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Volumn 5, Issue 9, 1996, Pages 1765-1775

Crystal structure of the 2[4Fe-4S] ferredoxin from Chromatium vinosum: Evolutionary and mechanistic inferences for [3/4Fe-4S] ferredoxins

Author keywords

Chromatium vinosum; crystal structure; electron transfer; evolution; ferredoxin; hydrogen bond; iron sulfur

Indexed keywords

FERREDOXIN;

EID: 0029786946     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560050902     Document Type: Article
Times cited : (63)

References (39)
  • 1
    • 0015919836 scopus 로고
    • The structure of a bacterial ferredoxin
    • Adman ET, Sieker LC, Jensen LH. 1973. The structure of a bacterial ferredoxin. J Biol Chem 248:3987-3996.
    • (1973) J Biol Chem , vol.248 , pp. 3987-3996
    • Adman, E.T.1    Sieker, L.C.2    Jensen, L.H.3
  • 2
    • 0017072232 scopus 로고
    • Structure of Peptococcus aerogenes ferredoxin. Refinement at 2 Å resolution
    • Adman ET, Sieker LC, Jensen LH. 1976. Structure of Peptococcus aerogenes ferredoxin. Refinement at 2 Å resolution. J Biol Chem 251:3801-3806.
    • (1976) J Biol Chem , vol.251 , pp. 3801-3806
    • Adman, E.T.1    Sieker, L.C.2    Jensen, L.H.3
  • 3
    • 0014008770 scopus 로고
    • Crystalline ferredoxin from the photosynthetic bacterium Chromatium
    • Bachofen R, Arnon DI 1966. Crystalline ferredoxin from the photosynthetic bacterium Chromatium. Biochim Biophys Acta 120:259-265.
    • (1966) Biochim Biophys Acta , vol.120 , pp. 259-265
    • Bachofen, R.1    Arnon, D.I.2
  • 7
    • 0344834199 scopus 로고
    • Iron clusters in enzymes
    • Cammack R. 1992 Iron clusters in enzymes. Adv Inorg Chem 38:281-322.
    • (1992) Adv Inorg Chem , vol.38 , pp. 281-322
    • Cammack, R.1
  • 9
    • 0028103275 scopus 로고
    • Collaborative Computational Project, Number 4. The CCP4 suite. Programs for protein crystallography
    • CCP4. 1994. Collaborative Computational Project, Number 4. The CCP4 suite. Programs for protein crystallography. Acta Crystollogr D 50:760-763.
    • (1994) Acta Crystollogr D , vol.50 , pp. 760-763
  • 10
    • 0028033838 scopus 로고
    • Refined crystal structure of the 2[4Fe-4S] ferredoxin from Clostridium acidurici at 1.84 Å resolution
    • Duée ED, Fanchon E, Vicat J, Sieker LC, Meyer J, Moulis JM. 1994. Refined crystal structure of the 2[4Fe-4S] ferredoxin from Clostridium acidurici at 1.84 Å resolution. J Mol Biol 243:683-695.
    • (1994) J Mol Biol , vol.243 , pp. 683-695
    • Duée, E.D.1    Fanchon, E.2    Vicat, J.3    Sieker, L.C.4    Meyer, J.5    Moulis, J.M.6
  • 11
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh RA, Huber R. 1991 Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallogr A 47:392-400.
    • (1991) Acta Crystallogr A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 12
    • 0024828942 scopus 로고
    • Structure of [4Fe-4S] ferredoxin from Bacillus thermoproteolyticus refined at 2.3 Å resolution
    • Fukuyama K, Matsubara H, Tsukihara T, Katsube Y. 1989. Structure of [4Fe-4S] ferredoxin from Bacillus thermoproteolyticus refined at 2.3 Å resolution. J Mol Biol 210:383-398.
    • (1989) J Mol Biol , vol.210 , pp. 383-398
    • Fukuyama, K.1    Matsubara, H.2    Tsukihara, T.3    Katsube, Y.4
  • 13
    • 0023918263 scopus 로고
    • Tertiary structure of Bacillus thermoproteolyticus [4Fe-4S] ferredoxin. Evolutionary implications for bacterial ferredoxins
    • Fukuyama K, Nagahara Y, Tsukihara T, Katsube Y, Hase T, Matsubara H. 1988. Tertiary structure of Bacillus thermoproteolyticus [4Fe-4S] ferredoxin. Evolutionary implications for bacterial ferredoxins. J Mol Biol 199:183-193.
    • (1988) J Mol Biol , vol.199 , pp. 183-193
