메뉴 건너뛰기




Volumn 45, Issue 3, 2006, Pages 709-718

Light-induced reduction of bovine adrenodoxin via the covalently bound ruthenium(II) bipyridyl complex: Intramolecular electron transfer and crystal structure

Author keywords

[No Author keywords available]

Indexed keywords

CRYSTAL STRUCTURE; ELECTRON TRANSITIONS; PROTEINS; RATE CONSTANTS;

EID: 31144443742     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0510330     Document Type: Article
Times cited : (8)

References (49)
  • 3
    • 0018563695 scopus 로고
    • SCC with adrenodoxin and adrenodoxin reductase-adrenodoxin complex. The implication in ACTH function
    • SCC with adrenodoxin and adrenodoxin reductase-adrenodoxin complex. The implication in ACTH function, J. Biol. Chem. 254, 11806-11815.
    • (1979) J. Biol. Chem. , vol.254 , pp. 11806-11815
    • Kido, T.1    Kimura, T.2
  • 5
    • 0032520951 scopus 로고    scopus 로고
    • New aspects of electron transfer revealed by the crystal structure of a truncated bovine adrenodoxin, Adx(4-108)
    • Müller, A., Müller, J. J., Muller, Y. A., Uhlmann, H., Bernhardt, R., and Heinemann, U. (1998) New aspects of electron transfer revealed by the crystal structure of a truncated bovine adrenodoxin, Adx(4-108), Structure 6, 269-280.
    • (1998) Structure , vol.6 , pp. 269-280
    • Müller, A.1    Müller, J.J.2    Muller, Y.A.3    Uhlmann, H.4    Bernhardt, R.5    Heinemann, U.6
  • 6
    • 0035951779 scopus 로고    scopus 로고
    • Adrenodoxin reductase-adrenodoxin complex structure suggests electron-transfer path in steroid biosynthesis
    • Müller, J. J., Lapko, A., Bourenkov, G., Ruckpaul, K., and Heinemann, U. (2001) Adrenodoxin reductase-adrenodoxin complex structure suggests electron-transfer path in steroid biosynthesis, J. Biol. Chem. 276, 2786-2789.
    • (2001) J. Biol. Chem. , vol.276 , pp. 2786-2789
    • Müller, J.J.1    Lapko, A.2    Bourenkov, G.3    Ruckpaul, K.4    Heinemann, U.5
  • 8
    • 0037172776 scopus 로고    scopus 로고
    • A new electron transport mechanism in mitochondrial steroid hydroxylase systems based on structural changes upon the reduction of adrenodoxin
    • Beilke, D., Weiss, R., Lohr, F., Pristovsek, P., Hannemann, F., Bernhardt, R., and Rüterjans, H. (2002) A new electron transport mechanism in mitochondrial steroid hydroxylase systems based on structural changes upon the reduction of adrenodoxin, Biochemistry 41, 7969-7978.
    • (2002) Biochemistry , vol.41 , pp. 7969-7978
    • Beilke, D.1    Weiss, R.2    Lohr, F.3    Pristovsek, P.4    Hannemann, F.5    Bernhardt, R.6    Rüterjans, H.7
  • 9
    • 0026496878 scopus 로고
    • Expression of bovine adrenodoxin in E. coli and site-directed mutagenesis of /2 FE- -2S/ cluster ligands
    • Uhlmann, H., Becken, V., Schwarz, D., and Bernhardt, R. (1992) Expression of bovine adrenodoxin in E. coli and site-directed mutagenesis of /2 FE- -2S/ cluster ligands, Biochem. Biophys. Res. Commun. 188, 1131-1138.
    • (1992) Biochem. Biophys. Res. Commun. , vol.188 , pp. 1131-1138
    • Uhlmann, H.1    Becken, V.2    Schwarz, D.3    Bernhardt, R.4
  • 10
    • 0026279733 scopus 로고
    • Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system
    • Studier, F. W. (1991) Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system, J. Mol. Biol. 219, 37-44.
    • (1991) J. Mol. Biol. , vol.219 , pp. 37-44
    • Studier, F.W.1
  • 11
    • 0343052039 scopus 로고    scopus 로고
    • Preparation and crystallization of a cross-linked complex of bovine adrenodoxin and adrenodoxin reductase
    • Lapko, A., Müller, A., Heese, O., Ruckpaul, K., and Heinemann, U. (1997) Preparation and crystallization of a cross-linked complex of bovine adrenodoxin and adrenodoxin reductase, Proteins: Struct., Funct., Genet. 28, 289-292.
    • (1997) Proteins: Struct., Funct., Genet. , vol.28 , pp. 289-292
    • Lapko, A.1    Müller, A.2    Heese, O.3    Ruckpaul, K.4    Heinemann, U.5
  • 12
    • 0021272401 scopus 로고
    • The domain structure of the cholesterol side-chain cleavage cytochrome P-450 from bovine adrenocortical mitochondria
