hemebound PAS domain of a heme-based oxygen sensor from Escherichia coli (Ec DOS) plays critical roles in autoxidation and binding to gases, particularly O2
    • Ishitsuka Y, Araki Y, Tanaka A, Igarashi J, Ito O, and Shimizu T. Arg97 at the heme-distal side of the isolated hemebound PAS domain of a heme-based oxygen sensor from Escherichia coli (Ec DOS) plays critical roles in autoxidation and binding to gases, particularly O2. Biochemistry 47:8874-8884, 2008.
    • (2008) Biochemistry , vol.47 , pp. 8874-8884
    • Ishitsuka, Y.1    Araki, Y.2    Tanaka, A.3    Igarashi, J.4    Ito, O.5    Shimizu, T.6
  • 37
    • 9144261238 scopus 로고    scopus 로고
    • Ancient conserved domains shared by animal soluble guanylyl cyclases and bacterial signaling proteins
    • Iyer L, Anantharaman V, and Aravind L. Ancient conserved domains shared by animal soluble guanylyl cyclases and bacterial signaling proteins. BMC Genom 4:5, 2003.
    • (2003) BMC Genom , vol.4 , pp. 5
    • Iyer, L.1    Anantharaman, V.2    Aravind, L.3
  • 38
    • 0037260847 scopus 로고    scopus 로고
    • Mechanisms of ligand discrimination by heme proteins
    • DOI 10.1007/s00775-002-0405-8
    • Jain R and Chan MK. Mechanisms of ligand discrimination by heme proteins. J Biol Inorg Chem 8:1-11, 2003. (Pubitemid 36168887)
    • (2003) Journal of Biological Inorganic Chemistry , vol.8 , Issue.1-2 , pp. 1-11
    • Jain, R.1    Chan, M.K.2
  • 39
    • 3543102591 scopus 로고    scopus 로고
    • Spectroscopic characterization of the soluble guanylate cyclase-like heme domains from Vibrio cholerae and Thermoanaerobacter tengcongensis
    • DOI 10.1021/bi049374l
    • Karow DS, Pan D, Tran R, Pellicena P, Presley A, Mathies RA, and Marletta MA. Spectroscopic characterization of the soluble guanylate cyclase-like heme domains from Vibrio cholerae and Thermoanaerobacter tengcongensis. Biochemistry 43:10203-10211, 2004. (Pubitemid 39030911)
    • (2004) Biochemistry , vol.43 , Issue.31 , pp. 10203-10211
    • Karow, D.S.1    Pan, D.2    Tran, R.3    Pellicena, P.4    Presley, A.5    Mathies, R.A.6    Marletta, M.A.7
  • 40
    • 0028925554 scopus 로고
    • Carbon monoxidedependent growth of Rhodospirillum rubrum
    • Kerby RL, Ludden PW, and Roberts GP. Carbon monoxidedependent growth of Rhodospirillum rubrum. J Bacteriol 177:2241-2244, 1995.
    • (1995) J Bacteriol , vol.177 , pp. 2241-2244
    • Kerby, R.L.1    Ludden, P.W.2    Roberts, G.P.3
  • 41
    • 42549120776 scopus 로고    scopus 로고
    • RcoM: A new single-component transcriptional regulator of CO metabolism in bacteria
    • DOI 10.1128/JB.00033-08
    • Kerby RL, Youn H, and Roberts GP. RcoM: A new singlecomponent transcriptional regulator of CO metabolism in bacteria. J Bacteriol 190:3336-3343, 2008. (Pubitemid 351581429)
    • (2008) Journal of Bacteriology , vol.190 , Issue.9 , pp. 3336-3343
    • Kerby, R.L.1    Youn, H.2    Roberts, G.P.3
  • 42
    • 77957327437 scopus 로고    scopus 로고
    • Different roles of DosS and DosT in the hypoxic adaptation of Mycobacteria
    • Kim MJ, Park KJ, Ko IJ, Kim YM, and Oh JI. Different roles of DosS and DosT in the hypoxic adaptation of Mycobacteria. J Bacteriol 192:4868-4875, 2010.
