메뉴 건너뛰기




Volumn 6, Issue 11, 1999, Pages

Fix L, a haemoglobin that acts as an oxygen sensor: Signalling mechanism and structural basis of its homology with PAS domains

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA; BACTERIA (MICROORGANISMS); CETACEA; RHIZOBIUM;

EID: 0033229863     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(99)80121-5     Document Type: Short Survey
Times cited : (55)

References (29)
  • 1
    • 0001266103 scopus 로고
    • A three-dimensional model of the myoglobin molecule obtained by X-ray analysis
    • Kendrew, J.C., Bodo, G., Dintzis, H.M., Parrish, R.G., Wykoff, H. & Phillips, D.C. (1958). A three-dimensional model of the myoglobin molecule obtained by X-ray analysis. Nature 174, 946-950.
    • (1958) Nature , vol.174 , pp. 946-950
    • Kendrew, J.C.1    Bodo, G.2    Dintzis, H.M.3    Parrish, R.G.4    Wykoff, H.5    Phillips, D.C.6
  • 2
    • 0025878267 scopus 로고
    • A haemoprotein with kinase activity encoded by the oxygen sensor of Rhizobium meliloti
    • Gilles-Gonzalez, M.A., Ditta, G.S. & Helinski, D.R. (1991). A haemoprotein with kinase activity encoded by the oxygen sensor of Rhizobium meliloti. Nature 350, 170-172.
    • (1991) Nature , vol.350 , pp. 170-172
    • Gilles-Gonzalez, M.A.1    Ditta, G.S.2    Helinski, D.R.3
  • 3
    • 0024006507 scopus 로고
    • Common regulatory elements control symbiotic and microaerobic induction of nif A in Rhizobium meliloti
    • Virts, E.L., Stanfield, S.W., Helinski, D.R. & Ditta, G.S. (1988). Common regulatory elements control symbiotic and microaerobic induction of nif A in Rhizobium meliloti. Proc. Natl Acad. Sci. USA 85, 7850-7854.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 7850-7854
    • Virts, E.L.1    Stanfield, S.W.2    Helinski, D.R.3    Ditta, G.S.4
  • 4
    • 0001848362 scopus 로고
    • Symbiotic expression of Rhizobium meliloti nitrogen fixation genes is regulated by oxygen
    • (Hoch, J.A. & Silhavy, T.J., eds) American Society for Microbiology, Washington, DC.
    • Agnou, P.G. & Helinski, D.R. (1995). Symbiotic expression of Rhizobium meliloti nitrogen fixation genes is regulated by oxygen. In Two-component Signal Transduction. pp. 275-287. (Hoch, J.A. & Silhavy, T.J., eds) American Society for Microbiology, Washington, DC.
    • (1995) Two-component Signal Transduction , pp. 275-287
    • Agnou, P.G.1    Helinski, D.R.2
  • 5
    • 0027219226 scopus 로고
    • Regulation of kinase activity of heme protein Fix L from the two-component system Fix L/Fix J of Rhizobium meliloti
    • Gilles-Gonzalez, M.A. & Gonzalez, J. (1993). Regulation of kinase activity of heme protein Fix L from the two-component system Fix L/Fix J of Rhizobium meliloti. J. Biol. Chem. 268, 16293-16297.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16293-16297
    • Gilles-Gonzalez, M.A.1    Gonzalez, J.2
  • 6
    • 0028241788 scopus 로고
    • Heme-based sensors, exemplified by the kinase Fix L, are a new class of heme protein with distinctive ligand binding and autoxidation
    • Gilles-Gonzalez, M.A., Gonzalez, J., Perutz, M.F., Kiger, L., Warden, M.C. & Poyart, L. (1994). Heme-based sensors, exemplified by the kinase Fix L, are a new class of heme protein with distinctive ligand binding and autoxidation. Biochemistry 33, 8067-8073.
    • (1994) Biochemistry , vol.33 , pp. 8067-8073
    • Gilles-Gonzalez, M.A.1    Gonzalez, J.2    Perutz, M.F.3    Kiger, L.4    Warden, M.C.5    Poyart, L.6
  • 7
    • 0018654083 scopus 로고
    • Regulation of oxygen affinity of hemoglobin. Influence of the structure of the globin on the heme iron
    • Perutz, M.F. (1979). Regulation of oxygen affinity of hemoglobin. Influence of the structure of the globin on the heme iron. Annu. Rev. Biochem. 48, 327-386.
    • (1979) Annu. Rev. Biochem. , vol.48 , pp. 327-386
    • Perutz, M.F.1
  • 8
    • 0028949951 scopus 로고
    • Kinase activity of oxygen sensor Fix L depends on the spin state of the heme iron