    • Chashchin, V. L., Vasilevsky, V. I., Shkumatov, V. M., and Akhrem, A. A. (1984) The domain structure of the cholesterol side-chain cleavage cytochrome P-450 from bovine adrenocortical mitochondria, Biochim. Biophys. Acta 787, 27-38.
    • (1984) Biochim. Biophys. Acta , vol.787 , pp. 27-38
    • Chashchin, V.L.1    Vasilevsky, V.I.2    Shkumatov, V.M.3    Akhrem, A.A.4
  • 13
    • 0015939436 scopus 로고
    • Adrenal steroid hydroxylases. Oxidation-reduction properties of adrenal iron-sulfur protein (adrenodoxin)
    • Huang, J. J., and Kimura, T. (1973) Adrenal steroid hydroxylases. Oxidation-reduction properties of adrenal iron-sulfur protein (adrenodoxin), Biochemistry 12, 406-409.
    • (1973) Biochemistry , vol.12 , pp. 406-409
    • Huang, J.J.1    Kimura, T.2
  • 14
    • 0015935335 scopus 로고
    • Studies on adrenal steroid hydroxylases. Molecular and catalytic properties of adrenodoxin reductase (a flavoprotein)
    • Chu, J. W., and Kimura, T. (1973) Studies on adrenal steroid hydroxylases. Molecular and catalytic properties of adrenodoxin reductase (a flavoprotein), J. Biol. Chem. 248, 2089-2094.
    • (1973) J. Biol. Chem. , vol.248 , pp. 2089-2094
    • Chu, J.W.1    Kimura, T.2
  • 15
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature
    • Omura, T., and Sato, R. (1964) The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature, J. Biol. Chem. 239, 2370-2378.
    • (1964) J. Biol. Chem. , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 16
    • 0037145078 scopus 로고    scopus 로고
    • cam covalently bound with tris(2,2'-bipyridyl)ruthenium(II): Structural changes detected by FTIR spectroscopy
    • cam covalently bound with tris(2,2'-bipyridyl)ruthenium(II): structural changes detected by FTIR spectroscopy, J. Inorg. Biochem. 91, 607-617.
    • (2002) J. Inorg. Biochem. , vol.91 , pp. 607-617
    • Contzen, J.1    Kostka, S.2    Kraft, R.3    Jung, C.4
  • 17
    • 0001127948 scopus 로고
    • A thermodynamic model of regulation: Modulation of redox equilibria in camphor monoxygenase
    • Sugar, S. G., and Gunsalus, I. C. (1976) A thermodynamic model of regulation: modulation of redox equilibria in camphor monoxygenase, Proc. Natl. Acad. Sci. U.S.A. 73, 1078-1082.
    • (1976) Proc. Natl. Acad. Sci. U.S.A. , vol.73 , pp. 1078-1082
    • Sugar, S.G.1    Gunsalus, I.C.2
  • 18
    • 0342769911 scopus 로고
    • Studies on oxidation-reduction. XVIII. Simple safranines
    • Stiehler, R. D., Chen, T.-T., and Mansfield Clark, W. (1933) Studies on oxidation-reduction. XVIII. Simple safranines, J. Am. Chem. Soc. 55, 891-907.
    • (1933) J. Am. Chem. Soc. , vol.55 , pp. 891-907
    • Stiehler, R.D.1    Chen, T.-T.2    Mansfield Clark, W.3
  • 20
    • 0000562811 scopus 로고
    • Hydrogen-production by visible-light using viologen-dye mediated redox cycles
    • Keller, P., Moradpour, A., Amouyal, E., and Kagan, H. B. (1980) Hydrogen-production by visible-light using viologen-dye mediated redox cycles, Nouv. J. Chim. 4. 377-384.
    • (1980) Nouv. J. Chim. , vol.4 , pp. 377-384
    • Keller, P.1    Moradpour, A.2    Amouyal, E.3    Kagan, H.B.4
  • 22
    • 0024431817 scopus 로고
    • Photoinduced electron-transfer kinetics of singly labeled ruthenium bis(bipyridine) dicarboxybipyridine cytochrome c derivatives
    • Durham, D., Pan, L. P., Long, J. E., and Millet, F. (1989) Photoinduced electron-transfer kinetics of singly labeled ruthenium bis(bipyridine) dicarboxybipyridine cytochrome c derivatives, Biochemistry 28, 8659-8665.
    • (1989) Biochemistry , vol.28 , pp. 8659-8665
    • Durham, D.1    Pan, L.P.2    Long, J.E.3    Millet, F.4
  • 24
    • 0014007458 scopus 로고
    • Study of the adrenal non-heme iron protein (adrenodoxin) by electron spin resonance
    • Watari, H., and Kimura, T. (1966) Study of the adrenal non-heme iron protein (adrenodoxin) by electron spin resonance, Biochem. Biophys. Res. Commun. 24, 106-112.
    • (1966) Biochem. Biophys. Res. Commun. , vol.24 , pp. 106-112
    • Watari, H.1    Kimura, T.2
  • 26
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. (1994) AMoRe: an automated package for molecular replacement, Acta Crystallogr. A50, 157-163.
