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Volumn 28, Issue 2, 1997, Pages 289-292

Preparation and crystallization of a cross-linked complex of bovine adrenodoxin and adrenodoxin reductase

Author keywords

Adrenodoxin adrenodoxin reductase complex; Cross linking; Crystallization; Mass spectrometry; X ray diffraction

Indexed keywords

1 (3 DIMETHYLAMINOPROPYL) 3 ETHYLCARBODIIMIDE; ADRENODOXIN; FERREDOXIN NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE REDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE;

EID: 0343052039     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199706)28:2<289::AID-PROT16>3.0.CO;2-E     Document Type: Article
Times cited : (13)

References (28)
  • 1
    • 0023645035 scopus 로고
    • The high resolution crystal structure of P450cam
    • Poulos, T.L., Finzel, B.C., Howard, A.J. The high resolution crystal structure of P450cam. J. Mol. Biol. 195:687-700, 1987.
    • (1987) J. Mol. Biol. , vol.195 , pp. 687-700
    • Poulos, T.L.1    Finzel, B.C.2    Howard, A.J.3
  • 3
    • 0028267490 scopus 로고
    • Crystal structure and refinement of cytochrome P450terp at 2.3 Å resolution
    • Hasemann, C.A., Ravichandran, K.G., Peterson, J.A., Deisenhofer, J. Crystal structure and refinement of cytochrome P450terp at 2.3 Å resolution. J. Mol. Biol. 236:1169-1185, 1994.
    • (1994) J. Mol. Biol. , vol.236 , pp. 1169-1185
    • Hasemann, C.A.1    Ravichandran, K.G.2    Peterson, J.A.3    Deisenhofer, J.4
  • 4
    • 0029586252 scopus 로고
    • Structure of cytochrome P450eryF involved in erythromycin biosynthesis
    • Cupp-Vickery, J.R., Poulos, T.L. Structure of cytochrome P450eryF involved in erythromycin biosynthesis. Nat. Struct. Biol. 2:144-153, 1995.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 144-153
    • Cupp-Vickery, J.R.1    Poulos, T.L.2
  • 6
    • 0027375730 scopus 로고
    • Crystallization of bovine adrenodoxin-reductase in a new unit cell and its crystallographic characterization
    • Kuban, R.-J., Marg, A., Ruckpaul, K. Crystallization of bovine adrenodoxin-reductase in a new unit cell and its crystallographic characterization. J. Mol. Biol. 234:245-248, 1993.
    • (1993) J. Mol. Biol. , vol.234 , pp. 245-248
    • Kuban, R.-J.1    Marg, A.2    Ruckpaul, K.3
  • 7
    • 0026795156 scopus 로고
    • Electrostatic interactions stabilizing electron transfer complexes. Disruption by "conservative mutations."
    • Coghlan, V.M., Vickery, L.E. Electrostatic interactions stabilizing electron transfer complexes. Disruption by "conservative mutations." J. Biol. Chem. 267:8932-8935, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8932-8935
    • Coghlan, V.M.1    Vickery, L.E.2
  • 8
    • 0021772804 scopus 로고
    • Selective chemical modification of a functional linked lysine in cytochrome P-450 LM2
    • Bernhardt, R., Makower, A., Jänig, G.-R., Ruckpaul, K. Selective chemical modification of a functional linked lysine in cytochrome P-450 LM2. Biochim. Biophys. Acta 785:186-190, 1984.
    • (1984) Biochim. Biophys. Acta , vol.785 , pp. 186-190
    • Bernhardt, R.1    Makower, A.2    Jänig, G.-R.3    Ruckpaul, K.4
  • 9
    • 0023695280 scopus 로고
    • Electrostatic interactions between cytochrome P-450 LM2 and NADPH-cytochrome P-450 reductase
    • Bernhardt, R., Kraft, R., Otto, A., Ruckpaul, K. Electrostatic interactions between cytochrome P-450 LM2 and NADPH-cytochrome P-450 reductase. Biomed. Biochim. Acta 47:581-592, 1988.
