메뉴 건너뛰기




Volumn 386, Issue 1, 2009, Pages 246-260

HisE11 and HisF8 Provide Bis-histidyl Heme Hexa-coordination in the Globin Domain of Geobacter sulfurreducens Globin-coupled Sensor

Author keywords

3D structure; Geobacter sulfurreducens; globin coupled sensor; hexacoordination; ligand binding properties

Indexed keywords

GLOBIN; HEME; HISE11 PROTEIN; HISF8 PROTEIN; MEMBRANE PROTEIN; UNCLASSIFIED DRUG;

EID: 58549113376     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.12.023     Document Type: Article
Times cited : (46)

References (53)
  • 1
    • 10444268892 scopus 로고    scopus 로고
    • Heme-based sensors: defining characteristics, recent developments, and regulatory hypotheses
    • Gilles-Gonzalez M.A., and Gonzalez G. Heme-based sensors: defining characteristics, recent developments, and regulatory hypotheses. J. Inorg. Biochem. 99 (2005) 1-22
    • (2005) J. Inorg. Biochem. , vol.99 , pp. 1-22
    • Gilles-Gonzalez, M.A.1    Gonzalez, G.2
  • 2
    • 0141761124 scopus 로고    scopus 로고
    • The diversity of globin-coupled sensors
    • Freitas T.A., Hou S., and Alam M. The diversity of globin-coupled sensors. FEBS Lett. 552 (2003) 99-104
    • (2003) FEBS Lett. , vol.552 , pp. 99-104
    • Freitas, T.A.1    Hou, S.2    Alam, M.3
  • 4
    • 0042334880 scopus 로고    scopus 로고
    • Structure of the oxygen sensor in Bacillus subtilis: signal transduction of chemotaxis by control of symmetry
    • Zhang W., and Phillips Jr. G.N. Structure of the oxygen sensor in Bacillus subtilis: signal transduction of chemotaxis by control of symmetry. Structure (Camb.) 11 (2003) 1097-1110
    • (2003) Structure (Camb.) , vol.11 , pp. 1097-1110
    • Zhang, W.1    Phillips Jr., G.N.2
  • 7
    • 38949170616 scopus 로고    scopus 로고
    • Archaeal protoglobin structure indicates new ligand diffusion paths and modulation of haem-reactivity
    • Nardini M., Pesce A., Thijs L., Saito J.A., Dewilde S., Alam M., et al. Archaeal protoglobin structure indicates new ligand diffusion paths and modulation of haem-reactivity. EMBO Rep. 9 (2008) 157-163
    • (2008) EMBO Rep. , vol.9 , pp. 157-163
    • Nardini, M.1    Pesce, A.2    Thijs, L.3    Saito, J.A.4    Dewilde, S.5    Alam, M.6
  • 8
    • 2142763872 scopus 로고    scopus 로고
    • Cleaning up with genomics: applying molecular biology to bioremediation
    • Lovley D.R. Cleaning up with genomics: applying molecular biology to bioremediation. Nature Rev. Microbiol. 1 (2003) 35-44
    • (2003) Nature Rev. Microbiol. , vol.1 , pp. 35-44
    • Lovley, D.R.1
  • 9
    • 0346243803 scopus 로고    scopus 로고
    • Genome of Geobacter sulfurreducens: metal reduction in subsurface environments
    • Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W., Heidelberg J.F., et al. Genome of Geobacter sulfurreducens: metal reduction in subsurface environments. Science 302 (2003) 1967-1969
    • (2003) Science , vol.302 , pp. 1967-1969
    • Methe, B.A.1    Nelson, K.E.2    Eisen, J.A.3    Paulsen, I.T.4    Nelson, W.5    Heidelberg, J.F.6
  • 10
    • 3843070019 scopus 로고    scopus 로고
    • Geobacter sulfurreducens can grow with oxygen as a terminal electron acceptor
    • Lin W.C., Coppi M.V., and Lovley D.R. Geobacter sulfurreducens can grow with oxygen as a terminal electron acceptor. Appl. Environ. Microbiol. 70 (2004) 2525-2528
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 2525-2528
    • Lin, W.C.1    Coppi, M.V.2    Lovley, D.R.3
  • 12
    • 0027459747 scopus 로고
    • Structural alignment of globins, phycocyanins and colicin A
    • Holm L., and Sander C. Structural alignment of globins, phycocyanins and colicin A. FEBS Lett. 315 (1993) 301-306
    • (1993) FEBS Lett. , vol.315 , pp. 301-306
