메뉴 건너뛰기




Volumn 48, Issue 14, 2009, Pages 3109-3119

Protein motifs involved in coenzyme interaction and enzymatic efficiency in anabaena ferredoxin-NADP+ reductase

Author keywords

[No Author keywords available]

Indexed keywords

COENZYME SPECIFICITIES; ENZYMATIC EFFICIENCIES; FLAVIN COFACTOR; HYDRIDE TRANSFERS; PROTEIN MOTIFS;

EID: 65249171975     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi802077c     Document Type: Article
Times cited : (18)

References (48)
  • 1
    • 0028314680 scopus 로고
    • Structure-function relations for ferredoxin reductase
    • Karplus, P. A., and Bruns, C. M. (1994) Structure-function relations for ferredoxin reductase. J. Bioenerg. Biomembr. 26, 89-99.
    • (1994) J. Bioenerg. Biomembr , vol.26 , pp. 89-99
    • Karplus, P.A.1    Bruns, C.M.2
  • 3
    • 0037073754 scopus 로고    scopus 로고
    • Modification of the nucleotide cofactor-binding site of cytochrome P-450 reductase to enhance turnover with NADH in vivo
    • Elmore, C. L., and Porter, T. D. (2002) Modification of the nucleotide cofactor-binding site of cytochrome P-450 reductase to enhance turnover with NADH in vivo. J. Biol. Chem. 277, 48960-48964.
    • (2002) J. Biol. Chem , vol.277 , pp. 48960-48964
    • Elmore, C.L.1    Porter, T.D.2
  • 6
    • 0025019734 scopus 로고
    • Redesign of the coenzyme specificity of a dehydrogenase by protein engineering
    • Scrutton, N. S., Berry, A., and Perham, R. N. (1990) Redesign of the coenzyme specificity of a dehydrogenase by protein engineering. Nature 343, 38-43.
    • (1990) Nature , vol.343 , pp. 38-43
    • Scrutton, N.S.1    Berry, A.2    Perham, R.N.3
  • 8
    • 0141791270 scopus 로고    scopus 로고
    • Engineering and characterization of a NADPH-utilizing cytochrome b5 reductase
    • Marohnic, C. C., Bewley, M. C., and Barber, M. J. (2003) Engineering and characterization of a NADPH-utilizing cytochrome b5 reductase. Biochemistry 42, 11170-11182.
    • (2003) Biochemistry , vol.42 , pp. 11170-11182
    • Marohnic, C.C.1    Bewley, M.C.2    Barber, M.J.3
  • 9
    • 0142071842 scopus 로고    scopus 로고
    • Complete reversal of coenzyme specificity by concerted mutation of three consecutive residues in alcohol dehydrogenase
    • Rosell, A., Valencia, E., Ochoa, W. F., Fita, I., Pares, X., and Farres, J. (2003) Complete reversal of coenzyme specificity by concerted mutation of three consecutive residues in alcohol dehydrogenase. J. Biol. Chem. 278, 40573-40580.
    • (2003) J. Biol. Chem , vol.278 , pp. 40573-40580
    • Rosell, A.1    Valencia, E.2    Ochoa, W.F.3    Fita, I.4    Pares, X.5    Farres, J.6
  • 13
    • 12144286291 scopus 로고    scopus 로고
    • Interaction of ferre-doxin-NADP(+) reductase with its substrates: Optimal interaction for efficient electron transfer
    • Medina, M., and Gomez-Moreno, C. (2004) Interaction of ferre-doxin-NADP(+) reductase with its substrates: optimal interaction for efficient electron transfer. Photosynth. Res. 79, 113-131.
    • (2004) Photosynth. Res , vol.79 , pp. 113-131
    • Medina, M.1    Gomez-Moreno, C.2
  • 15
    • 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, C. M., and Karplus, P. A. (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
  • 20
    • 40349108840 scopus 로고    scopus 로고
    • Modulation of the enzymatic efficiency of ferredoxin-NADP(H) reductase by the amino acid volume around the catalytic site
    • Musumeci, M. A., Arakaki, A. K., Rial, D. V., Catalano-Dupuy, D. L., and Ceccarelli, E. A. (2008) Modulation of the enzymatic efficiency of ferredoxin-NADP(H) reductase by the amino acid volume around the catalytic site. FEBS J. 275, 1350-1366.
    • (2008) FEBS J , vol.275 , pp. 1350-1366
    • Musumeci, M.A.1    Arakaki, A.K.2    Rial, D.V.3    Catalano-Dupuy, D.L.4    Ceccarelli, E.A.5
  • 23
    • 33745907556 scopus 로고    scopus 로고
    • Structural basis for the alteration of coenzyme specificity in a malate dehydrogenase mutant
    • Tomita, T., Fushinobu, S., Kuzuyama, T., and Nishiyama, M. (2006) Structural basis for the alteration of coenzyme specificity in a malate dehydrogenase mutant. Biochem. Biophys. Res. Commun. 347, 502-508.