    • (1994) Acta Crystallogr. , vol.A50 , pp. 157-163
    • Navaza, J.1
  • 27
    • 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
  • 29
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zhou, J.-Y., Cowan, S. W., and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models, Acta Crystallogr. A47, 110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zhou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 30
    • 0001212417 scopus 로고
    • Holographic methods in X-ray crystallography. II. Detailed theory and connection to other methods of crystallography
    • Szoke, A. (1993). Holographic methods in X-ray crystallography. II. Detailed theory and connection to other methods of crystallography, Acta Crystallogr. A49, 853-866.
    • (1993) Acta Crystallogr. , vol.A49 , pp. 853-866
    • Szoke, A.1
  • 32
    • 84893482610 scopus 로고
    • A solution for the best rotation to relate two sets of vectors
    • Kabsch, W. (1976) A solution for the best rotation to relate two sets of vectors, Acta Crystallogr. A32, 922-923.
    • (1976) Acta Crystallogr. , vol.A32 , pp. 922-923
    • Kabsch, W.1
  • 34
    • 0027979002 scopus 로고
    • C-terminal region of adrenodoxin affects its structural integrity and determines differences in its electron-transfer function to cytochrome P-450
    • Uhlmann, H., Kraft, R., and Bernhardt, R. (1994) C-terminal region of adrenodoxin affects its structural integrity and determines differences in its electron-transfer function to cytochrome P-450, J. Biol. Chem. 269, 22567-22564.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22567-122564
    • Uhlmann, H.1    Kraft, R.2    Bernhardt, R.3
  • 35
    • 0037438454 scopus 로고    scopus 로고
    • Modeling of electrostatic recognition processes in the mammalian mitochondrial steroid hydroxylase system
    • Müller, J. J., Lapko, A., Ruckpaul, K., and Heinemann, U. (2003) Modeling of electrostatic recognition processes in the mammalian mitochondrial steroid hydroxylase system, Biophys. Chem. 100, 281-292.
    • (2003) Biophys. Chem. , vol.100 , pp. 281-292
    • Müller, J.J.1    Lapko, A.2    Ruckpaul, K.3    Heinemann, U.4
  • 36
    • 0000718441 scopus 로고
    • Intramolecular electron transfer in cytochrome 65 labelled with ruthenium(II) polypyridine complexes: Rate measurements in the Marcus inverted region
    • Scott, J. R., Willie, A., McLean, M., Stayton, P. S., Sugar, S. G., Durham, B., and Millett, F. (1993) Intramolecular electron transfer in cytochrome 65 labelled with ruthenium(II) polypyridine complexes: rate measurements in the Marcus inverted region, J. Am. Chem. Soc. 115, 6820-6824.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 6820-6824
    • Scott, J.R.1    Willie, A.2    McLean, M.3    Stayton, P.S.4    Sugar, S.G.5    Durham, B.6    Millett, F.7
  • 37
    • 0029639076 scopus 로고
    • Pressure tuning voltammetry. Reaction volumes for electron transfer in cytochrome c and ruthenium-modified cytochromes c
    • Sun, J., Wishart, J. F., van Eldik, R., Shalders, R. D., and Swaddle, T. W. (1995) Pressure tuning voltammetry. Reaction volumes for electron transfer in cytochrome c and ruthenium-modified cytochromes c, J. Am. Chem. Soc. 117, 2600-2605.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 2600-2605
    • Sun, J.1    Wishart, J.F.2    Van Eldik, R.3    Shalders, R.D.4    Swaddle, T.W.5
  • 38
    • 0039721999 scopus 로고
    • Ru(II) polypyridine complexes: Photophysics, photochemistry, electrochemistry, and chemiluminescence
    • Juris, A., Balzani, V., Barigelletti, F., Campagna, S., Belser, P., and Vonzelewsky, A. (1988) Ru(II) polypyridine complexes: photophysics, photochemistry, electrochemistry, and chemiluminescence, Coord. Chem. Rev. 84, 85-277.
    • (1988) Coord. Chem. Rev. , vol.84 , pp. 85-277
    • Juris, A.1    Balzani, V.2    Barigelletti, F.3    Campagna, S.4    Belser, P.5    Vonzelewsky, A.6
  • 39
    • 0033523919 scopus 로고    scopus 로고
    • Natural engineering principles of electron tunnelling in biological oxidation-reduction
