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Volumn 3, Issue 2, 1999, Pages 152-157

Fe-S proteins in sensing and regulatory functions

Author keywords

[No Author keywords available]

Indexed keywords

ACONITATE HYDRATASE; AMIDOPHOSPHORIBOSYLTRANSFERASE; ENDONUCLEASE; FERROCHELATASE; IRON; IRON REGULATORY FACTOR; IRON SULFUR PROTEIN; NITRIC OXIDE; NITROGENASE; OXYGEN; REGULATOR PROTEIN;

EID: 0033120863     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1367-5931(99)80027-1     Document Type: Article
Times cited : (181)

References (59)
  • 1
    • 0030868605 scopus 로고    scopus 로고
    • Iron-sulfur clusters: Nature's modular, multipurpose structures
    • Beinert H, Holm RH, Münck E: Iron-sulfur clusters: Nature's modular, multipurpose structures. Science 1997, 277:653-659. This paper and [2••] represent the most recent concise surreys of the Fe-S field, with emphasis on new insights concerning chemical, physical and biological aspects.
    • (1997) Science , vol.277 , pp. 653-659
    • Beinert, H.1    Holm, R.H.2    Münck, E.3
  • 2
    • 0032043449 scopus 로고    scopus 로고
    • Iron-sulfur proteins: New roles for old clusters
    • Johnson MK: Iron-sulfur proteins: New roles for old clusters. Curr Opin Chem Biol 1998, 2:173-181. See annotation [1••].
    • (1998) Curr Opin Chem Biol , vol.2 , pp. 173-181
    • Johnson, M.K.1
  • 3
    • 0000968111 scopus 로고
    • Iron-sulfur proteins
    • Edited by King RB. Chichester: John Wiley & Sons
    • Johnson MK: Iron-sulfur proteins. In Encyclopedia of Inorganic Chemistry. Edited by King RB. Chichester: John Wiley & Sons; 1994:1896-1913.
    • (1994) Encyclopedia of Inorganic Chemistry , pp. 1896-1913
    • Johnson, M.K.1
  • 5
    • 0032457906 scopus 로고    scopus 로고
    • Oxygen sensing by the global regulator, FNR: The role of the iron-sulfur cluster
    • Kiley PJ, Beinert H: Oxygen sensing by the global regulator, FNR: The role of the iron-sulfur cluster. FEMS Microbiol Rev 1999, 22:341-352. This work summarizes the present status of knowledge concerning the function of Fe-S clusters in FNR of E. coli.
    • (1999) FEMS Microbiol Rev , vol.22 , pp. 341-352
    • Kiley, P.J.1    Beinert, H.2
  • 6
    • 0000989147 scopus 로고    scopus 로고
    • Aconitase as iron-sulfur protein, enzyme, and iron-regulatory protein
    • Beinert H, Kennedy MC, Stout DC: Aconitase as iron-sulfur protein, enzyme, and iron-regulatory protein. Chem Rev 1996, 96:2335-2373.
    • (1996) Chem Rev , vol.96 , pp. 2335-2373
    • Beinert, H.1    Kennedy, M.C.2    Stout, D.C.3
  • 7
    • 0029758487 scopus 로고    scopus 로고
    • Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress
    • Hentze MW, Kühn LC: Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress. Proc Natl Acad Sci USA 1996, 93:8175-8182.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8175-8182
    • Hentze, M.W.1    Kühn, L.C.2
  • 8
    • 0027452550 scopus 로고
    • Regulating the fate of mRNA: The control of cellular iron metabolism
    • Klausner RD, Rouault TA, Harford JB: Regulating the fate of mRNA: The control of cellular iron metabolism. Cell 1993, 72:19-28.
    • (1993) Cell , vol.72 , pp. 19-28
    • Klausner, R.D.1    Rouault, T.A.2    Harford, J.B.3
  • 9
    • 0024498908 scopus 로고
    • Evidence that the iron-sulfur cluster of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase determines stability of the enzyme to degradation in vivo
    • Grandoni JA, Switzer RL, Makaroff CA, Zalkin H: Evidence that the iron-sulfur cluster of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase determines stability of the enzyme to degradation in vivo. J Biol Chem 1989, 264:6058-6064.