    • Holm, L.1    Sander, C.2
  • 13
    • 17144408393 scopus 로고    scopus 로고
    • Structure-function relationships in the growing hexa-coordinate hemoglobin sub-family
    • de Sanctis D., Pesce A., Nardini M., Bolognesi M., Bocedi A., and Ascenzi P. Structure-function relationships in the growing hexa-coordinate hemoglobin sub-family. IUBMB Life 56 (2004) 643-651
    • (2004) IUBMB Life , vol.56 , pp. 643-651
    • de Sanctis, D.1    Pesce, A.2    Nardini, M.3    Bolognesi, M.4    Bocedi, A.5    Ascenzi, P.6
  • 14
    • 33646341657 scopus 로고    scopus 로고
    • A phylogenetic and structural analysis of truncated hemoglobins
    • Vuletich D.A., and Lecomte J.T. A phylogenetic and structural analysis of truncated hemoglobins. J. Mol. Evol. 62 (2006) 196-210
    • (2006) J. Mol. Evol. , vol.62 , pp. 196-210
    • Vuletich, D.A.1    Lecomte, J.T.2
  • 15
    • 34447530237 scopus 로고    scopus 로고
    • Protein fold and structure in the truncated (2/2) globin family
    • Nardini M., Pesce A., Milani M., and Bolognesi M. Protein fold and structure in the truncated (2/2) globin family. Gene 398 (2007) 2-11
    • (2007) Gene , vol.398 , pp. 2-11
    • Nardini, M.1    Pesce, A.2    Milani, M.3    Bolognesi, M.4
  • 16
    • 0037018935 scopus 로고    scopus 로고
    • Truncated hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002: evidence for hexacoordination and covalent adduct formation in the ferric recombinant protein
    • Scott N.L., Falzone C.J., Vuletich D.A., Zhao J., Bryant D.A., and Lecomte J.T. Truncated hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002: evidence for hexacoordination and covalent adduct formation in the ferric recombinant protein. Biochemistry 41 (2002) 6902-6910
    • (2002) Biochemistry , vol.41 , pp. 6902-6910
    • Scott, N.L.1    Falzone, C.J.2    Vuletich, D.A.3    Zhao, J.4    Bryant, D.A.5    Lecomte, J.T.6
  • 17
    • 1942533441 scopus 로고    scopus 로고
    • The crystal structure of Synechocystis hemoglobin with a covalent heme linkage
    • Hoy J.A., Kundu S., Trent III J.T., Ramaswamy S., and Hargrove M.S. The crystal structure of Synechocystis hemoglobin with a covalent heme linkage. J. Biol. Chem. 279 (2004) 16535-16542
    • (2004) J. Biol. Chem. , vol.279 , pp. 16535-16542
    • Hoy, J.A.1    Kundu, S.2    Trent III, J.T.3    Ramaswamy, S.4    Hargrove, M.S.5
  • 18
    • 3843100441 scopus 로고    scopus 로고
    • Crystallographic analysis of synechocystis cyanoglobin reveals the structural changes accompanying ligand binding in a hexacoordinate hemoglobin
    • Trent III J.T., Kundu S., Hoy J.A., and Hargrove M.S. Crystallographic analysis of synechocystis cyanoglobin reveals the structural changes accompanying ligand binding in a hexacoordinate hemoglobin. J. Mol. Biol. 341 (2004) 1097-1108
    • (2004) J. Mol. Biol. , vol.341 , pp. 1097-1108
    • Trent III, J.T.1    Kundu, S.2    Hoy, J.A.3    Hargrove, M.S.4
  • 19
    • 0035914459 scopus 로고    scopus 로고
    • Biochemical characterization and ligand binding properties of neuroglobin, a novel member of the globin family
    • Dewilde S., Kiger L., Burmester T., Hankeln T., Baudin-Creuza V., Aerts T., et al. Biochemical characterization and ligand binding properties of neuroglobin, a novel member of the globin family. J. Biol. Chem. 276 (2001) 38949-38955
    • (2001) J. Biol. Chem. , vol.276 , pp. 38949-38955
    • Dewilde, S.1    Kiger, L.2    Burmester, T.3    Hankeln, T.4    Baudin-Creuza, V.5    Aerts, T.6
  • 20
    • 0033548681 scopus 로고    scopus 로고
    • Chlamydomonas chloroplast ferrous hemoglobin. Heme pocket structure and reactions with ligands