    • Gilles-Gonzalez, M.A., Gonzalez, G. & Perutz, M.F. (1995). Kinase activity of oxygen sensor Fix L depends on the spin state of the heme iron. Biochemistry 34, 232-236.
    • (1995) Biochemistry , vol.34 , pp. 232-236
    • Gilles-Gonzalez, M.A.1    Gonzalez, G.2    Perutz, M.F.3
  • 10
    • 0017193799 scopus 로고
    • Equilibrium between six- and five-coordinated hemes in nitrosylhemoglobin: Interpretation of electron spin resonance spectra
    • Szabo, A. & Perutz, M.F. (1976). Equilibrium between six- and five-coordinated hemes in nitrosylhemoglobin: Interpretation of electron spin resonance spectra. Biochemistry 15, 4427-4428.
    • (1976) Biochemistry , vol.15 , pp. 4427-4428
    • Szabo, A.1    Perutz, M.F.2
  • 11
    • 0030265676 scopus 로고    scopus 로고
    • Nonsteric factors dominate binding of nitric oxide, azide, imidazole, cyanide, and fluoride to the rhizobial heme-based oxygen sensor Fix L
    • Winkler, W.C., et al., & Gilles-Gonzalez, M.A. (1996). Nonsteric factors dominate binding of nitric oxide, azide, imidazole, cyanide, and fluoride to the rhizobial heme-based oxygen sensor Fix L. Chem. Biol. 3, 841-850.
    • (1996) Chem. Biol. , vol.3 , pp. 841-850
    • Winkler, W.C.1    Gilles-Gonzalez, M.A.2
  • 12
    • 0024519403 scopus 로고
    • Discrimination between oxygen and carbon monoxide and inhibition of autoxidation by myogloblin. Site-directed mutagenesis of the distal histidine
    • Springer, B.A., Egebert, K.D., Sligar, S.G., Rohlfs, R.J., Mathews, A.J. & Olson, J.S. (1989). Discrimination between oxygen and carbon monoxide and inhibition of autoxidation by myogloblin. Site-directed mutagenesis of the distal histidine. J. Biol. Chem. 264, 3057-3060.
    • (1989) J. Biol. Chem. , vol.264 , pp. 3057-3060
    • Springer, B.A.1    Egebert, K.D.2    Sligar, S.G.3    Rohlfs, R.J.4    Mathews, A.J.5    Olson, J.S.6
  • 13
    • 0032837780 scopus 로고    scopus 로고
    • Synthetic models for hemoglobin and myoglobin
    • Collman, J.P. & Fu, L. (1999). Synthetic models for hemoglobin and myoglobin. Accounts Chem. Res. 32, 455-463.
    • (1999) Accounts Chem. Res. , vol.32 , pp. 455-463
    • Collman, J.P.1    Fu, L.2
  • 15
    • 0032516492 scopus 로고    scopus 로고
    • Mechanism of autoxidation of the oxygen sensor Fix L and Aplysia myoglobin: Implications for oxygen-binding heme proteins
    • Gonzales, G., Gilles-Gonzales, M.A., Rybak-Akimova, E.V., Buchalova, M. & Busch, D.H. (1998). Mechanism of autoxidation of the oxygen sensor Fix L and Aplysia myoglobin: Implications for oxygen-binding heme proteins. Biochemistry 37, 10188-10194.
    • (1998) Biochemistry , vol.37 , pp. 10188-10194
    • Gonzales, G.1    Gilles-Gonzales, M.A.2    Rybak-Akimova, E.V.3    Buchalova, M.4    Busch, D.H.5
  • 16
    • 0019995366 scopus 로고
    • Mechanism of autoxidation of hemoglobins and myoglobins. Promotion of superoxide production by protons and anions
    • Wallace, W.J., Houtchens, R.A., Maxwell, J.S. & Caughey, W.S. (1982). Mechanism of autoxidation of hemoglobins and myoglobins. Promotion of superoxide production by protons and anions. J. Biol. Chem. 257, 4966-4977
    • (1982) J. Biol. Chem. , vol.257 , pp. 4966-4977
    • Wallace, W.J.1    Houtchens, R.A.2    Maxwell, J.S.3    Caughey, W.S.4
  • 17
    • 0025344693 scopus 로고
    • Mechanisms regulating the reactions of human hemoglobin with oxygen and carbon monoxide
    • Perutz, M.F. (1990). Mechanisms regulating the reactions of human hemoglobin with oxygen and carbon monoxide. Annu. Rev. Physiol. 52, 1-25.
    • (1990) Annu. Rev. Physiol. , vol.52 , pp. 1-25
    • Perutz, M.F.1
  • 18
    • 0032990441 scopus 로고    scopus 로고
    • PAS domains: Internal sensors of oxygen, redox and light
    • Taylor, B.L. & Zhulin, I.B. (1999). PAS domains: Internal sensors of oxygen, redox and light. Microbiol. Mol. Biol. Rev. 63, 479-506.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 479-506
    • Taylor, B.L.1    Zhulin, I.B.2
