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Volumn 79, Issue 2, 2004, Pages 113-131

Interaction of ferredoxin-NADP+ reductase with its substrates: Optimal interaction for efficient electron transfer

Author keywords

Catalysis; Coenzyme recognition; Electron transfer; Ferredoxin; Flavodoxin; FNR; NADP+ H; Protein protein interactions; X ray structure

Indexed keywords

ALGAE; CYANOBACTERIA;

EID: 12144286291     PISSN: 01668595     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:PRES.0000015386.67746.2c     Document Type: Review
Times cited : (81)

References (83)
  • 6
  • 7
    • 1542311387 scopus 로고
    • Some further investigations on chloroplasts TPNH diaphorase
    • Avron M and Jagendorf AT (1957) Some further investigations on chloroplasts TPNH diaphorase. Arch Biochem Biophys 72: 17-24
    • (1957) Arch Biochem Biophys , vol.72 , pp. 17-24
    • Avron, M.1    Jagendorf, A.T.2
  • 9
    • 0021209611 scopus 로고
    • + oxidoreductase. Rapid-reaction evidence for participation of a ternary complex
    • + oxidoreductase. Rapid-reaction evidence for participation of a ternary complex. J Biol Chem 259: 11976-11985
    • (1984) J Biol Chem , vol.259 , pp. 11976-11985
    • Batie, C.J.1    Kamin, H.2
  • 10
    • 0023002182 scopus 로고
    • +(H). Specificity and oxidation-reduction properties
    • +(H). Specificity and oxidation-reduction properties. J Biol Chem 261: 11214-11223
    • (1986) J Biol Chem , vol.261 , pp. 11214-11223
    • Batie, C.J.1    Kamin, H.2
  • 11
    • 0034087490 scopus 로고    scopus 로고
    • The role of adrenodoxin in adrenal steroidogenesis
    • Bernhardt R (2000) The role of adrenodoxin in adrenal steroidogenesis. Curr Opin End Diab 7: 109-115
    • (2000) Curr Opin End Diab , vol.7 , pp. 109-115
    • Bernhardt, R.1
  • 13
    • 0028921929 scopus 로고
    • Refined crystal structure of spinach ferredoxin reductase at 1.7 Å resolution: Oxidized, reduced and 2′-phospho-5′-AMP bound states
    • Bruns CM and Karplus PA (1995) Refined crystal structure of spinach ferredoxin reductase at 1.7 Å resolution: oxidized, reduced and 2′-phospho-5′-AMP bound states. J Mol Biol 247: 125-145
    • (1995) J Mol Biol , vol.247 , pp. 125-145
    • Bruns, C.M.1    Karplus, P.A.2
  • 14
    • 0039441128 scopus 로고    scopus 로고
    • Nitrate reductase structure, function and regulation: Bridging the gap between biochemistry and physiology
    • Campbell WH (1999) Nitrate reductase structure, function and regulation: bridging the gap between biochemistry and physiology. Annu Rev Plant Physiol Plant Mol Biol 50: 277-303
    • (1999) Annu Rev Plant Physiol Plant Mol Biol , vol.50 , pp. 277-303
    • Campbell, W.H.1
  • 19
    • 0027093793 scopus 로고
    • Phtalate dioxygenase reductase: A modular structure for electron transfer from pyridine nucleotides to [2Fe-2S]
    • Correll CC, Batie CJ, Ballou DP and Ludwig ML (1992) Phtalate dioxygenase reductase: a modular structure for electron transfer from pyridine nucleotides to [2Fe-2S]. Science 258: 1604-1610
    • (1992) Science , vol.258 , pp. 1604-1610
    • Correll, C.C.1    Batie, C.J.2    Ballou, D.P.3    Ludwig, M.L.4
  • 20
    • 0142213304 scopus 로고    scopus 로고
    • Close encounters of the transient kind: Protein interactions in the photosynthetic redox chain investigated by NMR spectroscopy
    • Crowley PB and Ubbink M (2003) Close encounters of the transient kind: protein interactions in the photosynthetic redox chain investigated by NMR spectroscopy. Acc Chem Res 36: 723-730
    • (2003) Acc Chem Res , vol.36 , pp. 723-730
    • Crowley, P.B.1    Ubbink, M.2
  • 21
