메뉴 건너뛰기




Volumn 74, Issue 2, 2009, Pages 400-416

Geometric constraints for porphyrin binding in helical protein binding sites

Author keywords

Bionanotechnology, protein design; Heme binding; Heme ruffle; Rotamer

Indexed keywords

AMINO ACID; GLYCINE; HEME; HISTIDINE; LIGAND; NANOWIRE; PORPHYRIN; PROTEIN; CYTOCHROME C; HEMOPROTEIN; PROPIONIC ACID DERIVATIVE;

EID: 59449090563     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22143     Document Type: Article
Times cited : (22)

References (85)
  • 1
    • 33745185322 scopus 로고    scopus 로고
    • Intelligent design: The de novo engineering of proteins with specified functions
    • 1
    • 1.Koder RL, Dutton PL. Intelligent design: the de novo engineering of proteins with specified functions. Dalton Trans 2006;25:3045-3051.
    • (2006) Dalton Trans , vol.25 , pp. 3045-3051
    • Koder, R.L.1    Dutton, P.L.2
  • 3
    • 1542274547 scopus 로고    scopus 로고
    • Heme protein assemblies
    • Reedy CJ, Gibney BR. Heme protein assemblies. Chem Rev 2004; 104:617-649.
    • (2004) Chem Rev , vol.104 , pp. 617-649
    • Reedy, C.J.1    Gibney, B.R.2
  • 6
    • 0032558105 scopus 로고    scopus 로고
    • Differential binding of iron(III) and zinc(II) protoporphyrin IX to synthetic four-helix bundles
    • Sharp RE, Diers JR, Bocian DF, Dutton PL. Differential binding of iron(III) and zinc(II) protoporphyrin IX to synthetic four-helix bundles. J Am Chem Soc 1998;120:7103-7104.
    • (1998) J Am Chem Soc , vol.120 , pp. 7103-7104
    • Sharp, R.E.1    Diers, J.R.2    Bocian, D.F.3    Dutton, P.L.4
  • 7
    • 0034641675 scopus 로고    scopus 로고
    • Self-assembly of heme A and heme B in a designed four-helix bundle: Implications for a cytochrome c oxidase ma- quette
    • Gibney BR, Isogai Y, Rabanal F, Reddy KS, Grosset AM, Moser CC, Dutton PL. Self-assembly of heme A and heme B in a designed four-helix bundle: Implications for a cytochrome c oxidase ma- quette. Biochemistry 2000;39:11041-11049.
    • (2000) Biochemistry , vol.39 , pp. 11041-11049
    • Gibney, B.R.1    Isogai, Y.2    Rabanal, F.3    Reddy, K.S.4    Grosset, A.M.5    Moser, C.C.6    Dutton, P.L.7
  • 9
    • 33846436807 scopus 로고    scopus 로고
    • Design of a functional membrane protein by engineering a heme-binding site in glycophorin A
    • Cordova JM, Noack PL, Hilcove SA, Lear JD, Ghirlanda G. Design of a functional membrane protein by engineering a heme-binding site in glycophorin A. J Am Chem Soc 2007;129:512-518.
    • (2007) J Am Chem Soc , vol.129 , pp. 512-518
    • Cordova, J.M.1    Noack, P.L.2    Hilcove, S.A.3    Lear, J.D.4    Ghirlanda, G.5
  • 11
    • 33751337777 scopus 로고    scopus 로고
    • Insight into heme protein redox potential control and functional aspects of six-coordinate ligand-sensing heme proteins from studies of synthetic heme peptides
    • Cowley AB, Kennedy ML, Silchenko S, Lukat-Rodgers GS, Rodgers KR, Benson DR. Insight into heme protein redox potential control and functional aspects of six-coordinate ligand-sensing heme proteins from studies of synthetic heme peptides. Inorg Chem 2006;45: 9985-10001.
    • (2006) Inorg Chem , vol.45 , pp. 9985-10001
    • Cowley, A.B.1    Kennedy, M.L.2    Silchenko, S.3    Lukat-Rodgers, G.S.4    Rodgers, K.R.5    Benson, D.R.6
  • 12
    • 33846444898 scopus 로고    scopus 로고
    • Weak-field anions displace the histidine ligand in a synthetic heme peptide but not in N-acetylmicroperoxi-dase-8: Possible role of heme geometry differences
    • Cowley AB, Benson DR. Weak-field anions displace the histidine ligand in a synthetic heme peptide but not in N-acetylmicroperoxi-dase-8: possible role of heme geometry differences. Inorg Chem 2007; 46:48-59.