    • (2010) J Bacteriol , vol.192 , pp. 4868-4875
    • Kim, M.J.1    Park, K.J.2    Ko, I.J.3    Kim, Y.M.4    Oh, J.I.5
  • 43
    • 0027328295 scopus 로고
    • Identification and cloning of genes differentially expressed in the virulent strain of Mycobacterium tuberculosis
    • Kinger AK and Tyagi JS. Identification and cloning of genes differentially expressed in the virulent strain of Mycobacterium tuberculosis. Gene 131:113-117, 1993.
    • (1993) Gene , vol.131 , pp. 113-117
    • Kinger, A.K.1    Tyagi, J.S.2
  • 47
  • 50
    • 73649124591 scopus 로고    scopus 로고
    • Heme ligand binding properties and intradimer interactions in the full-length sensor protein DOS from Escherichia coli and its isolated heme domain
    • Lechauve C, Bouzhir-Sima L, Yamashita T, Marden MC, Vos MH, Liebl U, and Kiger L. Heme ligand binding properties and intradimer interactions in the full-length sensor protein DOS from Escherichia coli and its isolated heme domain. J Biol Chem 284:36146-36159, 2009.
    • (2009) J Biol Chem , vol.284 , pp. 36146-36159
    • Lechauve, C.1    Bouzhir-Sima, L.2    Yamashita, T.3    Marden, M.C.4    Vos, M.H.5    Liebl, U.6    Kiger, L.7
  • 51
    • 77949356979 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis DosR regulon assists in metabolic homeostasis and enables rapid recovery from nonrespiring dormancy
    • Leistikow RL, Morton RA, Bartek IL, Frimpong I, Wagner K, and Voskuil MI. The Mycobacterium tuberculosis DosR regulon assists in metabolic homeostasis and enables rapid recovery from nonrespiring dormancy. J Bacteriol 192:1662-1670, 2010.
    • (2010) J Bacteriol , vol.192 , pp. 1662-1670
    • Leistikow, R.L.1    Morton, R.A.2    Bartek, I.L.3    Frimpong, I.4    Wagner, K.5    Voskuil, M.I.6
  • 52
    • 50249155967 scopus 로고    scopus 로고
    • The transcription regulator RcoM-2 from Burkholderia xenovorans is a cysteine-ligated hemoprotein that undergoes a redox-mediated ligand switch
    • Marvin KA, Kerby RL, Youn H, Roberts GP, and Burstyn JN. The transcription regulator RcoM-2 from Burkholderia xenovorans is a cysteine-ligated hemoprotein that undergoes a redox-mediated ligand switch. Biochemistry 47:9016-9028, 2008.
    • (2008) Biochemistry , vol.47 , pp. 9016-9028
    • Marvin, K.A.1    Kerby, R.L.2    Youn, H.3    Roberts, G.P.4    Burstyn, J.N.5
  • 53
    • 33845338724 scopus 로고    scopus 로고
    • Projections of global mortality and burden of disease from 2002 to 2030
    • Mathers CD and Loncar D. Projections of global mortality and burden of disease from 2002 to 2030. PLoS medicine 3:e442, 2006.
    • (2006) PLoS Medicine , vol.3
    • Mathers, C.D.1    Loncar, D.2
  • 54
    • 0005312054 scopus 로고
    • The pathogenesis of minimal pulmonary tuberculosis: A study of 1, 225 necropsies in cases of sudden and unexpected death
    • Medlar EM. The pathogenesis of minimal pulmonary tuberculosis: A study of 1, 225 necropsies in cases of sudden and unexpected death. Am Rev Tuberculosis 58:583, 1948.