    • 0034681465 scopus 로고    scopus 로고
    • Convergent solutions to binding at a protein-protein interface
    • DeLano WL, Ultsch MH, de Vos AM and Wells JA (2000) Convergent solutions to binding at a protein-protein interface. Science 287: 1279-1283
    • (2000) Science , vol.287 , pp. 1279-1283
    • DeLano, W.L.1    Ultsch, M.H.2    De Vos, A.M.3    Wells, J.A.4
  • 23
    • 0039591353 scopus 로고    scopus 로고
    • Side-chain interactions in the plastocyanin-cytochrome f complex
    • Ejdebäck M, Bergkvist A, Karlsson BG and Ubbink M (2000) Side-chain interactions in the plastocyanin-cytochrome f complex. Biochemistry 39: 5022-5027
    • (2000) Biochemistry , vol.39 , pp. 5022-5027
    • Ejdebäck, M.1    Bergkvist, A.2    Karlsson, B.G.3    Ubbink, M.4
  • 26
    • 0014669469 scopus 로고
    • Complex formation between ferredoxin triphosphopyridine nucleotide reductase and electron transfer proteins
    • Foust GP, Mayhew SG and Massey V (1969) Complex formation between ferredoxin triphosphopyridine nucleotide reductase and electron transfer proteins. J Biol Chem 244: 964-970
    • (1969) J Biol Chem , vol.244 , pp. 964-970
    • Foust, G.P.1    Mayhew, S.G.2    Massey, V.3
  • 28
    • 0034716944 scopus 로고    scopus 로고
    • Four crystal structures of the 60 kDa flavoprotein monomer of the sulfite reductase indicate a disordered flavodoxin-like module
    • Gruez A, Pignol D, Zeghouf M, Covès J, Fontecave M, Ferrer J-L and Fontecilla-Camps JC (2000) Four crystal structures of the 60 kDa flavoprotein monomer of the sulfite reductase indicate a disordered flavodoxin-like module. J Mol Biol 299: 199-212
    • (2000) J Mol Biol , vol.299 , pp. 199-212
    • Gruez, A.1    Pignol, D.2    Zeghouf, M.3    Covès, J.4    Fontecave, M.5    Ferrer, J.-L.6    Fontecilla-Camps, J.C.7
  • 30
    • 0001227655 scopus 로고
    • The nature of π-π interactions
    • Hunter CA and Sanders JKM (1990) The nature of π-π interactions. J Am Chem Soc 112: 5525-5534
    • (1990) J Am Chem Soc , vol.112 , pp. 5525-5534
    • Hunter, C.A.1    Sanders, J.K.M.2
  • 33
    • 0027982705 scopus 로고
    • + reductase system from Anabaena: Requirement of a negative charge at position 94 in ferredoxin for rapid electron transfer
    • + reductase system from Anabaena: requirement of a negative charge at position 94 in ferredoxin for rapid electron transfer. Arch Biochem Biophys 312: 480-486
    • (1994) Arch Biochem Biophys , vol.312 , pp. 480-486
    • Hurley, J.K.1    Medina, M.2    Gómez-Moreno, C.3    Tollin, G.4
  • 36
    • 0031585989 scopus 로고    scopus 로고
    • The three-dimensional structure of flavodoxin reductase from Escherichia coli at 1.7 Å resolution
    • Ingelman M, Bianchi V and Eklund H (1997) The three-dimensional structure of flavodoxin reductase from Escherichia coli at 1.7 Å resolution. J Mol Biol 268: 147-157
    • (1997) J Mol Biol , vol.268 , pp. 147-157
    • Ingelman, M.1    Bianchi, V.2    Eklund, H.3
  • 37
    • 0033152746 scopus 로고    scopus 로고
    • Crystal structure of NAD(P)H: Flavin oxidoreductase from Escherichia coli
    • Ingelman M, Ramaswamy S, Nivière V, Fontecave M and Eklund H (1999) Crystal structure of NAD(P)H: flavin oxidoreductase from Escherichia coli. Biochemistry 38: 7040-7049
    • (1999) Biochemistry , vol.38 , pp. 7040-7049
    • Ingelman, M.1    Ramaswamy, S.2    Nivière, V.3    Fontecave, M.4    Eklund, H.5
  • 38
    • 0027942020 scopus 로고
    • + reductase and the role of water at the complex interface
    • + reductase and the role of water at the complex interface. Biochemistry 33: 13321-13328
    • (1994) Biochemistry , vol.33 , pp. 13321-13328