    • Fukuyama, K.1    Nagahara, Y.2    Tsukihara, T.3    Katsube, Y.4    Hase, T.5    Matsubara, H.6
  • 14
    • 0027520505 scopus 로고
    • Effect of replacing conserved proline residues on the EPR and NMR properties of Clostridium pasteurianum 2[4Fe-4S] ferredoxin
    • Gaillard J, Quinkal I, Moulis JM. 1993. Effect of replacing conserved proline residues on the EPR and NMR properties of Clostridium pasteurianum 2[4Fe-4S] ferredoxin. Biochemistry 32:9881-9887.
    • (1993) Biochemistry , vol.32 , pp. 9881-9887
    • Gaillard, J.1    Quinkal, I.2    Moulis, J.M.3
  • 15
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm L, Sander C. 1993. Protein structure comparison by alignment of distance matrices. J Mol Biol 233:123-138.
    • (1993) J Mol Biol , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 16
    • 0028936095 scopus 로고
    • NMR of Chromatium vinosum ferredoxin: Evidence for structural inequivalence and impeded electron transfer between the two [4Fe-4S] clusters
    • Huber JG, Gaillard J, Moulis JM 1995 NMR of Chromatium vinosum ferredoxin: Evidence for structural inequivalence and impeded electron transfer between the two [4Fe-4S] clusters. Biochemistry 34:194-205.
    • (1995) Biochemistry , vol.34 , pp. 194-205
    • Huber, J.G.1    Gaillard, J.2    Moulis, J.M.3
  • 17
    • 0000356656 scopus 로고
    • A graphics model building and refinement system for macromolecules
    • Jones TA. 1978. A graphics model building and refinement system for macromolecules. J Appl Crystallogr 11:268-272.
    • (1978) J Appl Crystallogr , vol.11 , pp. 268-272
    • Jones, T.A.1
  • 18
    • 0025899519 scopus 로고
    • Refined crystal structure of ferredoxin II from Desulfovibrio gigas at 1.7 Å
    • Kissinger CR, Sieker LC, Adman ET, Jensen LH. 1991. Refined crystal structure of ferredoxin II from Desulfovibrio gigas at 1.7 Å J Mol Biol 219:693-715.
    • (1991) J Mol Biol , vol.219 , pp. 693-715
    • Kissinger, C.R.1    Sieker, L.C.2    Adman, E.T.3    Jensen, L.H.4
  • 19
    • 0001720577 scopus 로고
    • A restrained-parameter thermal-factor refinement procedure
    • Konnert JH, Hendrickson WA 1980 A restrained-parameter thermal-factor refinement procedure. Acta Crystallogr A 36:344-350.
    • (1980) Acta Crystallogr A , vol.36 , pp. 344-350
    • Konnert, J.H.1    Hendrickson, W.A.2
  • 20
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 24:946-950.
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 21
    • 0000127585 scopus 로고
    • Automated refinement of protein models
    • Lamzin VS, Wilson KS 1993. Automated refinement of protein models. Acta Crystallogr D 49:129-147.
    • (1993) Acta Crystallogr D , vol.49 , pp. 129-147
    • Lamzin, V.S.1    Wilson, K.S.2
  • 22
  • 23
    • 0022004980 scopus 로고
    • Electron transfers in chemistry and biology
    • Marcus RA, Sutin N. 1985. Electron transfers in chemistry and biology. Biochim Biophys Acta 811:265-322.
    • (1985) Biochim Biophys Acta , vol.811 , pp. 265-322
    • Marcus, R.A.1    Sutin, N.2
  • 24
    • 77956772373 scopus 로고
    • Structural and functional diversity of ferredoxins and related proteins
    • Matsubara H, Saeki K. 1992. Structural and functional diversity of ferredoxins and related proteins. Adv Inorg Chem 38:223-280.
    • (1992) Adv Inorg Chem , vol.38 , pp. 223-280
    • Matsubara, H.1    Saeki, K.2
  • 25
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews BW. 1968. Solvent content of protein crystals. J Mol Biol 33:491-497.
    • (1968) J Mol Biol , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 26
    • 0030608046 scopus 로고    scopus 로고
    • Molecular cloning and expression of the gene encoding Chromatium vinosum 2[4Fe-4S] ferredoxin
    • Forthcoming