    • (1948) Am Rev Tuberculosis , vol.58 , pp. 583
    • Medlar, E.M.1
  • 55
    • 77957358837 scopus 로고    scopus 로고
    • The PpaA/AerR regulators of photosynthesis gene expression from anoxygenic phototrophic proteobacteria contain hemebinding SCHIC domains
    • Moskvin OV, Gilles-Gonzalez MA, and Gomelsky M. The PpaA/AerR regulators of photosynthesis gene expression from anoxygenic phototrophic proteobacteria contain hemebinding SCHIC domains. J Bacteriol 192:5253-5256, 2010.
    • (2010) J Bacteriol , vol.192 , pp. 5253-5256
    • Moskvin, O.V.1    Gilles-Gonzalez, M.A.2    Gomelsky, M.3
  • 56
    • 9444240366 scopus 로고    scopus 로고
    • Femtomolar sensitivity of a NO sensor from Clostridium botulinum
    • DOI 10.1126/science.1103596
    • Nioche P, Berka V, Vipond J, Minton N, Tsai AL, and Raman CS. Femtomolar sensitivity of a NO sensor from Clostridium botulinum. Science 306:1550-1553, 2004. (Pubitemid 39564949)
    • (2004) Science , vol.306 , Issue.5701 , pp. 1550-1553
    • Nioche, P.1    Berka, V.2    Vipond, J.3    Minton, N.4    Tsai, A.-L.5    Raman, C.S.6
  • 57
    • 0041827138 scopus 로고    scopus 로고
    • The effects of reactive nitrogen intermediates on gene expression in Mycobacterium tuberculosis
    • DOI 10.1046/j.1462-5822.2003.00307.x
    • Ohno H, Zhu G, Mohan VP, Chu D, Kohno S, Jacobs WR, and Chan J. The effects of reactive nitrogen intermediates on gene expression in Mycobacterium tuberculosis. Cell Microbiol 5:637-648, 2003. (Pubitemid 37080674)
    • (2003) Cellular Microbiology , vol.5 , Issue.9 , pp. 637-648
    • Ohno, H.1    Zhu, G.2    Mohan, V.P.3    Chu, D.4    Kohno, S.5    Jacobs Jr., W.R.6    Chan, J.7
  • 59
    • 64549129166 scopus 로고    scopus 로고
    • Iron-based redox switches in biology
    • Outten FW and Theil EC. Iron-based redox switches in biology. Antioxid Redox Signal 11:1029-1046, 2009.
    • (2009) Antioxid Redox Signal , vol.11 , pp. 1029-1046
    • Outten, F.W.1    Theil, E.C.2
  • 60
    • 0036260085 scopus 로고    scopus 로고
    • Structure-function relationships in heme-proteins
    • DOI 10.1089/104454902753759690
    • Paoli M, Marles-Wright J, and Smith A. Structure-function relationships in heme-proteins. DNA Cell Biol 21:271-280, 2002. (Pubitemid 34594541)
    • (2002) DNA and Cell Biology , vol.21 , Issue.4 , pp. 271-280
    • Paoli, M.1    Marles-Wright, J.2    Smith, A.3
  • 61
    • 0036049852 scopus 로고    scopus 로고
    • Nitric oxide scavenging and detoxification by the Mycobacterium tuberculosis haemoglobin, HbN in Escherichia coli
    • DOI 10.1046/j.1365-2958.2002.03095.x
    • Pathania R, Navani NK, Gardner AM, Gardner PR, and Dikshit KL. Nitric oxide scavenging and detoxification by the Mycobacterium tuberculosis haemoglobin, HbN in Escherichia coli. Mol Microbiol 45:1303-1314, 2002. (Pubitemid 35015354)
    • (2002) Molecular Microbiology , vol.45 , Issue.5 , pp. 1303-1314
    • Pathania, R.1    Navani, N.K.2    Gardner, A.M.3    Gardner, P.R.4    Dikshit, K.L.5
  • 62