    • (1989) J Biol Chem , vol.264 , pp. 6058-6064
    • Grandoni, J.A.1    Switzer, R.L.2    Makaroff, C.A.3    Zalkin, H.4
  • 11
    • 0029119097 scopus 로고
    • Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure
    • Thayer MM, Ahern H, Xing D, Cunningham RP, Tainer JA: Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure. EMBO J 1995, 14:4108-4120.
    • (1995) EMBO J , vol.14 , pp. 4108-4120
    • Thayer, M.M.1    Ahern, H.2    Xing, D.3    Cunningham, R.P.4    Tainer, J.A.5
  • 12
    • 0030912902 scopus 로고    scopus 로고
    • Redox signal transduction via iron-sulfur clusters in the SoxR transcription activator
    • Hidalgo E, Ding H, Demple B: Redox signal transduction via iron-sulfur clusters in the SoxR transcription activator. Trends Biochem Sci 1997, 22:207-210. This contains a concise presentation and discussion of knowledge of the SoxR/SoxS system up to early 1997.
    • (1997) Trends Biochem Sci , vol.22 , pp. 207-210
    • Hidalgo, E.1    Ding, H.2    Demple, B.3
  • 13
    • 0029790760 scopus 로고    scopus 로고
    • SoxR, a [2Fe-2S] transcription factor, is active only in its oxidized form
    • Gaudu P, Weiss B: SoxR, a [2Fe-2S] transcription factor, is active only in its oxidized form. Proc Natl Acad Sci USA 1996, 93:10094-10098.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 10094-10098
    • Gaudu, P.1    Weiss, B.2
  • 15
    • 0030738589 scopus 로고    scopus 로고
    • Alternative respiratory pathways of Escherichia coli: Energetics and transcriptional regulation in response to electron acceptors
    • Unden G, Bongaerts J: Alternative respiratory pathways of Escherichia coli: Energetics and transcriptional regulation in response to electron acceptors. BBA - Bioenergetics 1997, 1320:217-234.
    • (1997) BBA - Bioenergetics , vol.1320 , pp. 217-234
    • Unden, G.1    Bongaerts, J.2
  • 16
    • 0027451092 scopus 로고
    • The activity of the Escherichia coli transcription factor FNR is regulated by a change in oligomeric state
    • Lazazzera BA, Bates DM, Kiley PJ: The activity of the Escherichia coli transcription factor FNR is regulated by a change in oligomeric state. Genes Dev 1993, 7:1993-2005.
    • (1993) Genes Dev , vol.7 , pp. 1993-2005
    • Lazazzera, B.A.1    Bates, D.M.2    Kiley, P.J.3
  • 17
    • 0030029817 scopus 로고    scopus 로고
    • DNA binding and dimerization of the Fe-S containing FNR protein from Escherichia coli are regulated by oxygen
    • Lazazzera BA, Beinert H, Khoroshilova N, Kennedy MC, Kiley PJ: DNA binding and dimerization of the Fe-S containing FNR protein from Escherichia coli are regulated by oxygen. J Biol Chem 1996, 271:2762-2768.
    • (1996) J Biol Chem , vol.271 , pp. 2762-2768
    • Lazazzera, B.A.1    Beinert, H.2    Khoroshilova, N.3    Kennedy, M.C.4    Kiley, P.J.5
  • 19
    • 0032505869 scopus 로고    scopus 로고
    • Mössbauer spectroscopy as a tool for the study of activation/inactivation of the transcription regulator FNR in whole cells of Escherichia coli
    • Popescu C, Bates D, Münck E, Beinert H: Mössbauer spectroscopy as a tool for the study of activation/inactivation of the transcription regulator FNR in whole cells of Escherichia coli. Proc Natl Acad Sci USA 1998, 95:13431-13435.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 13431-13435
    • Popescu, C.1    Bates, D.2    Münck, E.3    Beinert, H.4
  • 20
    • 0032557666 scopus 로고    scopus 로고
    • Assembly of iron-sulfur clusters: Identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii
    • Zheng L, Cash VL, Flint DH, Dean DR: Assembly of iron-sulfur clusters: Identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii. J Biol Chem 1998, 273:13264-13272.