    • (2007) Inorg Chem , vol.46 , pp. 48-59
    • Cowley, A.B.1    Benson, D.R.2
  • 13
    • 1042299967 scopus 로고    scopus 로고
    • A possible role for the covalent heme-protein linkage in cytochrome c revealed via comparison of N-acetylmicroperoxidase-8 and a synthetic, monohistidine-coordinated heme peptide
    • 13
    • 13.Cowley AB, Lukat-Rodgers GS, Rodgers KR, Benson DR. A possible role for the covalent heme-protein linkage in cytochrome c revealed via comparison of N-acetylmicroperoxidase-8 and a synthetic, monohistidine-coordinated heme peptide. Biochemistry 2004;43: 1656-1666.
    • (2004) Biochemistry , vol.43 , pp. 1656-1666
    • Cowley, A.B.1    Lukat-Rodgers, G.S.2    Rodgers, K.R.3    Benson, D.R.4
  • 15
    • 33846099581 scopus 로고    scopus 로고
    • Thermodynamic investigation into the mechanisms of proton-coupled electron transfer events in heme protein maquettes
    • Reddi AR, Reedy CJ, Mui S, Gibney BR. Thermodynamic investigation into the mechanisms of proton-coupled electron transfer events in heme protein maquettes. Biochemistry 2007;46: 291-305.
    • (2007) Biochemistry , vol.46 , pp. 291-305
    • Reddi, A.R.1    Reedy, C.J.2    Mui, S.3    Gibney, B.R.4
  • 17
    • 0034610349 scopus 로고    scopus 로고
    • Heme redox potential control in de novo designed four-alpha- helix bundle proteins
    • Shifman JM, Gibney BR, Sharp RE, Dutton PL. Heme redox potential control in de novo designed four-alpha- helix bundle proteins. Biochemistry 2000;39:14813-14821.
    • (2000) Biochemistry , vol.39 , pp. 14813-14821
    • Shifman, J.M.1    Gibney, B.R.2    Sharp, R.E.3    Dutton, P.L.4
  • 18
  • 19
    • 0344977110 scopus 로고    scopus 로고
    • Bacteriochlorophyll protein maquettes
    • Grimm B, Porra W, Ruediger W, Scheer H, editors, Dorderecht: Kluwer;
    • Noy D, Moser CC, Dutton PL. Bacteriochlorophyll protein maquettes. In: Grimm B, Porra W, Ruediger W, Scheer H, editors. Biochemistry and biophysics of chlorophylls. Dorderecht: Kluwer; 2003.
    • (2003) Biochemistry and biophysics of chlorophylls
    • Noy, D.1    Moser, C.C.2    Dutton, P.L.3
  • 20
    • 0032564310 scopus 로고    scopus 로고
    • Functionalized de novo designed proteins: Mechanism of proton coupling to oxidation/reduction in heme protein maquettes
    • Shifman JM, Moser CC, Kalsbeck WA, Bocian DF, Dutton PL. Functionalized de novo designed proteins: mechanism of proton coupling to oxidation/reduction in heme protein maquettes. Bio-chemistry 1998;37:16815-16827.
    • (1998) Bio-chemistry , vol.37 , pp. 16815-16827
    • Shifman, J.M.1    Moser, C.C.2    Kalsbeck, W.A.3    Bocian, D.F.4    Dutton, P.L.5
  • 21
    • 1842631425 scopus 로고    scopus 로고
    • The HP-1 maquette: From an apoprotein structure to a structured hemoprotein designed to promote redox-coupled proton exchange
    • Huang SS, Koder RL, Lewis M, Wand AJ, Dutton PL. The HP-1 maquette: from an apoprotein structure to a structured hemoprotein designed to promote redox-coupled proton exchange. Proc Natl Acad Sci USA 2004;101:5536-5541.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 5536-5541
    • Huang, S.S.1    Koder, R.L.2    Lewis, M.3    Wand, A.J.4    Dutton, P.L.5
  • 24
    • 0037424025 scopus 로고    scopus 로고
    • Thermodynamic characterization of ferric and ferrous haem binding to a designed four-alpha-helix protein
    • Reedy CJ, Kennedy ML, Gibney BR. Thermodynamic characterization of ferric and ferrous haem binding to a designed four-alpha-helix protein. Chem Commun 2003(5):570-571.