    • 44949234852 scopus 로고    scopus 로고
    • Responses of Mycobacterium tuberculosis hemoglobin promoters to in vitro and in vivo growth conditions
    • DOI 10.1128/AEM.02663-07
    • Pawaria S, Lama A, Raje M, and Dikshit KL. Responses of Mycobacterium tuberculosis hemoglobin promoters to in vitro and in vivo growth conditions. Appl Environ Microbiol 74:3512-3522, 2008. (Pubitemid 351812806)
    • (2008) Applied and Environmental Microbiology , vol.74 , Issue.11 , pp. 3512-3522
    • Pawaria, S.1    Lama, A.2    Raje, M.3    Dikshit, K.L.4
  • 63
    • 0034681189 scopus 로고    scopus 로고
    • Electronic absorption, EPR, and resonance raman spectroscopy of CooA, a CO-sensing transcription activator from R. rubrum, reveals a five-coordinate NO-heme
    • DOI 10.1021/bi991378g
    • Reynolds MF, Parks RB, Burstyn JN, Shelver D, Thorsteinsson MV, Kerby RL, Roberts GP, Vogel KM, and Spiro TG. Electronic absorption, EPR, and resonance Raman spectroscopy of CooA, a CO-sensing transcription activator from R. rubrum, reveals a five-coordinate NO-heme. Biochemistry 39:388-396, 2000. (Pubitemid 30056474)
    • (2000) Biochemistry , vol.39 , Issue.2 , pp. 388-396
    • Reynolds, M.F.1    Parks, R.B.2    Burstyn, J.N.3    Shelver, D.4    Thorsteinsson, M.V.5    Kerby, R.L.6    Roberts, G.P.7    Vogel, K.M.8    Spiro, T.G.9
  • 64
    • 0027428005 scopus 로고
    • Oxygen-regulated in vitro transcription of Rhizobium meliloti nifA and fixK genes
    • Reyrat JM, David M, Blonski C, Boistard P, and Batut J. Oxygen-regulated in vitro transcription of Rhizobium meliloti nifA and fixK genes. J Bacteriol 175:6867-6872, 1993. (Pubitemid 23322436)
    • (1993) Journal of Bacteriology , vol.175 , Issue.21 , pp. 6867-6872
    • Reyrat, J.-M.1    David, M.2    Blonski, C.3    Boistard, P.4    Batut, J.5
  • 65
    • 0033120934 scopus 로고    scopus 로고
    • Heme-based sensors in biological systems
    • DOI 10.1016/S1367-5931(99)80028-3
    • Rodgers KR. Heme-based sensors in biological systems. Curr Opinion Chem Biol 3:158-167, 1999. (Pubitemid 29145782)
    • (1999) Current Opinion in Chemical Biology , vol.3 , Issue.2 , pp. 158-167
    • Rodgers, K.R.1
  • 66
    • 35848943478 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis Invasion of Macrophages: Linking Bacterial Gene Expression to Environmental Cues
    • DOI 10.1016/j.chom.2007.09.006, PII S1931312807002211
    • Rohde KH, Abramovitch RB, and Russell DG. Mycobacterium tuberculosis invasion of macrophages: Linking bacterial gene expression to environmental cues. Cell Host Microbe 2:352-364, 2007. (Pubitemid 350056395)
    • (2007) Cell Host and Microbe , vol.2 , Issue.5 , pp. 352-364
    • Rohde, K.H.1    Abramovitch, R.B.2    Russell, D.G.3
  • 67
    • 69449098185 scopus 로고    scopus 로고
    • Heme oxygenase-1/carbon monoxide: From metabolism to molecular therapy
    • Ryter SW and Choi AM. Heme oxygenase-1/carbon monoxide: From metabolism to molecular therapy. Am J Resp Cell Mol Biol 41:251-260, 2009.