    • (1998) J Biol Chem , vol.273 , pp. 13264-13272
    • Zheng, L.1    Cash, V.L.2    Flint, D.H.3    Dean, D.R.4
  • 21
    • 0028960504 scopus 로고
    • Association of a polynuclear iron-sulfur center with a mutant FNR protein enhances DNA binding
    • Khoroshilova N, Beinert H, Kiley PJ: Association of a polynuclear iron-sulfur center with a mutant FNR protein enhances DNA binding. Proc Natl Acad Sci USA 1995, 92:2499-2503.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 2499-2503
    • Khoroshilova, N.1    Beinert, H.2    Kiley, P.J.3
  • 22
    • 0029797082 scopus 로고    scopus 로고
    • Reconstitution of the [4Fe-4S] cluster in FNR and demonstration of the aerobic-anaerobic switch in vitro
    • Green J, Bennett B, Jordan P, Ralph E, Thomson A, Guest J: Reconstitution of the [4Fe-4S] cluster in FNR and demonstration of the aerobic-anaerobic switch in vitro. Biochem J 1996, 316:887-892.
    • (1996) Biochem J , vol.316 , pp. 887-892
    • Green, J.1    Bennett, B.2    Jordan, P.3    Ralph, E.4    Thomson, A.5    Guest, J.6
  • 23
    • 0031037665 scopus 로고    scopus 로고
    • FnrP and NNR of Paracoccus denitrificans are both members of the FNR family of transcriptional activators but have distinct roles in respiratory adaptation in response to oxygen limitation
    • Van Spanning RJ, De Boer APN, Reijnders WNM, Westerhoff HV, Stouthamer AH, Van Der Oost J: FnrP and NNR of Paracoccus denitrificans are both members of the FNR family of transcriptional activators but have distinct roles in respiratory adaptation in response to oxygen limitation. Mol Microbiol 1997, 23:893-907. This contains an excellent survey and discussion of the FNR protein family of transcriptional activators.
    • (1997) Mol Microbiol , vol.23 , pp. 893-907
    • Van Spanning, R.J.1    De Boer, A.P.N.2    Reijnders, W.N.M.3    Westerhoff, H.V.4    Stouthamer, A.H.5    Van Der Oost, J.6
  • 24
    • 0027081042 scopus 로고
    • Purification and characterization of cytosolic aconitase from beef liver and its relationship to the iron-responsive element binding protein
    • Kennedy MC, Mende-Mueller L, Blondin GA, Beinert H: Purification and characterization of cytosolic aconitase from beef liver and its relationship to the iron-responsive element binding protein. Proc Natl Acad Sci USA 1992, 89:11730-11734.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 11730-11734
    • Kennedy, M.C.1    Mende-Mueller, L.2    Blondin, G.A.3    Beinert, H.4
  • 25
    • 0027050315 scopus 로고
    • Cellular regulation of the iron-responsive element binding protein: Disassembly of the cubane iron-sulfur cluster results in high-affinity RNA binding
    • Haile DJ, Rouault TA, Harford JB, Kennedy MC, Blondin GA, Beinert H, Klausner RD: Cellular regulation of the iron-responsive element binding protein: Disassembly of the cubane iron-sulfur cluster results in high-affinity RNA binding. Proc Natl Acad Sci USA 1992, 89:11735-11739.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 11735-11739
    • Haile, D.J.1    Rouault, T.A.2    Harford, J.B.3    Kennedy, M.C.4    Blondin, G.A.5    Beinert, H.6    Klausner, R.D.7
  • 26
    • 0029034338 scopus 로고
    • Characterization and expression of iron regulatory protein 2 (IRP2)
    • Guo B, Brown FM, Phillips JD, Yu Y, Leibold EA: Characterization and expression of iron regulatory protein 2 (IRP2). J Biol Chem 1995, 270:16529-16535.
