메뉴 건너뛰기




Volumn 45, Issue 20, 2006, Pages 6363-6371

Structural and -functional studies on DHC, the diheme cytochrome c from rhodobacter Sphaeroides, and its interaction with SHP, the sphaeroides heme protein

Author keywords

[No Author keywords available]

Indexed keywords

CRYSTAL STRUCTURE; ELECTRONS; ELECTROSTATICS; GENES; OXYGEN; RATE CONSTANTS;

EID: 33646874131     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi060288q     Document Type: Article
Times cited : (17)

References (32)
  • 1
    • 0021816536 scopus 로고
    • Soluble cytochrome composition of the purple phototrophic bacterium, Rhodopseudomonas sphaeroides ATCC 17023
    • Meyer, T. E., and Cusanovich, M. A. (1985) Soluble cytochrome composition of the purple phototrophic bacterium, Rhodopseudomonas sphaeroides ATCC 17023, Biochim. Biophys. Acta 807, 308-319.
    • (1985) Biochim. Biophys. Acta , vol.807 , pp. 308-319
    • Meyer, T.E.1    Cusanovich, M.A.2
  • 2
    • 0026511245 scopus 로고
    • The FixL protein of Rhizobium meliloti can be separated into a heme-binding oxygen-sensing domain and a functional C-terminal kinase domain
    • Monson, E. K., Weinstein, M., Ditta, G. S., and Helinski, D. R. (1992) The FixL protein of Rhizobium meliloti can be separated into a heme-binding oxygen-sensing domain and a functional C-terminal kinase domain, Proc. Natl. Acad. Sci. U.S.A. 89, 4280-4284.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 4280-4284
    • Monson, E.K.1    Weinstein, M.2    Ditta, G.S.3    Helinski, D.R.4
  • 3
    • 0344066227 scopus 로고    scopus 로고
    • Biochemical and Biophysical Properties of the CO-Sensing Transcriptional Activator CooA
    • Aono, S. (2003) Biochemical and Biophysical Properties of the CO-Sensing Transcriptional Activator CooA, Acc. Chem. Res. 36, 825-831.
    • (2003) Acc. Chem. Res. , vol.36 , pp. 825-831
    • Aono, S.1
  • 4
    • 0033120934 scopus 로고    scopus 로고
    • Heme-based sensors in biological systems
    • Rodgers, K. R. (1999) Heme-based sensors in biological systems, Curr. Opin. Chem. Biol. 3, 158-167.
    • (1999) Curr. Opin. Chem. Biol. , vol.3 , pp. 158-167
    • Rodgers, K.R.1
  • 7
    • 33646874645 scopus 로고    scopus 로고
    • www.jgi.doe.gov.
  • 8
    • 0041350484 scopus 로고    scopus 로고
    • Diversity and significance of Burkholderia species occupying diverse ecological niches
    • Coenye, T., and Vandamme, P. (2003) Diversity and significance of Burkholderia species occupying diverse ecological niches, Environ. Microbiol. 5, 719-729.
    • (2003) Environ. Microbiol. , vol.5 , pp. 719-729
    • Coenye, T.1    Vandamme, P.2
  • 9
    • 0035073389 scopus 로고    scopus 로고
    • Dechloromonas agitata gen. nov., sp. nov. and Dechlorosoma suillum gen. nov., sp. nov., two novel environmentally dominant (per)chlorate-reducing bacteria and their phylogenetic position
    • Achenbach, L. A., Michaelidou, U., Bruce, R. A., Fryman, J., and Coates, J. D. (2001) Dechloromonas agitata gen. nov., sp. nov. and Dechlorosoma suillum gen. nov., sp. nov., two novel environmentally dominant (per)chlorate-reducing bacteria and their phylogenetic position, Int. J. Syst. Bacteriol. 51, 527-533.
    • (2001) Int. J. Syst. Bacteriol. , vol.51 , pp. 527-533
    • Achenbach, L.A.1    Michaelidou, U.2    Bruce, R.A.3    Fryman, J.4    Coates, J.D.5
  • 10
  • 11
    • 0032558455 scopus 로고    scopus 로고
    • The primary structures of the low-redox potential diheme cytochromes c from the phototrophic bacteria Rhodobacter sphaeroides and Rhodobacter adriaticus reveal a new structural family of c-type cytochromes