    • (2009) Am J Resp Cell Mol Biol , vol.41 , pp. 251-260
    • Ryter, S.W.1    Choi, A.M.2
  • 68
    • 1342292544 scopus 로고    scopus 로고
    • DevR-DevS is a bona fide two-component system of Mycobacterium tuberculosis that is hypoxia-responsive in the absence of the DNA-binding domain of DevR
    • Saini DK, Malhotra V, Dey D, Pant N, Das TK, and Tyagi JS. DevR-DevS is a bona fide two-component system of Mycobacterium tuberculosis that is hypoxia-responsive in the absence of the DNA-binding domain of DevR. Microbiology 150:865-875, 2004. (Pubitemid 38519307)
    • (2004) Microbiology , vol.150 , Issue.4 , pp. 865-875
    • Saini, D.K.1    Malhotra, V.2    Dey, D.3    Pant, N.4    Das, T.K.5    Tyagi, J.S.6
  • 69
    • 84856935399 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis WhiB3: A novel iron-sulfur cluster protein that regulates redox homeostasis and virulence
    • Saini V, Farhana A, and Steyn A J C. Mycobacterium tuberculosis WhiB3: A novel iron-sulfur cluster protein that regulates redox homeostasis and virulence. Antioxid Redox Signal 16:687-697, 2011.
    • (2011) Antioxid Redox Signal , vol.16 , pp. 687-697
    • Saini, V.1    Farhana, A.2    Steyn, A.J.C.3
  • 70
  • 72
    • 33344477903 scopus 로고    scopus 로고
    • Structure-function relationships of Ec DOS, a hemeregulated phosphodiesterase from Escherichia coli
    • Sasakura Y, Yoshimura-Suzuki T, Kurokawa H, and Shimizu T. Structure-function relationships of Ec DOS, a hemeregulated phosphodiesterase from Escherichia coli. Acc Chem Res 39:37-43, 2006.
    • (2006) Acc Chem Res , vol.39 , pp. 37-43
    • Sasakura, Y.1    Yoshimura-Suzuki, T.2    Kurokawa, H.3    Shimizu, T.4
  • 73
    • 84055190273 scopus 로고    scopus 로고
    • Structure and dynamics of Mycobacterium tuberculosis truncated hemoglobin N: Insights from NMR spectroscopy and molecular dynamics simulations
    • Savard PY, Daigle R, Morin S, Sebilo A, Meindre F, Lague P, Guertin M, and Gagne SM. Structure and dynamics of Mycobacterium tuberculosis truncated hemoglobin N: Insights from NMR spectroscopy and molecular dynamics simulations. Biochemistry 50:11121-11130, 2011.
    • (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    Guertin, M.7    Gagne, S.M.8
  • 76
    • 0033514973 scopus 로고    scopus 로고
    • Identification of two important heme site residues (cysteine 75 and histidine 77) in CooA, the CO-sensing transcription factor of Rhodospirillum rubrum
    • Shelver D, Thorsteinsson MV, Kerby RL, Chung SY, Roberts GP, Reynolds MF, Parks RB, and Burstyn JN. Identification of two important heme site residues (cysteine 75 and histidine 77) in CooA, the CO-sensing transcription factor of Rhodospirillum rubrum. Biochemistry 38:2669-2678, 1999.