    • (1995) J Biol Chem , vol.270 , pp. 16529-16535
    • Guo, B.1    Brown, F.M.2    Phillips, J.D.3    Yu, Y.4    Leibold, E.A.5
  • 27
    • 0028788316 scopus 로고
    • Requirements for iron-regulated degradation of the RNA binding protein, iron regulatory protein 2
    • Iwai K, Klausner RD, Rouault TA: Requirements for iron-regulated degradation of the RNA binding protein, iron regulatory protein 2. EMBO J 1995, 14:5350-5357.
    • (1995) EMBO J , vol.14 , pp. 5350-5357
    • Iwai, K.1    Klausner, R.D.2    Rouault, T.A.3
  • 28
    • 0031758919 scopus 로고    scopus 로고
    • Drosophila ferritin mRNA: Alternative RNA splicing regulates the presence of the iron-responsive element
    • Lind MI, Ekengren S, Melefors Ö, Söderhäll K: Drosophila ferritin mRNA: Alternative RNA splicing regulates the presence of the iron-responsive element. FEBS Lett 1998, 436:476-482.
    • (1998) FEBS Lett , vol.436 , pp. 476-482
    • Lind, M.I.1    Ekengren, S.2    Melefors, Ö.3    Söderhäll, K.4
  • 30
    • 0026045587 scopus 로고
    • Superoxide sensitivity of the Escherichia coli aconitase
    • Gardner PR, Fridovich I: Superoxide sensitivity of the Escherichia coli aconitase. J Biol Chem 1991, 266:19328-19333.
    • (1991) J Biol Chem , vol.266 , pp. 19328-19333
    • Gardner, P.R.1    Fridovich, I.2
  • 31
    • 0027491617 scopus 로고
    • The inactivation of Fe-S cluster containing hydro-lyases by superoxide
    • Flint D, Tuminello J, Emptage M: The inactivation of Fe-S cluster containing hydro-lyases by superoxide. J Biol Chem 1993, 268:22369-22376.
    • (1993) J Biol Chem , vol.268 , pp. 22369-22376
    • Flint, D.1    Tuminello, J.2    Emptage, M.3
  • 32
    • 0028276577 scopus 로고
    • The bifunctional iron-responsive element binding protein/cytosolic aconitase: The role of active-site residues in ligand binding and regulation
    • Philpott CC, Klausner RD, Rouault TA: The bifunctional iron-responsive element binding protein/cytosolic aconitase: The role of active-site residues in ligand binding and regulation. Proc Natl Acad Sci USA 1994, 91:7321-7325.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 7321-7325
    • Philpott, C.C.1    Klausner, R.D.2    Rouault, T.A.3
  • 33
    • 0027301897 scopus 로고
    • Biosynthesis of nitric oxide activates iron regulatory factor in macrophages
    • Drapier J-C, Hirling H, Wietzerbin J, Kaldy P, Kühn LC: Biosynthesis of nitric oxide activates iron regulatory factor in macrophages. EMBO J 1993, 12:3643-3649.
    • (1993) EMBO J , vol.12 , pp. 3643-3649
    • Drapier, J.-C.1    Hirling, H.2    Wietzerbin, J.3    Kaldy, P.4    Kühn, L.C.5
  • 34
    • 0032245425 scopus 로고    scopus 로고
    • Targeting of a human iron-sulfur cluster assembly enzyme, nifS, to different subcellular compartments is regulated through alternative AUG utilization
    • Land T, Rouault TA: Targeting of a human iron-sulfur cluster assembly enzyme, nifS, to different subcellular compartments is regulated through alternative AUG utilization. Mol Cell 1998, 2:807-815.