    • (2003) Chem Commun , vol.5 , pp. 570-571
    • Reedy, C.J.1    Kennedy, M.L.2    Gibney, B.R.3
  • 25
    • 0001672040 scopus 로고    scopus 로고
    • Effects of amino acids substitution of hydrophobic residues on haem-binding properties of designed two-alpha-helix peptides
    • Perkin Trans2
    • Sakamoto S, Obataya I, Ueno A, Mihara H. Effects of amino acids substitution of hydrophobic residues on haem-binding properties of designed two-alpha-helix peptides. J Chem Soc Perkin Trans2 1999(10):2059-2069.
    • (1999) J Chem Soc , Issue.10 , pp. 2059-2069
    • Sakamoto, S.1    Obataya, I.2    Ueno, A.3    Mihara, H.4
  • 26
    • 0035104068 scopus 로고    scopus 로고
    • Design, synthesis, and characterization of a novel hemoprotein
    • Xu ZJ, Farid RS. Design, synthesis, and characterization of a novel hemoprotein. Protein Sci 2001;10:236-249.
    • (2001) Protein Sci , vol.10 , pp. 236-249
    • Xu, Z.J.1    Farid, R.S.2
  • 27
    • 24944473851 scopus 로고    scopus 로고
    • Design of amphiphilic protein maquettes: Enhancing maquette functionality through binding of extremely hydrophobic cofactors to lipophilic domains
    • Noy D, Discher BM, Rubtsov IV, Hochstrasser RA, Dutton PL. Design of amphiphilic protein maquettes: enhancing maquette functionality through binding of extremely hydrophobic cofactors to lipophilic domains. Biochemistry 2005;44:12344-12354.
    • (2005) Biochemistry , vol.44 , pp. 12344-12354
    • Noy, D.1    Discher, B.M.2    Rubtsov, I.V.3    Hochstrasser, R.A.4    Dutton, P.L.5
  • 28
    • 13444302392 scopus 로고    scopus 로고
    • Computational de novo design and characterization of a four-helix bundle protein that selectively binds a nonbiological cofactor
    • Cochran FV, Wu SP, Wang W, Nanda V, Saven JG, Therien MJ, DeGrado WF. Computational de novo design and characterization of a four-helix bundle protein that selectively binds a nonbiological cofactor. J Am Chem Soc 2005;127:1346-1347.
    • (2005) J Am Chem Soc , vol.127 , pp. 1346-1347
    • Cochran, F.V.1    Wu, S.P.2    Wang, W.3    Nanda, V.4    Saven, J.G.5    Therien, M.J.6    DeGrado, W.F.7
  • 29
    • 33846121641 scopus 로고    scopus 로고
    • Incorporation of designed extended chromophores into amphiphilic 4-helix bundle peptides for nonlinear optical biomolecular materials
    • Xu T, Wu SP, Miloradovic I, Therien MJ, Blasie JK. Incorporation of designed extended chromophores into amphiphilic 4-helix bundle peptides for nonlinear optical biomolecular materials. Nano Lett 2006;6:2387-2394.
    • (2006) Nano Lett , vol.6 , pp. 2387-2394
    • Xu, T.1    Wu, S.P.2    Miloradovic, I.3    Therien, M.J.4    Blasie, J.K.5
  • 30
    • 33846167452 scopus 로고    scopus 로고
    • Structural studies of amphiphilic 4-helix bundle peptides incorporating designed extended chromophores for nonlinear optical biomolecular materials
    • Strzalka J, Xu T, Tronin A, Wu SP, Miloradovic I, Kuzmenko I, Gog T, Therien MJ, Blasie JK. Structural studies of amphiphilic 4-helix bundle peptides incorporating designed extended chromophores for nonlinear optical biomolecular materials. Nano Lett 2006;6:2395-2405.