    • (1988) Biomed. Biochim. Acta , vol.47 , pp. 581-592
    • Bernhardt, R.1    Kraft, R.2    Otto, A.3    Ruckpaul, K.4
  • 10
    • 0025763404 scopus 로고
    • Identification of a cross-linked peptide of a covalent complex between adrenodoxin reductase and adrenodoxin
    • Hara, T., Miyata, T. Identification of a cross-linked peptide of a covalent complex between adrenodoxin reductase and adrenodoxin. J. Biochem. 110:261-266, 1991.
    • (1991) J. Biochem. , vol.110 , pp. 261-266
    • Hara, T.1    Miyata, T.2
  • 12
    • 0027284228 scopus 로고
    • Charge pair interactions stabilizing ferredoxin-ferredoxin reductase complexes. Identification by complementary site-specific mutations
    • Brandt, M.E., Vickery, L.E. Charge pair interactions stabilizing ferredoxin-ferredoxin reductase complexes. Identification by complementary site-specific mutations. J. Biol. Chem. 268:17126-17130, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17126-17130
    • Brandt, M.E.1    Vickery, L.E.2
  • 13
    • 0018291970 scopus 로고
    • Ionic effects on adrenal steroidogenic electron transport. The role of adrenodoxin as an electron shuttle
    • Lambeth, J.D., Seybert, D.W., Kamin, H. Ionic effects on adrenal steroidogenic electron transport. The role of adrenodoxin as an electron shuttle. J. Biol. Chem. 254:7255-7264, 1979.
    • (1979) J. Biol. Chem. , vol.254 , pp. 7255-7264
    • Lambeth, J.D.1    Seybert, D.W.2    Kamin, H.3
  • 15
    • 0018563695 scopus 로고
    • The formation of binary and ternary complexes of cytochrome P-450scc with adrenodoxin and adrenodoxin reductase-adrenodoxin complex
    • Kido, T., Kimura, T. The formation of binary and ternary complexes of cytochrome P-450scc with adrenodoxin and adrenodoxin reductase-adrenodoxin complex. J. Biol. Chem. 254:11806-11815, 1979.
    • (1979) J. Biol. Chem. , vol.254 , pp. 11806-11815
    • Kido, T.1    Kimura, T.2
  • 16
    • 0022434096 scopus 로고
    • Cross-linking studies of adrenocortical cytochrome P-450scc. Evidence for a covalent complex with adrenodoxin and localization of the adrenodoxin-binding domain
    • Chashchin, V.L., Turko, I.V., Akhrem, A.A., Usanov, S.A. Cross-linking studies of adrenocortical cytochrome P-450scc. Evidence for a covalent complex with adrenodoxin and localization of the adrenodoxin-binding domain. Biochim. Biophys. Acta 828:313-324, 1985.
    • (1985) Biochim. Biophys. Acta , vol.828 , pp. 313-324
    • Chashchin, V.L.1    Turko, I.V.2    Akhrem, A.A.3    Usanov, S.A.4
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage λ
    • Laemmli, U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage λ. Nature 277:680-685, 1970.
    • (1970) Nature , vol.277 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0026496878 scopus 로고
    • Expression of bovine adrenodoxin in E. coli and site directed mutagenesis of [2Fe-2S] cluster ligands
    • Uhlmann, H., Beckert, V., Schwarz, D., Bernhardt, R. Expression of bovine adrenodoxin in E. coli and site directed mutagenesis of [2Fe-2S] cluster ligands. Biochem. Biophys. Res. Commun. 288:1131-1138, 1992.
    • (1992) Biochem. Biophys. Res. Commun. , vol.288 , pp. 1131-1138
    • Uhlmann, H.1    Beckert, V.2    Schwarz, D.3    Bernhardt, R.4
  • 19
    • 0027292014 scopus 로고
    • Direct expression of adrenodoxin reductase in E. coli and the functional characterization