    • (1998) Mol Cell , vol.2 , pp. 807-815
    • Land, T.1    Rouault, T.A.2
  • 35
    • 0031002851 scopus 로고    scopus 로고
    • The iron-sulfur cluster of iron regulatory protein 1 modulates the accessibility of RNA binding and phosphorylation sites
    • Schalinske KL, Anderson SA, Tuazon PT, Chen OS, Kennedy MC, Eisenstein RS: The iron-sulfur cluster of iron regulatory protein 1 modulates the accessibility of RNA binding and phosphorylation sites. Biochemistry 1997, 36:3950-3958.
    • (1997) Biochemistry , vol.36 , pp. 3950-3958
    • Schalinske, K.L.1    Anderson, S.A.2    Tuazon, P.T.3    Chen, O.S.4    Kennedy, M.C.5    Eisenstein, R.S.6
  • 36
    • 0032167632 scopus 로고    scopus 로고
    • Activation of iron regulatory protein-1 by oxidative stress in vitro
    • Pantopoulos K, Hentze MW: Activation of iron regulatory protein-1 by oxidative stress in vitro. Proc Natl Acad Sci USA 1998, 95:10559-10563.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 10559-10563
    • Pantopoulos, K.1    Hentze, M.W.2
  • 37
    • 0002573398 scopus 로고    scopus 로고
    • The iron responsive element (IRE), the iron regulatory protein (IRP), and the cytosolic aconitase; postranscriptional regulation of mammalian iron metabolism
    • Edited by Walden W, Silver S. New York: Chapman and Hall
    • Eisentstein RS, Kennedy MC, Beinert HB: The iron responsive element (IRE), the iron regulatory protein (IRP), and the cytosolic aconitase; postranscriptional regulation of mammalian iron metabolism. In Metal Ions in Gene Regulation. Edited by Walden W, Silver S. New York: Chapman and Hall; 1998:157-216. This is an extensive survey and discussion of the subject.
    • (1998) Metal Ions in Gene Regulation , pp. 157-216
    • Eisentstein, R.S.1    Kennedy, M.C.2    Beinert, H.B.3
  • 38
    • 0031807487 scopus 로고    scopus 로고
    • The rpfA gene of Xanthomonas campestris pathovar campestris, which is involved in the regulation of pathogenicity factor production, encodes an aconitase
    • Wilson TJG, Bertrand N, Tang J-L, Feng J-X, Pan M-Q, Barber CE, Dow JM, Daniels MJ: The rpfA gene of Xanthomonas campestris pathovar campestris, which is involved in the regulation of pathogenicity factor production, encodes an aconitase. Mol Microbiol 1998, 28:961-970.
    • (1998) Mol Microbiol , vol.28 , pp. 961-970
    • Wilson, T.J.G.1    Bertrand, N.2    Tang, J.-L.3    Feng, J.-X.4    Pan, M.-Q.5    Barber, C.E.6    Dow, J.M.7    Daniels, M.J.8
  • 39
    • 0025301064 scopus 로고
    • MutY, an adenine glycosylase active on G-A mispairs, has homology to endonuclease III
    • Michaels ML, Pham L, Nghiem Y, Cruz C, Miller JH: MutY, an adenine glycosylase active on G-A mispairs, has homology to endonuclease III. Nucleic Acids Res 1990, 18:3841-3845.
    • (1990) Nucleic Acids Res , vol.18 , pp. 3841-3845
    • Michaels, M.L.1    Pham, L.2    Nghiem, Y.3    Cruz, C.4    Miller, J.H.5
  • 42
    • 0028929893 scopus 로고
    • Overproduction and physical characterization of SoxR, a [2Fe-2S] protein that governs an oxidative response regulon in Escherichia coli
    • Wu J, Dunham WR, Weiss B: Overproduction and physical characterization of SoxR, a [2Fe-2S] protein that governs an oxidative response regulon in Escherichia coli. J Biol Chem 1995, 270:10323-10327.