    • Couture M., Das T.K., Lee H.C., Peisach J., Rousseau D.L., Wittenberg B.A., et al. Chlamydomonas chloroplast ferrous hemoglobin. Heme pocket structure and reactions with ligands. J. Biol. Chem. 274 (1999) 6898-6910
    • (1999) J. Biol. Chem. , vol.274 , pp. 6898-6910
    • Couture, M.1    Das, T.K.2    Lee, H.C.3    Peisach, J.4    Rousseau, D.L.5    Wittenberg, B.A.6
  • 21
    • 0037134550 scopus 로고    scopus 로고
    • Resonance Raman and ligand binding studies of the oxygen-sensing signal transducer protein HemAT from Bacillus subtilis
    • Aono S., Kato T., Matsuki M., Nakajima H., Ohta T., Uchida T., and Kitagawa T. Resonance Raman and ligand binding studies of the oxygen-sensing signal transducer protein HemAT from Bacillus subtilis. J. Biol. Chem. 277 (2002) 13528-13538
    • (2002) J. Biol. Chem. , vol.277 , pp. 13528-13538
    • Aono, S.1    Kato, T.2    Matsuki, M.3    Nakajima, H.4    Ohta, T.5    Uchida, T.6    Kitagawa, T.7
  • 24
    • 0025214396 scopus 로고
    • A novel mechanism of heme-heme interaction in the homodimeric hemoglobin from Scapharca inaequivalvis as manifested upon cleavage of the proximal Fe-N epsilon bond at low pH
    • Coletta M., Boffi A., Ascenzi P., Brunori M., and Chiancone E. A novel mechanism of heme-heme interaction in the homodimeric hemoglobin from Scapharca inaequivalvis as manifested upon cleavage of the proximal Fe-N epsilon bond at low pH. J. Biol. Chem. 265 (1990) 4828-4830
    • (1990) J. Biol. Chem. , vol.265 , pp. 4828-4830
    • Coletta, M.1    Boffi, A.2    Ascenzi, P.3    Brunori, M.4    Chiancone, E.5
  • 25
    • 0018654083 scopus 로고
    • Regulation of oxygen affinity of hemoglobin: influence of structure of the globin on the heme iron
    • Perutz M.F. Regulation of oxygen affinity of hemoglobin: influence of structure of the globin on the heme iron. Annu. Rev. Biochem. 48 (1979) 327-386
    • (1979) Annu. Rev. Biochem. , vol.48 , pp. 327-386
    • Perutz, M.F.1
  • 26
    • 0030467166 scopus 로고    scopus 로고
    • Assignment of protoheme resonance Raman spectrum by heme labeling in myoglobin
    • Hu S.Z., Smith K., and Spiro T.G. Assignment of protoheme resonance Raman spectrum by heme labeling in myoglobin. J. Am. Chem. Soc. 118 (1996) 12638-12646
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 12638-12646
    • Hu, S.Z.1    Smith, K.2    Spiro, T.G.3
  • 27
    • 0034633996 scopus 로고    scopus 로고
    • Resonance Raman studies indicate a unique heme active site in prostaglandin H synthase
    • Lou B.S., Snyder J.K., Marshall P., Wang J.S., Wu G., Kulmacz R.J., et al. Resonance Raman studies indicate a unique heme active site in prostaglandin H synthase. Biochemistry 39 (2000) 12424-12434
    • (2000) Biochemistry , vol.39 , pp. 12424-12434
    • Lou, B.S.1    Snyder, J.K.2    Marshall, P.3    Wang, J.S.4    Wu, G.5    Kulmacz, R.J.6
  • 28
    • 0032538024 scopus 로고    scopus 로고
    • Unusual rocking freedom of the heme in the hydrogen sulfide-binding hemoglobin from Lucina pectinata
    • Cerda-Colon J.F., Silfa E., and Lopez-Garriga J. Unusual rocking freedom of the heme in the hydrogen sulfide-binding hemoglobin from Lucina pectinata. J. Am. Chem. Soc. 120 (1998) 9312-9317
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 9312-9317
    • Cerda-Colon, J.F.1    Silfa, E.2    Lopez-Garriga, J.3
  • 29
    • 20444374458 scopus 로고    scopus 로고
    • CO-dependent activity-controlling mechanism of heme-containing CO-sensor protein, neuronal PAS domain protein 2
    • Uchida T., Sato E., Sato A., Sagami I., Shimizu T., and Kitagawa T. CO-dependent activity-controlling mechanism of heme-containing CO-sensor protein, neuronal PAS domain protein 2. J. Biol. Chem. 280 (2005) 21358-21368