    • (2006) Biochem. Biophys. Res. Commun , vol.347 , pp. 502-508
    • Tomita, T.1    Fushinobu, S.2    Kuzuyama, T.3    Nishiyama, M.4
  • 24
    • 0034719132 scopus 로고    scopus 로고
    • Trp-676 facilitates nicotinamide coenzyme exchange in the reductive half-reaction of human cytochrome P450 reductase: Properties of the soluble W676H and W676A mutant reductases
    • Gutierrez, A., Doehr, O., Paine, M., Wolf, C. R., Scrutton, N. S., and Roberts, G C. (2000) Trp-676 facilitates nicotinamide coenzyme exchange in the reductive half-reaction of human cytochrome P450 reductase: Properties of the soluble W676H and W676A mutant reductases. Biochemistry 39, 15990-15999.
    • (2000) Biochemistry , vol.39 , pp. 15990-15999
    • Gutierrez, A.1    Doehr, O.2    Paine, M.3    Wolf, C.R.4    Scrutton, N.S.5    Roberts, G.C.6
  • 25
    • 0037109069 scopus 로고    scopus 로고
    • A conserved flavin-shielding residue regulates NO synthase electron transfer and nicotinamide coenzyme specificity
    • Adak, S., Sharma, M., Meade, A. L., and Stuehr, D. J. (2002) A conserved flavin-shielding residue regulates NO synthase electron transfer and nicotinamide coenzyme specificity. Proc. Natl. Acad. Sci. U.S.A. 99, 13516-13521.
    • (2002) Proc. Natl. Acad. Sci. U.S.A , vol.99 , pp. 13516-13521
    • Adak, S.1    Sharma, M.2    Meade, A.L.3    Stuehr, D.J.4
  • 26
    • 2442637815 scopus 로고    scopus 로고
    • Role of the C-terminal tyrosine of ferredoxin-nicotinamide adenine dinucleotide phosphate reductase in the electron transfer processes with its protein partners ferredoxin and flavodoxin
    • Nogues, I., Tejero, J., Hurley, J. K., Paladini, D., Frago, S., Tollin, G., Mayhew, S. G., Gomez-Moreno, C., Ceccarelli, E. A., Carrillo, N., and Medina, M. (2004) Role of the C-terminal tyrosine of ferredoxin-nicotinamide adenine dinucleotide phosphate reductase in the electron transfer processes with its protein partners ferredoxin and flavodoxin. Biochemistry 43, 6127-6137.
    • (2004) Biochemistry , vol.43 , pp. 6127-6137
    • Nogues, I.1    Tejero, J.2    Hurley, J.K.3    Paladini, D.4    Frago, S.5    Tollin, G.6    Mayhew, S.G.7    Gomez-Moreno, C.8    Ceccarelli, E.A.9    Carrillo, N.10    Medina, M.11
  • 27
    • 0029075043 scopus 로고
    • Structural studies on corn nitrate reductase: Refined structure of the cytochrome b reductase fragment at 2.5 Å, its ADP complex and an active-site mutant and modeling of the cytochrome b domain
    • Lu, G., Lindqvist, Y., Schneider, G., Dwivedi, U., and Campbell, W. (1995) Structural studies on corn nitrate reductase: Refined structure of the cytochrome b reductase fragment at 2.5 Å, its ADP complex and an active-site mutant and modeling of the cytochrome b domain. J. Mol. Biol. 248, 931-948.
    • (1995) J. Mol. Biol , vol.248 , pp. 931-948
    • Lu, G.1    Lindqvist, Y.2    Schneider, G.3    Dwivedi, U.4    Campbell, W.5
  • 28
    • 0028964322 scopus 로고
    • Crystal structure of NADH-cytochrome b5 reductase from pig liver at 2.4 Å resolution
    • Nishida, H., Inaka, K., Yamanaka, M., Kaida, S., Kobayashi, K., and Miki, K (1995) Crystal structure of NADH-cytochrome b5 reductase from pig liver at 2.4 Å resolution. Biochemistry 34, 2763-2767.
    • (1995) Biochemistry , vol.34 , pp. 2763-2767
    • Nishida, H.1    Inaka, K.2    Yamanaka, M.3    Kaida, S.4    Kobayashi, K.5    Miki, K.6
  • 29
    • 0027093793 scopus 로고
    • Phthalate dioxygenase reductase: A modular structure for electron transfer from pyridine nucleotides to [2Fe-2S]
    • Correll, C. C., Batie, C. J., Ballou, D. P., and Ludwig, M. L. (1992) Phthalate 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
  • 33
    • 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
  • 34
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron-density maps and the location of errors in these models
    • Jones, T. A., Zou, 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    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 35
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) PROCHECK: A program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 36
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modeling and drug design program