    • (2006) Nano Lett , vol.6 , pp. 2395-2405
    • Strzalka, J.1    Xu, T.2    Tronin, A.3    Wu, S.P.4    Miloradovic, I.5    Kuzmenko, I.6    Gog, T.7    Therien, M.J.8    Blasie, J.K.9
  • 35
    • 0034814589 scopus 로고    scopus 로고
    • Characterization of de novo synthesized four-helix bundle proteins with metalloporphyrin cofactors
    • Fahnenschmidt M, Bittl R, Schlodder E, Haehnel W, Lubitz W. Characterization of de novo synthesized four-helix bundle proteins with metalloporphyrin cofactors. Phys Chem Chem Phys 2001;3: 4082-4090.
    • (2001) Phys Chem Chem Phys , vol.3 , pp. 4082-4090
    • Fahnenschmidt, M.1    Bittl, R.2    Schlodder, E.3    Haehnel, W.4    Lubitz, W.5
  • 36
    • 0000933784 scopus 로고
    • A consensus zinc finger peptide-design, high-affinity metal-binding, a pH-de- pendent structure, and a His to Cys sequence variant
    • Krizek BA, Amann BT, Kilfoil VJ, Merkle DL, Berg JM. A consensus zinc finger peptide-design, high-affinity metal-binding, a pH-de- pendent structure, and a His to Cys sequence variant. J Am Chem Soc 1991;113:4518-4523.
    • (1991) J Am Chem Soc , vol.113 , pp. 4518-4523
    • Krizek, B.A.1    Amann, B.T.2    Kilfoil, V.J.3    Merkle, D.L.4    Berg, J.M.5
  • 39
    • 0037648552 scopus 로고    scopus 로고
    • Design of stable alpha-helical arrays from an idealized TPR motif
    • Main ERG, Xiong Y, Cocco MJ, D'Andrea L, Regan L. Design of stable alpha-helical arrays from an idealized TPR motif. Structure 2003;11:497-508.
    • (2003) Structure , vol.11 , pp. 497-508
    • Main, E.R.G.1    Xiong, Y.2    Cocco, M.J.3    D'Andrea, L.4    Regan, L.5
  • 40
    • 0001505616 scopus 로고
    • Ligand variation and metal-ion binding-specificity in zinc finger peptides
    • Krizek BA, Merkle DL, Berg JM. Ligand variation and metal-ion binding-specificity in zinc finger peptides. Inorg Chem 1993;32:937-940.
    • (1993) Inorg Chem , vol.32 , pp. 937-940
    • Krizek, B.A.1    Merkle, D.L.2    Berg, J.M.3
  • 42
    • 0034612192 scopus 로고    scopus 로고
    • Retrostructural analysis of metalloproteins: Application to the design of a minimal model for diiron proteins
    • ombardi A, Summa CM, Geremia S, Randaccio L, Pavone V, DeGrado WF. Retrostructural analysis of metalloproteins: application to the design of a minimal model for diiron proteins. Proc Natl Acad Sci USA 2000;97:6298-6305.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6298-6305
    • ombardi, A.1    Summa, C.M.2    Geremia, S.3    Randaccio, L.4    Pavone, V.5    DeGrado, W.F.6
  • 44
    • 0037117483 scopus 로고    scopus 로고
    • Noncovalent self-assembly of a heterote-trameric diiron protein
    • Marsh ENG, DeGrado WF. Noncovalent self-assembly of a heterote-trameric diiron protein. Proc Natl Acad Sci USA 2002;99:5150-5154.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 5150-5154
    • Marsh, E.N.G.1    DeGrado, W.F.2
  • 46
    • 0036385840 scopus 로고    scopus 로고
    • Computational de novo design, and characterization of an A(2)B(2) diiron protein
    • Summa CM, Rosenblatt MM, Hong JK, Lear JD, DeGrado WF. Computational de novo design, and characterization of an A(2)B(2) diiron protein. J Mol Biol 2002;321:923-938.
    • (2002) J Mol Biol , vol.321 , pp. 923-938
    • Summa, C.M.1    Rosenblatt, M.M.2    Hong, J.K.3    Lear, J.D.4    DeGrado, W.F.5
  • 47
    • 4143131151 scopus 로고    scopus 로고
    • De novo design of catalytic proteins
    • Kaplan J, Degrado WF. De novo design of catalytic proteins. Proc Natl Acad Sci 2004;101:11566-11570.