    • Page, C. C., Moser, C. C., Chen, X., and Dutton, L. (1999) Natural engineering principles of electron tunnelling in biological oxidation-reduction, Nature 402, 47-52.
    • (1999) Nature , vol.402 , pp. 47-52
    • Page, C.C.1    Moser, C.C.2    Chen, X.3    Dutton, L.4
  • 41
    • 0034732561 scopus 로고    scopus 로고
    • A novel method for determining the electron tunnelling pathways in protein
    • Kawatsu, T., Kakitani, T., and Yamato, T. (2000) A novel method for determining the electron tunnelling pathways in protein, Inorg. Chim. Acta 300-302, 862-868.
    • (2000) Inorg. Chim. Acta , vol.300-302 , pp. 862-868
    • Kawatsu, T.1    Kakitani, T.2    Yamato, T.3
  • 42
    • 0035902349 scopus 로고    scopus 로고
    • Worm model for electron tunnelling in proteins: Consolidation of the pathway model and the Dutton plot
    • Kawatsu, T., Kakitani, T., and Yamato, T. (2001) Worm model for electron tunnelling in proteins: consolidation of the pathway model and the Dutton plot, J. Phys. Chem. 105, 4424-4435.
    • (2001) J. Phys. Chem. , vol.105 , pp. 4424-4435
    • Kawatsu, T.1    Kakitani, T.2    Yamato, T.3
  • 43
    • 0015935048 scopus 로고
    • Environment of the iron-sulfur chromophore in adrenodoxin studied by EPR and ENDOR spectroscopy
    • Mukai, K., Kimura, T., Helbert, J., and Kevan, L. (1973) Environment of the iron-sulfur chromophore in adrenodoxin studied by EPR and ENDOR spectroscopy, Biochim. Biophys. Acta 295, 49-56.
    • (1973) Biochim. Biophys. Acta , vol.295 , pp. 49-56
    • Mukai, K.1    Kimura, T.2    Helbert, J.3    Kevan, L.4
  • 44
    • 0014197664 scopus 로고
    • Components of the electron transport system in adrenal steroid hydroxylase. Isolation and properties of non-heme iron protein (adrenodoxin)
    • Kimura, T., and Suzuki, K. (1967) Components of the electron transport system in adrenal steroid hydroxylase. Isolation and properties of non-heme iron protein (adrenodoxin), J. Biol. Chem. 242, 485-491.
    • (1967) J. Biol. Chem. , vol.242 , pp. 485-491
    • Kimura, T.1    Suzuki, K.2
  • 45
    • 0013849907 scopus 로고
    • Enzymatic reduction of nonheme iron protein (adrenodoxin) by reduced nicotinamide adenine dinucleotide phosphate
    • Kimura, T., and Suzuki, K. (1965) Enzymatic reduction of nonheme iron protein (adrenodoxin) by reduced nicotinamide adenine dinucleotide phosphate, Biochem. Biophys. Res. Commun. 20, 373-379.
    • (1965) Biochem. Biophys. Res. Commun. , vol.20 , pp. 373-379
    • Kimura, T.1    Suzuki, K.2
  • 46
    • 0033979988 scopus 로고    scopus 로고
    • The tertiary structure of full-length bovine adrenodoxin suggests functional dimers
    • Pikuleva, I. A., Tesh, K., Waterman, M. R., and Kim, Y. (2000) The tertiary structure of full-length bovine adrenodoxin suggests functional dimers, Arch. Biochem. Biophys. 373, 44-55.
    • (2000) Arch. Biochem. Biophys. , vol.373 , pp. 44-55
    • Pikuleva, I.A.1    Tesh, K.2    Waterman, M.R.3    Kim, Y.4
  • 47
    • 0024848158 scopus 로고
    • SCC- phenyl isocyanide complex upon binding of reduced adrenodoxin
    • SCC- phenyl isocyanide complex upon binding of reduced adrenodoxin, Biochemistry 28, 9777-9784.
    • (1989) Biochemistry , vol.28 , pp. 9777-9784
    • Tsubaki, M.1    Hiwatashi, A.2    Ichikawa, Y.3
  • 48
    • 0021099477 scopus 로고
    • scc- adrenodoxin complex. Reduction properties of the substrate-associated cytochrome and relation of the reduction states of heme and iron-sulfur centers to association of the proteins
    • scc- adrenodoxin complex. Reduction properties of the substrate-associated cytochrome and relation of the reduction states of heme and iron-sulfur centers to association of the proteins, J. Biol. Chem. 258, 5596-5602.
    • (1983) J. Biol. Chem. , vol.258 , pp. 5596-5602
    • Lambeth, J.D.1    Pember, S.O.2
  • 49
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M., and Wüthrich, K. (1996) MOLMOL: a program for display and analysis of macromolecular structures, J. Mol. Graphics 14, 51-55.
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.