    • Vandenberghe, I., Leys, D., Demol, H., Van Driessche, G., Meyer, T. E., Cusanovich, M. A., and Van Beeumen, J. J. (1998) The primary structures of the low-redox potential diheme cytochromes c from the phototrophic bacteria Rhodobacter sphaeroides and Rhodobacter adriaticus reveal a new structural family of c-type cytochromes, Biochemistry 37, 13075-13081.
    • (1998) Biochemistry , vol.37 , pp. 13075-13081
    • Vandenberghe, I.1    Leys, D.2    Demol, H.3    Van Driessche, G.4    Meyer, T.E.5    Cusanovich, M.A.6    Van Beeumen, J.J.7
  • 12
    • 33646891168 scopus 로고    scopus 로고
    • http://bccm.belspo.be/db/lmbp_plasmid_detaus.php?NM = pMc519.
  • 13
    • 0038072139 scopus 로고    scopus 로고
    • Haem-polypeptide interactions during cytochrome c maturation
    • Thöny-Meyer, L. (2000) Haem-polypeptide interactions during cytochrome c maturation, Biochim. Biophys. Acta 1459, 316-324.
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 316-324
    • Thöny-Meyer, L.1
  • 14
    • 33646867717 scopus 로고    scopus 로고
    • Ph.D. Thesis, University of Ghent, Ghent, Belgium
    • Backers, K. (2000) Ph.D. Thesis, University of Ghent, Ghent, Belgium.
    • (2000)
    • Backers, K.1
  • 15
    • 0028297612 scopus 로고
    • Production of enzymatically active rat protein disulfide isomerase in Escherichia coli
    • De Sutter, K., Hostens, K., Vandekerckhove, J., and Fiers, W. (1994) Production of enzymatically active rat protein disulfide isomerase in Escherichia coli, Gene 141, 163-170.
    • (1994) Gene , vol.141 , pp. 163-170
    • De Sutter, K.1    Hostens, K.2    Vandekerckhove, J.3    Fiers, W.4
  • 16
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode, Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 17
    • 0028103275 scopus 로고
    • The CCP4 Suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4 (1994) The CCP4 Suite: Programs for Protein Crystallography, Acta Crystallogr. D50, 760-763.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 19
    • 0005797141 scopus 로고    scopus 로고
    • The ARP/wARP suite for automated construction and refinement of protein models
    • (Rossmann, M. G., and Arnold, E., Eds.), Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Lamzin, V. S., Perrakis, A., and Wilson, K. S. (2001) The ARP/wARP suite for automated construction and refinement of protein models, in International Tables for Crystallography. Volume F: Crystallography of biological macromolecules (Rossmann, M. G., and Arnold, E., Eds.) pp 720-722, Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (2001) International Tables for Crystallography. Volume F: Crystallography of Biological Macromolecules , pp. 720-722
    • Lamzin, V.S.1    Perrakis, A.2    Wilson, K.S.3
  • 21
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Refinement of macromolecular structures by the maximum-likelihood method, Acta Crystallogr. D53, 240-255.
    • (1997) Acta Crystallogr. , vol.D53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 22
    • 0034645779 scopus 로고    scopus 로고
    • Structures of the flavocytochrome p-cresol methylhydroxylase and its enzyme-substrate complex: Gated substrate entry and proton relays support the proposed catalytic mechanism
    • Cunane, L. M., Chen, Z. W., Shamala, N., Mathews, F. S., Cronin, C. N., and Mcintire, W. S. (2000) Structures of the flavocytochrome p-cresol methylhydroxylase and its enzyme-substrate complex: Gated substrate entry and proton relays support the proposed catalytic mechanism, J. Mol. Biol. 295, 357-374.
    • (2000) J. Mol. Biol. , vol.295 , pp. 357-374