    • Jelesarov, I.1    Bosshard, H.R.2
  • 40
    • 0030953444 scopus 로고    scopus 로고
    • Negatively charged Anabaena flavodoxin residues (Asp144 and Glu145) are important for reconstitution of cytochrome P450 17-alpha-hydroxylase activity
    • Jenkins CM, Genzor CG, Fillat MF, Waterman MR and Gómez-Moreno C (1997) Negatively charged Anabaena flavodoxin residues (Asp144 and Glu145) are important for reconstitution of cytochrome P450 17-alpha-hydroxylase activity. J Biol Chem 36: 22509-22513
    • (1997) J Biol Chem , vol.36 , pp. 22509-22513
    • Jenkins, C.M.1    Genzor, C.G.2    Fillat, M.F.3    Waterman, M.R.4    Gómez-Moreno, C.5
  • 41
    • 0033614010 scopus 로고    scopus 로고
    • Complex formation between Azotobacter vinelandii ferredoxin and its physiological electron donor NADPH-ferredoxin reductase
    • Jung Y-S, Roberts VA, Stout CD and Burgess BK (1999) Complex formation between Azotobacter vinelandii ferredoxin and its physiological electron donor NADPH-ferredoxin reductase. J Biol Chem 274: 2978-2987
    • (1999) J Biol Chem , vol.274 , pp. 2978-2987
    • Jung, Y.-S.1    Roberts, V.A.2    Stout, C.D.3    Burgess, B.K.4
  • 42
    • 0028314680 scopus 로고
    • Structure-function relations for ferredoxin reductase
    • Karplus PA and Bruns M (1994) Structure-function relations for ferredoxin reductase. J Bioenerg Biobr 26: 89-99
    • (1994) J Bioenerg Biobr , vol.26 , pp. 89-99
    • Karplus, P.A.1    Bruns, M.2
  • 43
    • 0026023225 scopus 로고
    • + reductase: Prototype for a structurally novel flavoenzyme family
    • + reductase: prototype for a structurally novel flavoenzyme family. Science 251: 60-66
    • (1991) Science , vol.251 , pp. 60-66
    • Karplus, P.A.1    Daniels, M.J.2    Herriot, J.R.3
  • 45
    • 0028140477 scopus 로고
    • NADPH:ferredoxin oxidoreductase acts as a paraquat diaphorase and is a member of the soxRS regulon
    • Liocher SI, Hausladen A, Beyer WF and Fridovich I (1994) NADPH: ferredoxin oxidoreductase acts as a paraquat diaphorase and is a member of the soxRS regulon. Proc Natl Acad Sci USA 91: 1328-1331
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 1328-1331
    • Liocher, S.I.1    Hausladen, A.2    Beyer, W.F.3    Fridovich, I.4
  • 46
    • 0342327312 scopus 로고    scopus 로고
    • Differential stabilization of the three FMN redox forms by tyrosine 94 and tryptophan 57 in flavodoxin from Anabaena and its influence on the redox potentials
    • Lostao A, Gómez-Moreno C, Mayhew SG and Sancho J (1997) Differential stabilization of the three FMN redox forms by tyrosine 94 and tryptophan 57 in flavodoxin from Anabaena and its influence on the redox potentials. Biochemistry 36: 14334-14344
    • (1997) Biochemistry , vol.36 , pp. 14334-14344
    • Lostao, A.1    Gómez-Moreno, C.2    Mayhew, S.G.3    Sancho, J.4
  • 47
    • 0028774181 scopus 로고
    • Crystal structure of the FAD-containing fragment of maize nitrate reductase at 2.5 Å resolution: Relationship to other flavoprotein reductases
    • Lu G, Campbell WH, Schneider G and Lindqvist Y (1994) Crystal structure of the FAD-containing fragment of maize nitrate reductase at 2.5 Å resolution: relationship to other flavoprotein reductases. Structure 2: 809-821
    • (1994) Structure , vol.2 , pp. 809-821
    • Lu, G.1    Campbell, W.H.2    Schneider, G.3    Lindqvist, Y.4
  • 55
    • 0026541311 scopus 로고
    • + reductase from Anabaena sp. PCC 7119 involved in substrate binding
    • + reductase from Anabaena sp. PCC 7119 involved in substrate binding. FEBS Lett 298: 25-28
    • (1992) FEBS Lett , vol.298 , pp. 25-28
    • Medina, M.1    Mendez, E.2    Gómez-Moreno, C.3