    • (1995) J Biol Chem , vol.270 , pp. 10323-10327
    • Wu, J.1    Dunham, W.R.2    Weiss, B.3
  • 43
    • 0030936964 scopus 로고    scopus 로고
    • Redox signal transduction - Mutations shifting [2FE-2S] centers of the SoxR sensor-regulator to the oxidized form
    • Hidalgo E, Ding HG, Demple B: Redox signal transduction - Mutations shifting [2FE-2S] centers of the SoxR sensor-regulator to the oxidized form. Cell 1997, 88:121-129.
    • (1997) Cell , vol.88 , pp. 121-129
    • Hidalgo, E.1    Ding, H.G.2    Demple, B.3
  • 44
    • 0028140477 scopus 로고
    • NADPH: Ferredoxin oxidoreductase acts as a paraquat diaphorase and is a member of the soxRS regulon
    • Liochev SI, Hausladen A, Beyer WFJ, Fridovich I: NADPH: Ferredoxin oxidoreductase acts as a paraquat diaphorase and is a member of the soxRS regulon. Proc Natl Acad Sci USA 1994, 91:1328-1331.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 1328-1331
    • Liochev, S.I.1    Hausladen, A.2    Beyer, W.F.J.3    Fridovich, I.4
  • 45
    • 7744224797 scopus 로고    scopus 로고
    • Structural basis of biological nitrogen fixation
    • Howard JB, Rees DC: Structural basis of biological nitrogen fixation. Chem Rev 1996, 96:2965-2982.
    • (1996) Chem Rev , vol.96 , pp. 2965-2982
    • Howard, J.B.1    Rees, D.C.2
  • 46
    • 0000703950 scopus 로고    scopus 로고
    • Mechanism of molybdenum nitrogenase
    • Burgess BK, Lowe DJ: Mechanism of molybdenum nitrogenase. Chem Rev 1996, 96:2983-3011.
    • (1996) Chem Rev , vol.96 , pp. 2983-3011
    • Burgess, B.K.1    Lowe, D.J.2
  • 47
    • 0032039641 scopus 로고    scopus 로고
    • Nitrogen cycle enzymology
    • Ferguson SJ: Nitrogen cycle enzymology. Curr Opin Chem Biol 1998, 2:182-193.
    • (1998) Curr Opin Chem Biol , vol.2 , pp. 182-193
    • Ferguson, S.J.1
  • 48
    • 15144361084 scopus 로고    scopus 로고
    • An all-ferrous state of the Fe protein of nitrogenase
    • Angove HC, Yoo SJ, Münck E: An all-ferrous state of the Fe protein of nitrogenase. J Biol Chem 1998, 273:26330-26337.
    • (1998) J Biol Chem , vol.273 , pp. 26330-26337
    • Angove, H.C.1    Yoo, S.J.2    Münck, E.3
  • 49
    • 0032479047 scopus 로고    scopus 로고
    • All-ferrous titanium (III) citrate reduced Fe protein of nitrogenase: An XAS study of electronic and metrical structure
    • Musgrave KB, Angove HC, Burgess BK, Hedman B, Hodgson KO: All-ferrous titanium (III) citrate reduced Fe protein of nitrogenase: An XAS study of electronic and metrical structure. J Am Chem Soc 1998, 120:5325-5326.
    • (1998) J Am Chem Soc , vol.120 , pp. 5325-5326
    • Musgrave, K.B.1    Angove, H.C.2    Burgess, B.K.3    Hedman, B.4    Hodgson, K.O.5
  • 50
    • 0030700674 scopus 로고    scopus 로고
    • Changes in the midpoint potentials of the nitrogenase metal centers as a result of iron protein-molybdenum-iron protein complex formation
    • Lanzilotta WN, Seefeldt LC: Changes in the midpoint potentials of the nitrogenase metal centers as a result of iron protein-molybdenum-iron protein complex formation. Biochemistry 1997, 36:12976-12983.