    • (2004) Proc Natl Acad Sci , vol.101 , pp. 11566-11570
    • Kaplan, J.1    Degrado, W.F.2
  • 49
    • 0035800031 scopus 로고    scopus 로고
    • Factors determining the orientation of axially coordinated imidazoles in heme proteins
    • Zaric SD, Popovic DM, Knapp EW. Factors determining the orientation of axially coordinated imidazoles in heme proteins. Biochemistry 2001;40:7914-7928.
    • (2001) Biochemistry , vol.40 , pp. 7914-7928
    • Zaric, S.D.1    Popovic, D.M.2    Knapp, E.W.3
  • 51
    • 0028205447 scopus 로고
    • Enlarged representative set of protein structures
    • Hobohm U, Sander C. Enlarged representative set of protein structures. Protein Sci 1994;3:522-524.
    • (1994) Protein Sci , vol.3 , pp. 522-524
    • Hobohm, U.1    Sander, C.2
  • 52
    • 0043180474 scopus 로고    scopus 로고
    • PISCES: A protein sequence culling server
    • Wang GL, Dunbrack RL. PISCES: a protein sequence culling server Bioinformatics 2003;19:1589-1591.
    • (2003) Bioinformatics , vol.19 , pp. 1589-1591
    • Wang, G.L.1    Dunbrack, R.L.2
  • 53
    • 0023521842 scopus 로고
    • Analysis of the relationship between side-chain conformation and secondary structure in proteins
    • MacGregor MJ, Islam SA, Sternberg MJE. Analysis of the relationship between side-chain conformation and secondary structure in proteins. J Mol Biol 1987;198:295-310.
    • (1987) J Mol Biol , vol.198 , pp. 295-310
    • MacGregor, M.J.1    Islam, S.A.2    Sternberg, M.J.E.3
  • 54
    • 0034663581 scopus 로고    scopus 로고
    • Side-chain conformational entropy in protein unfolded states
    • Creamer TP. Side-chain conformational entropy in protein unfolded states. Proteins Struct Funct Genet 2000;40:443-450.
    • (2000) Proteins Struct Funct Genet , vol.40 , pp. 443-450
    • Creamer, T.P.1
  • 56
    • 84986512474 scopus 로고    scopus 로고
    • Brooks BR, Bruccoleri RE, Olafson BD, States DJ, Swaminathan S, Karplus M. Charmm-a program for macromolecular energy, minimization, and dynamics calculations. J Comput Chem 1983;4:187- 217.
    • Brooks BR, Bruccoleri RE, Olafson BD, States DJ, Swaminathan S, Karplus M. Charmm-a program for macromolecular energy, minimization, and dynamics calculations. J Comput Chem 1983;4:187- 217.
  • 57
    • 0034663722 scopus 로고    scopus 로고
    • Lovell SC, Word JM, Richardson JS, Richardson DC. The penultimate rotamer library. Proteins Struct Funct Genet 2000;40:389-408.
    • Lovell SC, Word JM, Richardson JS, Richardson DC. The penultimate rotamer library. Proteins Struct Funct Genet 2000;40:389-408.
  • 59
    • 1842523274 scopus 로고    scopus 로고
    • Amino acid propensities are position-dependent throughout the length of alpha-helices
    • Engel DE, DeGrado WF. Amino acid propensities are position-dependent throughout the length of alpha-helices. J Mol Biol 2004;337:1195-1205.
    • (2004) J Mol Biol , vol.337 , pp. 1195-1205
    • Engel, D.E.1    DeGrado, W.F.2
  • 60
    • 0025260032 scopus 로고
    • Side-chain contributions to the stability of alpha-helical structure in peptides
    • Lyu PC, Liff MI, Marky LA, Kallenbach NR. Side-chain contributions to the stability of alpha-helical structure in peptides. Science 1990;250:669-673.
    • (1990) Science , vol.250 , pp. 669-673
    • Lyu, P.C.1    Liff, M.I.2    Marky, L.A.3    Kallenbach, N.R.4
  • 62
    • 0015244817 scopus 로고
    • Empirical protein energy maps
    • Pohl FM. Empirical protein energy maps. Nat New Biol 1971;234:277-279.
    • (1971) Nat New Biol , vol.234 , pp. 277-279
    • Pohl, F.M.1
  • 67
    • 0033573140 scopus 로고    scopus 로고
    • Still a puzzle: Why is haem covalently attached in c-type cytochromes?