    • (2005) J. Biol. Chem. , vol.280 , pp. 21358-21368
    • Uchida, T.1    Sato, E.2    Sato, A.3    Sagami, I.4    Shimizu, T.5    Kitagawa, T.6
  • 30
    • 0001314340 scopus 로고    scopus 로고
    • Heme-protein interactions in cytochrome c peroxidase revealed by site-directed mutagenesis and resonance Raman spectra of isotopically labeled hemes
    • Smulevich G., Hu S.Z., Rodgers K.R., Goodin D.B., Smith K.M., and Spiro T.G. Heme-protein interactions in cytochrome c peroxidase revealed by site-directed mutagenesis and resonance Raman spectra of isotopically labeled hemes. Biospectroscopy 2 (1996) 365-376
    • (1996) Biospectroscopy , vol.2 , pp. 365-376
    • Smulevich, G.1    Hu, S.Z.2    Rodgers, K.R.3    Goodin, D.B.4    Smith, K.M.5    Spiro, T.G.6
  • 31
    • 3142615826 scopus 로고    scopus 로고
    • Heme structures of five variants of hemoglobin M probed by resonance Raman spectroscopy
    • Jin Y., Nagai M., Nagai Y., Nagatomo S., and Kitagawa T. Heme structures of five variants of hemoglobin M probed by resonance Raman spectroscopy. Biochemistry 43 (2004) 8517-8527
    • (2004) Biochemistry , vol.43 , pp. 8517-8527
    • Jin, Y.1    Nagai, M.2    Nagai, Y.3    Nagatomo, S.4    Kitagawa, T.5
  • 32
    • 33646824008 scopus 로고    scopus 로고
    • The nerve hemoglobin of the bivalve mollusc Spisula solidissima: molecular cloning, ligand binding studies, and phylogenetic analysis
    • Dewilde S., Ebner B., Vinck E., Gilany K., Hankeln T., Burmester T., et al. The nerve hemoglobin of the bivalve mollusc Spisula solidissima: molecular cloning, ligand binding studies, and phylogenetic analysis. J. Biol. Chem. 281 (2006) 5364-5372
    • (2006) J. Biol. Chem. , vol.281 , pp. 5364-5372
    • Dewilde, S.1    Ebner, B.2    Vinck, E.3    Gilany, K.4    Hankeln, T.5    Burmester, T.6
  • 33
    • 10444269414 scopus 로고    scopus 로고
    • CO as a vibrational probe of heme protein active sites
    • Spiro T.G., and Wasbotten I.H. CO as a vibrational probe of heme protein active sites. J. Inorg. Biochem. 99 (2005) 34-44
    • (2005) J. Inorg. Biochem. , vol.99 , pp. 34-44
    • Spiro, T.G.1    Wasbotten, I.H.2
  • 34
    • 17644393552 scopus 로고    scopus 로고
    • Mechanistic studies of the oxygen-mediated oxidation of nitrosylhemoglobin
    • Herold S., and Rock G. Mechanistic studies of the oxygen-mediated oxidation of nitrosylhemoglobin. Biochemistry 44 (2005) 6223-6231
    • (2005) Biochemistry , vol.44 , pp. 6223-6231
    • Herold, S.1    Rock, G.2
  • 35
    • 38049105509 scopus 로고    scopus 로고
    • Characterization of a globin-coupled oxygen sensor with a gene-regulating function
    • Thijs L., Vinck E., Bolli A., Trandafir F., Wan X., Hoogewijs D., et al. Characterization of a globin-coupled oxygen sensor with a gene-regulating function. J. Biol. Chem. 282 (2007) 37325-37340
    • (2007) J. Biol. Chem. , vol.282 , pp. 37325-37340
    • Thijs, L.1    Vinck, E.2    Bolli, A.3    Trandafir, F.4    Wan, X.5    Hoogewijs, D.6
  • 36
    • 22144452831 scopus 로고    scopus 로고
    • Biophysical and kinetic characterization of HemAT, an aerotaxis receptor from Bacillus subtilis
    • Zhang W., Olson J.S., and Phillips Jr. G.N. Biophysical and kinetic characterization of HemAT, an aerotaxis receptor from Bacillus subtilis. Biophys. J. 88 (2005) 2801-2814
    • (2005) Biophys. J. , vol.88 , pp. 2801-2814
    • Zhang, W.1    Olson, J.S.2    Phillips Jr., G.N.3
  • 38
    • 0001515662 scopus 로고
    • A kinetic model for R- and T-state haemoglobin
    • White D.K., Cannon J.B., and Traylor T.G. A kinetic model for R- and T-state haemoglobin. J. Am. Chem. Soc. 101 (1979) 2443-2454
    • (1979) J. Am. Chem. Soc. , vol.101 , pp. 2443-2454