  • 19
    • 0026698924 scopus 로고
    • Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides
    • Waksman, G., et al., & Kuriyan, J. (1992). Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides. Nature 358, 646-650.
    • (1992) Nature , vol.358 , pp. 646-650
    • Waksman, G.1    Kuriyan, J.2
  • 21
    • 0029110488 scopus 로고
    • 1.4 Å structure of photoreactive yellow protein, a cytosolic photoreceptor: Unusual fold, active site, and chromophore
    • Borgstahl, G.E.O., Williams, D.W.R. & Getzoff, E.D. (1995). 1.4 Å structure of photoreactive yellow protein, a cytosolic photoreceptor: Unusual fold, active site, and chromophore. Biochemistry 34, 6278-6287.
    • (1995) Biochemistry , vol.34 , pp. 6278-6287
    • Borgstahl, G.E.O.1    Williams, D.W.R.2    Getzoff, E.D.3
  • 22
    • 0032567106 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of HERG potassium channel N-terminus: A eukaryotic PAS domain
    • Morais Cabral, J.H., Lee, A., Cohen, S.L., Chait, B.T., Li, M. & Mackinnon, R. (1998). Crystal structure and functional analysis of HERG potassium channel N-terminus: A eukaryotic PAS domain. Cell 95, 649-655.
    • (1998) Cell , vol.95 , pp. 649-655
    • Morais Cabral, J.H.1    Lee, A.2    Cohen, S.L.3    Chait, B.T.4    Li, M.5    Mackinnon, R.6
  • 23
    • 85021467943 scopus 로고
    • Structure and function of haemoglobin II. Some relations between polypeptide chain configuration and amino acid sequence
    • Perutz, M.F., Kendrew, J.C. & Watson, H.C. (1965). Structure and function of haemoglobin II. Some relations between polypeptide chain configuration and amino acid sequence. J. Mol. Biol. 13, 669-678.
    • (1965) J. Mol. Biol. , vol.13 , pp. 669-678
    • Perutz, M.F.1    Kendrew, J.C.2    Watson, H.C.3
  • 24
    • 0023176681 scopus 로고
    • Determinants of globin fold. Unique features of the globin amino acid sequences
    • Bashford, D., Chothia, C. & Lesk, A.M. (1987). Determinants of globin fold. Unique features of the globin amino acid sequences. J. Mol. Biol. 196, 199-216.
    • (1987) J. Mol. Biol. , vol.196 , pp. 199-216
    • Bashford, D.1    Chothia, C.2    Lesk, A.M.3
  • 25
    • 0025753142 scopus 로고
    • Similarity of the three-dimensional structures of actin and the ATPase fragment of the 70 kDa heat shock cognate protein
    • Flaherty, K.M., McKay, D.B., Kabsch, W. & Holmes, K.C. (1991). Similarity of the three-dimensional structures of actin and the ATPase fragment of the 70 kDa heat shock cognate protein. Proc. Natl Acad. Sci. USA 88, 5041-5045.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 5041-5045
    • Flaherty, K.M.1    McKay, D.B.2    Kabsch, W.3    Holmes, K.C.4
  • 26
    • 0042706988 scopus 로고
    • What are enzyme structures telling us?
    • Perutz, M.F. (1992). What are enzyme structures telling us? Faraday Discuss. 93, 1-11.
    • (1992) Faraday Discuss. , vol.93 , pp. 1-11
    • Perutz, M.F.1
  • 27
    • 0033007795 scopus 로고    scopus 로고
    • Oxygen sensing and signalling: Impact on the regulation of physiologically important genes
    • Zhu, H. & Bunn, H.F. (1999). Oxygen sensing and signalling: Impact on the regulation of physiologically important genes. Respiration Physiol. 115, 239-248.
    • (1999) Respiration Physiol. , vol.115 , pp. 239-248
    • Zhu, H.1    Bunn, H.F.2
  • 28
    • 0025317502 scopus 로고
    • The definition of general topological equivalence in protein structures. A procedure involving comparison of properties and relationships through simulated annealing and dynamic programming
    • Sali, A. & Blundell, T.L. (1990). The definition of general topological equivalence in protein structures. A procedure involving comparison of properties and relationships through simulated annealing and dynamic programming. J. Mol. Biol. 212, 403-428.
    • (1990) J. Mol. Biol. , vol.212 , pp. 403-428
    • Sali, A.1    Blundell, T.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.