    • (1999) Biochemistry , vol.38 , pp. 2669-2678
    • Shelver, D.1    Thorsteinsson, M.V.2    Kerby, R.L.3    Chung, S.Y.4    Roberts, G.P.5    Reynolds, M.F.6    Parks, R.B.7    Burstyn, J.N.8
  • 78
    • 34547568747 scopus 로고    scopus 로고
    • DosT and DevS are oxygen-switched kinases in Mycobacterium tuberculosis
    • DOI 10.1110/ps.072897707
    • Sousa E H S, Tuckerman JR, Gonzalez G, and Gilles-Gonzalez MA. DosT and DevS are oxygen-switched kinases in Mycobacterium tuberculosis. Protein Sci 16:1708-1719, 2007. (Pubitemid 47195697)
    • (2007) Protein Science , vol.16 , Issue.8 , pp. 1708-1719
    • Sousa, E.H.S.1    Tuckerman, J.R.2    Gonzalez, G.3    Gilles-Gonzalez, M.-A.4
  • 79
    • 0028228808 scopus 로고
    • Soluble guanylate cyclase from bovine lung: Activation with nitric oxide and carbon monoxide and spectral characterization of the ferrous and ferric states
    • DOI 10.1021/bi00184a036
    • Stone JR and Marletta MA. Soluble guanylate cyclase from bovine lung: Activation with nitric oxide and carbon monoxide and spectral characterization of the ferrous and ferric states. Biochemistry 33:5636-5640, 1994. (Pubitemid 24163003)
    • (1994) Biochemistry , vol.33 , Issue.18 , pp. 5636-5640
    • Stone, J.R.1    Marletta, M.A.2
  • 80
    • 34547137430 scopus 로고    scopus 로고
    • 95, in locking catalysis of the phosphodiesterase from Escherichia coli (Ec DOS) toward cyclic diGMP
    • DOI 10.1074/jbc.M701920200
    • Tanaka A, Takahashi H, and Shimizu T. Critical role of the heme axial ligand, Met95, in locking catalysis of the phosphodiesterase from Escherichia coli (Ec DOS) toward cyclic diGMP. J Biol Chem 282:21301-21307, 2007. (Pubitemid 47099927)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.29 , pp. 21301-21307
    • Tanaka, A.1    Takahashi, H.2    Shimizu, T.3
  • 81
    • 77956277547 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis transcriptional adaptation, growth arrest and dormancy phenotype development is triggered by vitamin C
    • Taneja NK, Dhingra S, Mittal A, Naresh M, and Tyagi JS. Mycobacterium tuberculosis transcriptional adaptation, growth arrest and dormancy phenotype development is triggered by vitamin C. PloS One 5:e10860, 2010.
    • (2010) PloS One , vol.5
    • Taneja, N.K.1    Dhingra, S.2    Mittal, A.3    Naresh, M.4    Tyagi, J.S.5
  • 83
    • 84856816307 scopus 로고    scopus 로고
    • A sliding-scale rule for selectivity between NO, CO and O2 by heme protein sensors
    • Tsai AL, Berka V, Martin E, and Olson JS. A sliding-scale rule for selectivity between NO, CO and O2 by heme protein sensors. Biochemistry 51:172-186, 2011.
    • (2011) Biochemistry , vol.51 , pp. 172-186
    • Tsai, A.L.1    Berka, V.2    Martin, E.3    Olson, J.S.4
  • 84
    • 0035804935 scopus 로고    scopus 로고
    • Complexation precedes phosphorylation for two-component regulatory system FixL/FixJ of Sinorhizobium meliloti
    • DOI 10.1006/jmbi.2001.4591
    • Tuckerman JR, Gonzalez G, and Gilles-Gonzalez MA. Complexation precedes phosphorylation for two-component regulatory system FixL/FixJ of Sinorhizobium meliloti. J Mol Biol 308:449-455, 2001. (Pubitemid 33027611)
    • (2001) Journal of Molecular Biology , vol.308 , Issue.3 , pp. 449-455
    • Tuckerman, J.R.1    Gonzalez, G.2    Gilles-Gonzalez, M.-A.3
  • 86
    • 24344498616 scopus 로고    scopus 로고
    • Mechanism for transduction of the ligand-binding signal in heme-based gas sensory proteins revealed by resonance Raman spectroscopy
    • DOI 10.1021/ar030267d
    • Uchida T and Kitagawa T. Mechanism for transduction of the ligand-binding signal in heme-based gas sensory proteins revealed by resonance Raman spectroscopy. Acc Chem Res 38:662-670, 2005. (Pubitemid 41260520)
    • (2005) Accounts of Chemical Research , vol.38 , Issue.8 , pp. 662-670
    • Uchida, T.1    Kitagawa, T.2
  • 87
    • 84859645414 scopus 로고    scopus 로고
    • The response of Mycobacterium tuberculosis to reactive oxygen and nitrogen species
    • Voskuil MI, Bartek IL, Visconti K, and Schoolnik GK. The response of Mycobacterium tuberculosis to reactive oxygen and nitrogen species. Front Microbiol 2:105, 2011.