    • Cunane, L.M.1    Chen, Z.W.2    Shamala, N.3    Mathews, F.S.4    Cronin, C.N.5    Mcintire, W.S.6
  • 23
    • 0031865006 scopus 로고    scopus 로고
    • Touring protein fold space with Dali/FSSP
    • Holm, L., and Sander, C. (1998) Touring protein fold space with Dali/FSSP, Nucleic Acids Res. 26, 316-319.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 316-319
    • Holm, L.1    Sander, C.2
  • 24
    • 21644463020 scopus 로고    scopus 로고
    • Molecular basis of intramolecular electron transfer in sulfite-oxidizing enzymes is revealed by high-resolution structure of a heterodimeric complex of the catalytic molybdopterin subunit and a c-type cytochrome subunit
    • Kappler, U., and Bailey, S. (2005) Molecular basis of intramolecular electron transfer in sulfite-oxidizing enzymes is revealed by high-resolution structure of a heterodimeric complex of the catalytic molybdopterin subunit and a c-type cytochrome subunit, J. Biol. Chem. 280, 24999-25007.
    • (2005) J. Biol. Chem. , vol.280 , pp. 24999-25007
    • Kappler, U.1    Bailey, S.2
  • 25
    • 0037117405 scopus 로고    scopus 로고
    • The 1.25 Å resolution structure of the diheme NapB subunit of soluble nitrate reductase reveals a novel cytochrome c fold with a stacked heme arrangement
    • Brige, A., Leys, D., Meyer, T. E., Cusanovich, M. A., and Van Beeumen, J. J. (2002) The 1.25 Å resolution structure of the diheme NapB subunit of soluble nitrate reductase reveals a novel cytochrome c fold with a stacked heme arrangement, Biochemistry 41, 4827-4836.
    • (2002) Biochemistry , vol.41 , pp. 4827-4836
    • Brige, A.1    Leys, D.2    Meyer, T.E.3    Cusanovich, M.A.4    Van Beeumen, J.J.5
  • 26
    • 24944572187 scopus 로고    scopus 로고
    • Structural and biochemical characterization of DHC2, a novel diheme cytochrome c from Geobacter sulfurreducens
    • Heitmann, D., and Einsle, O. (2005) Structural and biochemical characterization of DHC2, a novel diheme cytochrome c from Geobacter sulfurreducens, Biochemistry 44, 12411-12419.
    • (2005) Biochemistry , vol.44 , pp. 12411-12419
    • Heitmann, D.1    Einsle, O.2
  • 28
    • 0028241788 scopus 로고
    • Heme-based sensors, exemplified by the kinase FixL, are a new class of heme protein with distinctive ligand binding and autoxidation
    • Gilles-Gonzalez, M. A., Gonzalez, G., Perutz, M. F., Kiger, L., Marden, M. C., and Poyart, C. (1994) 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) Biochemistry , vol.33 , pp. 8067-8073
    • Gilles-Gonzalez, M.A.1    Gonzalez, G.2    Perutz, M.F.3    Kiger, L.4    Marden, M.C.5    Poyart, C.6
  • 29
    • 0034646392 scopus 로고    scopus 로고
    • Dos, a heme-binding PAS protein from Escherichia coli, is a direct oxygen sensor
    • Delgado-Nixon, V. M., Gonzalez, G., and Gilles-Gonzalez, M. A. (2000) Dos, a heme-binding PAS protein from Escherichia coli, is a direct oxygen sensor, Biochemistry 39, 2685-2691.
    • (2000) Biochemistry , vol.39 , pp. 2685-2691
    • Delgado-Nixon, V.M.1    Gonzalez, G.2    Gilles-Gonzalez, M.A.3
  • 31
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    • Esnouf, R. M. (1997) An extensively modified version of MolScript that includes greatly enhanced coloring capabilities, J. Mol. Graphics 15, 132-134.
    • (1997) J. Mol. Graphics , vol.15 , pp. 132-134
    • Esnouf, R.M.1
  • 32
    • 0028057108 scopus 로고
    • Raster3D, version 2.0. A program for photorealistic molecular graphics
    • Merritt, E. A., and Murphy, M. E. P. (1994) Raster3D, version 2.0. A program for photorealistic molecular graphics, Acta Crystallogr. D50, 869-873.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.