    • Sagara, Y., Wada, A., Takata, Y. Waterman, M.R., Sekimizu, K., Horiuchi, T. Direct expression of adrenodoxin reductase in E. coli and the functional characterization. Biol. Pharm. Bull. 16:627-630, 1993.
    • (1993) Biol. Pharm. Bull. , vol.16 , pp. 627-630
    • Sagara, Y.1    Wada, A.2    Takata, Y.3    Waterman, M.R.4    Sekimizu, K.5    Horiuchi, T.6
  • 20
    • 0019942457 scopus 로고
    • Two forms of adrenodoxin reductase from mitochondria of bovine adrenal cortex
    • Suhara, K., Nakayama, K., Takikawa, O., Katagiri, M. Two forms of adrenodoxin reductase from mitochondria of bovine adrenal cortex. Eur. J. Biochem. 125:659-664, 1982.
    • (1982) Eur. J. Biochem. , vol.125 , pp. 659-664
    • Suhara, K.1    Nakayama, K.2    Takikawa, O.3    Katagiri, M.4
  • 21
    • 0021351056 scopus 로고
    • Identification of specific carboxylate groups on adrenodoxin that are involved in the interaction with adrenodoxin reductase
    • Geren, L.M., O'Brien, P., Stonehuerner, J., Millett, F. Identification of specific carboxylate groups on adrenodoxin that are involved in the interaction with adrenodoxin reductase. J. Biol. Chem. 259:2155-2160, 1984.
    • (1984) J. Biol. Chem. , vol.259 , pp. 2155-2160
    • Geren, L.M.1    O'Brien, P.2    Stonehuerner, J.3    Millett, F.4
  • 22
    • 0000434996 scopus 로고
    • Mounting of crystals for macromolecular crystallography in a free-standing thin film
    • Teng, T.Y. Mounting of crystals for macromolecular crystallography in a free-standing thin film. J. Appl. Crystallogr. 23:387-391, 1990.
    • (1990) J. Appl. Crystallogr. , vol.23 , pp. 387-391
    • Teng, T.Y.1
  • 23
    • 0343374919 scopus 로고    scopus 로고
    • A removable arc for mounting and recovering flash-cooled crystals
    • Engel, C., Wierenga, R., Tucker, P.A. A removable arc for mounting and recovering flash-cooled crystals. J. Appl. Crystallogr. 29:208-210, 1996.
    • (1996) J. Appl. Crystallogr. , vol.29 , pp. 208-210
    • Engel, C.1    Wierenga, R.2    Tucker, P.A.3
  • 24
    • 0022330342 scopus 로고
    • Cross-linking studies of steroidogenic electron transfer: Covalent complex of adrenodoxin reductase with adrenodoxin
    • Usanov, S.A., Turko, I.V., Chashchin, V.L., Akhrem, A.A. Cross-linking studies of steroidogenic electron transfer: covalent complex of adrenodoxin reductase with adrenodoxin. Biochim. Biophys. Acta 832:288-296, 1985.
    • (1985) Biochim. Biophys. Acta , vol.832 , pp. 288-296
    • Usanov, S.A.1    Turko, I.V.2    Chashchin, V.L.3    Akhrem, A.A.4
  • 25
    • 0024592960 scopus 로고
    • Purification and catalytic properties of a cross-linked complex between adrenodoxin reductase and adrenodoxin
    • Hara, T., Kimura, T. Purification and catalytic properties of a cross-linked complex between adrenodoxin reductase and adrenodoxin. J. Biochem. 105:594-600, 1989.
    • (1989) J. Biochem. , vol.105 , pp. 594-600
    • Hara, T.1    Kimura, T.2
  • 27
    • 0028103275 scopus 로고
    • Number 4. The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4. The CCP4 suite: Programs for protein crystallography. Acta Crystallogr. D50:760-763, 1994.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 28
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews, B.W. Solvent content of protein crystals. J. Mol. Biol. 33:491-497, 1968.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.