    • (2011) Front Microbiol , vol.2 , pp. 105
    • Voskuil, M.I.1    Bartek, I.L.2    Visconti, K.3    Schoolnik, G.K.4
  • 88
    • 77949362600 scopus 로고    scopus 로고
    • Oxygen, nitic oxide and carbon Monoxide signalling
    • T Parish and A Brown, eds. Norfolk, UK: Caister Academic Press
    • Voskuil MI, Honaker, R. W and Steyn A J C. Oxygen, nitic oxide and carbon Monoxide signalling. In: Mycobacterium Genomics and Molecualar Biology, T Parish and A Brown, eds. Norfolk, UK: Caister Academic Press, 2009, p. 119-147.
    • (2009) Mycobacterium Genomics and Molecualar Biology , pp. 119-147
    • Voskuil, M.I.1    Honaker, R.W.2    Steyn, A.J.C.3
  • 90
    • 3042838120 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis gene expression during adaptation to stationary phase and low-oxygen dormancy
    • DOI 10.1016/j.tube.2004.02.003, PII S147297920400023X
    • Voskuil MI, Visconti KC, and Schoolnik GK. Mycobacterium tuberculosis gene expression during adaptation to stationary phase and low-oxygen dormancy. Tuberculosis 84:218-227, 2004. (Pubitemid 38857854)
    • (2004) Tuberculosis , vol.84 , Issue.3-4 , pp. 218-227
    • Voskuil, M.I.1    Visconti, K.C.2    Schoolnik, G.K.3
  • 92
    • 34249826339 scopus 로고    scopus 로고
    • Heme and virulence: How bacterial pathogens regulate, transport and utilize heme
    • DOI 10.1039/b604193k
    • Wilks A and Burkhard KA. Heme and virulence: How bacterial pathogens regulate, transport and utilize heme. Natural Prod Rep 24:511-522, 2007. (Pubitemid 46848712)
    • (2007) Natural Product Reports , vol.24 , Issue.3 , pp. 511-522
    • Wilks, A.1    Burkhard, K.A.2
  • 93
    • 25144498358 scopus 로고    scopus 로고
    • Ec, a heme-regulated phosphodiesterase, plays an important role in the regulation of the cyclic AMP level in Escherichia coli
    • DOI 10.1128/JB.187.19.6678-6682.2005
    • Yoshimura-Suzuki T, Sagami I, Yokota N, Kurokawa H, and Shimizu T. DOSEc, a heme-regulated phosphodiesterase, plays an important role in the regulation of the cyclic AMP level in Escherichia coli. J Bacteriol 187:6678-6682, 2005. (Pubitemid 41356240)
    • (2005) Journal of Bacteriology , vol.187 , Issue.19 , pp. 6678-6682
    • Yoshimura-Suzuki, T.1    Sagami, I.2    Yokota, N.3    Kurokawa, H.4    Shimizu, T.5
  • 94
    • 34548228384 scopus 로고    scopus 로고
    • Interdomain interactions within the two-component heme-based sensor DevS from Mycobacterium tuberculosis
    • DOI 10.1021/bi7008695
    • Yukl ET, Ioanoviciu A, De Montellano P R O, and Moenne-Loccoz P. Interdomain interactions within the two-component heme-based sensor DevS from Mycobacterium tuberculosis. Biochemistry 46:9728-9736, 2007. (Pubitemid 47328579)
    • (2007) Biochemistry , vol.46 , Issue.34 , pp. 9728-9736
    • Yukl, E.T.1    Ioanoviciu, A.2    Ortiz De Montellano, P.R.3    Moenne-Loccoz, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.