    • Vriend, G (1990) WHAT IF: A molecular modeling and drug design program. J. Mol. Graphics 8, 52-56, 29.
    • (1990) J. Mol. Graphics , vol.8 , Issue.52-56 , pp. 29
    • Vriend, G.1
  • 38
    • 0021209611 scopus 로고
    • + reductase. Rapid-reaction evidence for participation of a ternary complex
    • + reductase. 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
  • 41
    • 0035856561 scopus 로고    scopus 로고
    • The structure and biochemistry of NADH-dependent cytochrome b5 reductase are now consistent
    • Bewley, M. C., Marohnic, C. C., and Barber, M. J. (2001) The structure and biochemistry of NADH-dependent cytochrome b5 reductase are now consistent. Biochemistry 40, 13574-13582.
    • (2001) Biochemistry , vol.40 , pp. 13574-13582
    • Bewley, M.C.1    Marohnic, C.C.2    Barber, M.J.3
  • 42
    • 35448935698 scopus 로고    scopus 로고
    • Mechanism of coenzyme binding to human methionine synthase reductase revealed through the crystal structure of the FNR-like module and isothermal titration calorimetry
    • Wolthers, K. R., Lou, X., Toogood, H. S., Leys, D., and Scrutton, N. S. (2007) Mechanism of coenzyme binding to human methionine synthase reductase revealed through the crystal structure of the FNR-like module and isothermal titration calorimetry. Biochemistry 46, 11833-11844.
    • (2007) Biochemistry , vol.46 , pp. 11833-11844
    • Wolthers, K.R.1    Lou, X.2    Toogood, H.S.3    Leys, D.4    Scrutton, N.S.5
  • 43
    • 0030873316 scopus 로고    scopus 로고
    • Three-dimensional structure of NADPH-cytochrome P450 reductase: Prototype for FMN- and FAD-containing enzymes
    • Wang, M., Roberts, D. L., Paschke, R., Shea, T. M., Masters, B. S., and Kim, J. J. (1997) Three-dimensional structure of NADPH-cytochrome P450 reductase: Prototype for FMN- and FAD-containing enzymes. Proc. Natl. Acad. Sci. U.S.A. 94, 8411-8416.
    • (1997) Proc. Natl. Acad. Sci. U.S.A , 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
  • 44
    • 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., Coves, J., Fontecave, M., Ferrer, J. L., and Fontecilla-Camps, J. C. (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    Coves, J.4    Fontecave, M.5    Ferrer, J.L.6    Fontecilla-Camps, J.C.7
  • 46
    • 84989758039 scopus 로고
    • Regulation of Maize Root Nitrate Reductase Messenger-RNA Levels
    • Long, D. M., Oaks, A., and Rothstein, S. J. (1992) Regulation of Maize Root Nitrate Reductase Messenger-RNA Levels. Physiol. Plant. 85, 561-566.
    • (1992) Physiol. Plant , vol.85 , pp. 561-566
    • Long, D.M.1    Oaks, A.2    Rothstein, S.J.3
  • 48
    • 0036933705 scopus 로고    scopus 로고
    • Nelson, K. E., Weinel, C., Paulsen, I. T., Dodson, R. J., Hilbert, H., Martins dos Santos, V. A., Fouts, D. E., Gill, S. R., Pop, M., Holmes, M., Brinkac, L., Beanan, M., DeBoy, R. T., Daugherty, S., Kolonay, J., Madupu, R., Nelson, W., White, O., Peterson, J., Khouri, H., Hance, I., Chris Lee, P., Holtzapple, E., Scanlan, D., Tran, K., Moazzez, A., Utterback, T., Rizzo, M., Lee, K., Kosack, D., Moestl, D., Wedler, H., Lauber, J., Stjepandic, D., Hoheisel, J., Straetz, M., Heim, S., Kiewitz, C., Eisen, J. A., Timmis, K. N., Dusterhoft, A., Tummler, B., and Fraser, C. M. (2002) Complete genome sequence and comparative analysis of the metabolically versatile Pseudomonas putida KT2440. Environ. Microbiol. 4, 799-808.
    • Nelson, K. E., Weinel, C., Paulsen, I. T., Dodson, R. J., Hilbert, H., Martins dos Santos, V. A., Fouts, D. E., Gill, S. R., Pop, M., Holmes, M., Brinkac, L., Beanan, M., DeBoy, R. T., Daugherty, S., Kolonay, J., Madupu, R., Nelson, W., White, O., Peterson, J., Khouri, H., Hance, I., Chris Lee, P., Holtzapple, E., Scanlan, D., Tran, K., Moazzez, A., Utterback, T., Rizzo, M., Lee, K., Kosack, D., Moestl, D., Wedler, H., Lauber, J., Stjepandic, D., Hoheisel, J., Straetz, M., Heim, S., Kiewitz, C., Eisen, J. A., Timmis, K. N., Dusterhoft, A., Tummler, B., and Fraser, C. M. (2002) Complete genome sequence and comparative analysis of the metabolically versatile Pseudomonas putida KT2440. Environ. Microbiol. 4, 799-808.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.