    • (1997) Biochemistry , vol.36 , pp. 12976-12983
    • Lanzilotta, W.N.1    Seefeldt, L.C.2
  • 51
    • 0029929865 scopus 로고    scopus 로고
    • Evidence for electron transfer from the nitrogenase iron protein to the molybdenum-iron protein without MgATP hydrolysis: Characterization of a tight protein-protein complex
    • Lanzilotta WN, Fisher K, Seefeldt LC: Evidence for electron transfer from the nitrogenase iron protein to the molybdenum-iron protein without MgATP hydrolysis: Characterization of a tight protein-protein complex. Biochemistry 1996, 35:7188-7196.
    • (1996) Biochemistry , vol.35 , pp. 7188-7196
    • Lanzilotta, W.N.1    Fisher, K.2    Seefeldt, L.C.3
  • 52
    • 0032584694 scopus 로고    scopus 로고
    • Redox properties and electron paramagnetic resonance spectroscopy of the transition state complex of Azotobacter vinelandii nitrogenase
    • Spee JH, Arendsen AF, Wassink H, Marritt SJ, Hagen WR, Haaker H: Redox properties and electron paramagnetic resonance spectroscopy of the transition state complex of Azotobacter vinelandii nitrogenase. FEBS Lett 1998, 432:55-58.
    • (1998) FEBS Lett , vol.432 , pp. 55-58
    • Spee, J.H.1    Arendsen, A.F.2    Wassink, H.3    Marritt, S.J.4    Hagen, W.R.5    Haaker, H.6
  • 53
  • 54
    • 0029999490 scopus 로고    scopus 로고
    • Functional necessity and physicochemical characteristics of the [2Fe-2S] cluster in mammalian ferrochelatase
    • Lloyd SG, Franco R, Moura JJG, Moura I, Ferreira GC, Huynh BH: Functional necessity and physicochemical characteristics of the [2Fe-2S] cluster in mammalian ferrochelatase. J Am Chem Soc 1996, 118:9892-9900.
    • (1996) J Am Chem Soc , vol.118 , pp. 9892-9900
    • Lloyd, S.G.1    Franco, R.2    Moura, J.J.G.3    Moura, I.4    Ferreira, G.C.5    Huynh, B.H.6
  • 55
    • 0029970569 scopus 로고    scopus 로고
    • Function of the [2Fe-2S] cluster in mammalian ferrochelatase: A possible role as a nitric oxide sensor
    • Sellers VM, Johnson MK, Dailey HA: Function of the [2Fe-2S] cluster in mammalian ferrochelatase: A possible role as a nitric oxide sensor. Biochemistry 1996, 35:2699-2704.
    • (1996) Biochemistry , vol.35 , pp. 2699-2704
    • Sellers, V.M.1    Johnson, M.K.2    Dailey, H.A.3
  • 56
    • 0029023937 scopus 로고
    • Nitric oxide-mediated inactivation of mammalian ferrochelatase in vivo and in vitro: Possible involvement of the iron-sulphur cluster of the enzyme
    • Furukawa T, Kohno H, Tokunaga R, Taketani S: Nitric oxide-mediated inactivation of mammalian ferrochelatase in vivo and in vitro: Possible involvement of the iron-sulphur cluster of the enzyme. Biochem J 1995, 310:533-538.
    • (1995) Biochem J , vol.310 , pp. 533-538
    • Furukawa, T.1    Kohno, H.2    Tokunaga, R.3    Taketani, S.4
  • 58
    • 0038434902 scopus 로고    scopus 로고
    • Reconstitution and characterization of the polynuclear iron-sulfur cluster in pyruvate formate-lyase-activating enzyme
    • Kulzer R, Pils T, Kappl R, Hüttermann J, Knappe J: Reconstitution and characterization of the polynuclear iron-sulfur cluster in pyruvate formate-lyase-activating enzyme. J Biol Chem 1998, 273:4897-4903.
    • (1998) J Biol Chem , vol.273 , pp. 4897-4903
    • Kulzer, R.1    Pils, T.2    Kappl, R.3    Hüttermann, J.4    Knappe, J.5


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