    • White, D.K.1    Cannon, J.B.2    Traylor, T.G.3
  • 39
    • 33746072949 scopus 로고    scopus 로고
    • The proteome of dissimilatory metal-reducing microorganism Geobacter sulfurreducens under various growth conditions
    • Ding Y.H., Hixson K.K., Giometti C.S., Stanley A., Esteve-Nunez A., Khare T., et al. The proteome of dissimilatory metal-reducing microorganism Geobacter sulfurreducens under various growth conditions. Biochim. Biophys. Acta 1764 (2006) 1198-1206
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 1198-1206
    • Ding, Y.H.1    Hixson, K.K.2    Giometti, C.S.3    Stanley, A.4    Esteve-Nunez, A.5    Khare, T.6
  • 41
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50 (1994) 760-763
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 42
    • 0033081959 scopus 로고    scopus 로고
    • Discrimination of solvent from protein regions in native Fouriers as a means of evaluating heavy-atom solutions in the MIR and MAD methods
    • Terwilliger T.C., and Berendzen J. Discrimination of solvent from protein regions in native Fouriers as a means of evaluating heavy-atom solutions in the MIR and MAD methods. Acta Crystallogr. D 55 (1999) 501-505
    • (1999) Acta Crystallogr. D , vol.55 , pp. 501-505
    • Terwilliger, T.C.1    Berendzen, J.2
  • 43
    • 58549086703 scopus 로고    scopus 로고
    • Cowtan, K. (1994). Joint CCP4 and ESF-EACBM newsletter on protein crystallography. 31, 34-38.
    • Cowtan, K. (1994). Joint CCP4 and ESF-EACBM newsletter on protein crystallography. 31, 34-38.
  • 44
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis A., Morris R., and Lamzin V.S. Automated protein model building combined with iterative structure refinement. Nature Struct. Biol. 6 (1999) 458-463
    • (1999) Nature Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 45
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60 (2004) 2126-2132
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 46
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53 (1997) 240-255
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 47
  • 50
    • 28844486080 scopus 로고    scopus 로고
    • EasySpin, a comprehensive software package for spectral simulation and analysis in EPR
    • Stoll S., and Schweiger A. EasySpin, a comprehensive software package for spectral simulation and analysis in EPR. J. Magn. Reson. 178 (2006) 42-55
    • (2006) J. Magn. Reson. , vol.178 , pp. 42-55
    • Stoll, S.1    Schweiger, A.2
  • 51
    • 0015519084 scopus 로고
    • Functional properties of native and reconstituted hemoglobins from Chironomus thummi thummi
    • Amiconi G., Antonini E., Brunori M., Formaneck H., and Huber R. Functional properties of native and reconstituted hemoglobins from Chironomus thummi thummi. Eur J. Biochem. 31 (1972) 52-58
    • (1972) Eur J. Biochem. , vol.31 , pp. 52-58
    • Amiconi, G.1    Antonini, E.2    Brunori, M.3    Formaneck, H.4    Huber, R.5
  • 52
    • 0023042546 scopus 로고
    • A kinetic description of ligand binding to sperm whale myoglobin
    • Gibson Q.H., Olson J.S., McKinnie R.E., and Rohlfs R.J. A kinetic description of ligand binding to sperm whale myoglobin. J. Biol. Chem. 261 (1986) 10228-10239
    • (1986) J. Biol. Chem. , vol.261 , pp. 10228-10239
    • Gibson, Q.H.1    Olson, J.S.2    McKinnie, R.E.3    Rohlfs, R.J.4
  • 53
    • 0017112413 scopus 로고
    • Cooperativity in the dissociation of nitric oxide from hemoglobin
    • Moore E.G., and Gibson Q.H. Cooperativity in the dissociation of nitric oxide from hemoglobin. J. Biol. Chem. 251 (1976) 2788-2794
    • (1976) J. Biol. Chem. , vol.251 , pp. 2788-2794
    • Moore, E.G.1    Gibson, Q.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.