    • Moulis JM. 1996 Molecular cloning and expression of the gene encoding Chromatium vinosum 2[4Fe-4S] ferredoxin. Biochim Biophys Acta. Forthcoming.
    • (1996) Biochim Biophys Acta
    • Moulis, J.M.1
  • 27
    • 0029611001 scopus 로고
    • Probing the role of electrostatic forces in the interaction of Clostridium pasteurianum ferredoxin with its redox partners
    • Moulis JM, Davasse V. 1995. Probing the role of electrostatic forces in the interaction of Clostridium pasteurianum ferredoxin with its redox partners. Biochemistry 34:16781-16788.
    • (1995) Biochemistry , vol.34 , pp. 16781-16788
    • Moulis, J.M.1    Davasse, V.2
  • 29
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Mavaza J. 1994. AMoRe: An automated package for molecular replacement. Acta Crystallogr A 50:157-163
    • (1994) Acta Crystallogr A , vol.50 , pp. 157-163
    • Mavaza, J.1
  • 30
    • 0023480691 scopus 로고
    • Examination of protein sequence homologies: IV. Twenty seven bacterial ferredoxins
    • Otaka E, Ooi T. 1987. Examination of protein sequence homologies: IV. Twenty seven bacterial ferredoxins. J Mol Evol 26:257-267
    • (1987) J Mol Evol , vol.26 , pp. 257-267
    • Otaka, E.1    Ooi, T.2
  • 32
    • 0029044881 scopus 로고
    • Observation of holoprotein molecular ions of several ferredoxins by electrospray-ionization mass spectrometry
    • Pétillot Y, Forest E, Meyer J, Moulis JM. 1995. Observation of holoprotein molecular ions of several ferredoxins by electrospray-ionization mass spectrometry. Anal Biochem 228:56-63.
    • (1995) Anal Biochem , vol.228 , pp. 56-63
    • Pétillot, Y.1    Forest, E.2    Meyer, J.3    Moulis, J.M.4
  • 33
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases from partial structures with errors
    • Read RJ. 1986. Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr A 42:140-149.
    • (1986) Acta Crystallogr A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 34
    • 0028605623 scopus 로고
    • Crystal structure of the ferredoxin I from Desulfovibrio africanus at 2.3 Å resolution
    • Séry A, Housset D, Serre L, Bonicel J, Hatchikian C, Frey M, Roth M. 1994. Crystal structure of the ferredoxin I from Desulfovibrio africanus at 2.3 Å resolution. Biochemistry 33:15408-15417.
    • (1994) Biochemistry , vol.33 , pp. 15408-15417
    • Séry, A.1    Housset, D.2    Serre, L.3    Bonicel, J.4    Hatchikian, C.5    Frey, M.6    Roth, M.7
  • 36
    • 0024035859 scopus 로고
    • Interesting observations on the nature of protein crystals and their growth
    • Sieker LC. 1988. Interesting observations on the nature of protein crystals and their growth. J Crystal Growth 90:31-38.
    • (1988) J Crystal Growth , vol.90 , pp. 31-38
    • Sieker, L.C.1
  • 37
    • 0025079118 scopus 로고
    • Redox properties of several bacterial ferredoxins using square wave voltammetry
    • Smith ET, Feinberg BA. 1990. Redox properties of several bacterial ferredoxins using square wave voltammetry. J Biol Chem 265:14371-14376.
    • (1990) J Biol Chem , vol.265 , pp. 14371-14376
    • Smith, E.T.1    Feinberg, B.A.2
  • 38
    • 0024961696 scopus 로고
    • Refinement of the 7 Fe ferredoxin from Azotobacter vinelandii at 1.9 Å resolution
    • Stout CD. 1989. Refinement of the 7 Fe ferredoxin from Azotobacter vinelandii at 1.9 Å resolution. J Mol Biol 205:545-555.
    • (1989) J Mol Biol , vol.205 , pp. 545-555
    • Stout, C.D.1
  • 39
    • 0000984346 scopus 로고
    • Determination of absolute from relative X-ray data intensities
    • Wilson AJC. 1942 Determination of absolute from relative X-ray data intensities. Nature (Lond) 150:151-152
    • (1942) Nature (Lond) , vol.150 , pp. 151-152
    • Wilson, A.J.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.