  • 59
    • 0033619724 scopus 로고    scopus 로고
    • Refined X-ray structures of the oxidized, at 1.3 Å, and reduced, at 1.17 Å, [2Fe-2S] ferredoxin from the cyanobacterium Anabaena PCC7119 show redox-linked conformational changes
    • Morales R, Charon MH, Hudry-Clergeon G, Petillot Y, Norager S, Medina M and Frey M (1999) Refined X-ray structures of the oxidized, at 1.3 Å, and reduced, at 1.17 Å, [2Fe-2S] ferredoxin from the cyanobacterium Anabaena PCC7119 show redox-linked conformational changes. Biochemistry 38: 15764-15773
    • (1999) Biochemistry , vol.38 , pp. 15764-15773
    • Morales, R.1    Charon, M.H.2    Hudry-Clergeon, G.3    Petillot, Y.4    Norager, S.5    Medina, M.6    Frey, M.7
  • 65
    • 0022919721 scopus 로고
    • Crystal structure of substrate-free Pseudomonas putida cytochrome P-450
    • Poulos TL, Finzel BC and Howard AJ (1986) Crystal structure of substrate-free Pseudomonas putida cytochrome P-450. Biochemistry 25: 5314-5322
    • (1986) Biochemistry , vol.25 , pp. 5314-5322
    • Poulos, T.L.1    Finzel, B.C.2    Howard, A.J.3
  • 68
    • 0026325678 scopus 로고
    • + reductase from Anabaena PCC7119 and of their electrostatic and covalent complexes
    • + reductase from Anabaena PCC7119 and of their electrostatic and covalent complexes. Eur J Biochem 202: 1065-1071
    • (1991) Eur J Biochem , vol.202 , pp. 1065-1071
    • Pueyo, J.J.1    Gómez-Moreno, C.2    Mayhew, S.G.3
  • 73
    • 0002374519 scopus 로고
    • Crystallization of ferredoxin-TPN reductase and its role in the photosynthetic apparatus of chloroplasts
    • Shin M, Tagawa K and Arnon DI (1963) Crystallization of ferredoxin-TPN reductase and its role in the photosynthetic apparatus of chloroplasts. Biochem Z 238: 84-86
    • (1963) Biochem Z , vol.238 , pp. 84-86
    • Shin, M.1    Tagawa, K.2    Arnon, D.I.3
  • 75
    • 0014013044 scopus 로고
    • Triphosphopyridine nucleotide photoreduction with cell-free preparations of Anabaena variabilis
    • Susor WA and Krogmann DW (1966) Triphosphopyridine nucleotide photoreduction with cell-free preparations of Anabaena variabilis. Biochim Biophys Acta 120: 65-72
    • (1966) Biochim Biophys Acta , vol.120 , pp. 65-72
    • Susor, W.A.1    Krogmann, D.W.2
  • 79
    • 0030873316 scopus 로고    scopus 로고
    • Three-dimensional structure of NADPH-cytochrome P450 reductase: Prototype for FMN- and FAD-containing enzymes
    • Wang M, Roberts DL, Paschke R, Shea TM, Masters BS and Kim JJ (1997) Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes. Proc Natl Acad Sci USA 94: 8411-8416
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 8411-8416
    • Wang, M.1    Roberts, D.L.2    Paschke, R.3    Shea, T.M.4    Masters, B.S.5    Kim, J.J.6
  • 82
    • 0034641677 scopus 로고    scopus 로고
    • + and NADPH suggesting a mechanism for the electron transfer of an enzyme family
    • + and NADPH suggesting a mechanism for the electron transfer of an enzyme family. Biochemistry 39: 10986-10995
    • (2000) Biochemistry , vol.39 , pp. 10986-10995
    • Ziegler, G.A.1    Schulz, G.2
  • 83
    • 0033057396 scopus 로고    scopus 로고
    • The structure of adrenodoxin reductase of mitochondrial P450 systems: Electron transfer for steroid biosynthesis
    • Ziegler GA, Vonrhein C, Hanukoglu I and Schulz G (1999) The structure of adrenodoxin reductase of mitochondrial P450 systems: electron transfer for steroid biosynthesis. J Mol Biol 289: 981-990
    • (1999) J Mol Biol , vol.289 , pp. 981-990
    • Ziegler, G.A.1    Vonrhein, C.2    Hanukoglu, I.3    Schulz, G.4


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