    • Barker PD, Ferguson SJ. Still a puzzle: why is haem covalently attached in c-type cytochromes? Structure 1999;7:R281-R290.
    • (1999) Structure , vol.7
    • Barker, P.D.1    Ferguson, S.J.2
  • 69
    • 31544467296 scopus 로고    scopus 로고
    • Cytochrome c: Occurrence and functions
    • Bertini I, Cavallaro G, Rosato A. Cytochrome c: occurrence and functions. Chem Rev 2006;106:90-115.
    • (2006) Chem Rev , vol.106 , pp. 90-115
    • Bertini, I.1    Cavallaro, G.2    Rosato, A.3
  • 71
    • 0028923142 scopus 로고
    • Conserved nonplanar heme distortions in cytochromes-C
    • Hobbs JD, Shelnutt JA. Conserved nonplanar heme distortions in cytochromes-C. J Protein Chem 1995;14:19-25.
    • (1995) J Protein Chem , vol.14 , pp. 19-25
    • Hobbs, J.D.1    Shelnutt, J.A.2
  • 74
    • 0037033048 scopus 로고    scopus 로고
    • Sulfate respiration in Desulfovibrio vulgaris Hildenborough-structure of the 16-heme cytochrome c HmcA at 2.5-Angstrom resolution and a view of its role in transmembrane electron transfer
    • Matias PM, Coelho AV, Valente FMA, Placido D, LeGall J, Xavier AV, Pereira IAC, Carrondo MA. Sulfate respiration in Desulfovibrio vulgaris Hildenborough-structure of the 16-heme cytochrome c HmcA at 2.5-Angstrom resolution and a view of its role in transmembrane electron transfer. J Biol Chem 2002;277:47907-47916.
    • (2002) J Biol Chem , vol.277 , pp. 47907-47916
    • Matias, P.M.1    Coelho, A.V.2    Valente, F.M.A.3    Placido, D.4    LeGall, J.5    Xavier, A.V.6    Pereira, I.A.C.7    Carrondo, M.A.8
  • 75
    • 27744493432 scopus 로고    scopus 로고
    • Multi-heme cytochromes-new structures, new chemistry
    • Mowat CG, Chapman SK. Multi-heme cytochromes-new structures, new chemistry. Dalton Trans 2005(21):3381-3389.
    • (2005) Dalton Trans , vol.21 , pp. 3381-3389
    • Mowat, C.G.1    Chapman, S.K.2
  • 76
    • 0021476470 scopus 로고
    • Calculations of electrostatic interactions in biological-systems and in solutions
    • Warshel A, Russell ST. Calculations of electrostatic interactions in biological-systems and in solutions. Q Rev Biophys 1984;17:283-422.
    • (1984) Q Rev Biophys , vol.17 , pp. 283-422
    • Warshel, A.1    Russell, S.T.2
  • 77
    • 0018129356 scopus 로고
    • Heme exposure as determinate of oxidation-reduction potential of heme proteins
    • Stellwagen E. Heme exposure as determinate of oxidation-reduction potential of heme proteins. Nature 1978;275:73-74.
    • (1978) Nature , vol.275 , pp. 73-74
    • Stellwagen, E.1
  • 78
    • 16244388916 scopus 로고    scopus 로고
    • Probing metal-protein interactions using a de novo design approach
    • Ghosh D, Pecoraro VL. Probing metal-protein interactions using a de novo design approach. Curr Opin Chem Biol 2005;9:97-103.
    • (2005) Curr Opin Chem Biol , vol.9 , pp. 97-103
    • Ghosh, D.1    Pecoraro, V.L.2
  • 79
    • 33748260448 scopus 로고    scopus 로고
    • Stability and folding kinetics of structurally characterized cytochrome c-b(562).Biochemistry
    • Faraone-Mennella J, Tezcan FA, Gray HB, Winkler JR. Stability and folding kinetics of structurally characterized cytochrome c-b(562).Biochemistry 2006;45:10504-10511.
    • (2006) , vol.45 , pp. 10504-10511
    • Faraone-Mennella, J.1    Tezcan, F.A.2    Gray, H.B.3    Winkler, J.R.4
  • 81
    • 0346101796 scopus 로고    scopus 로고
    • A cytochrome b(562) variant with a c-type cytochrome CXXCH heme-binding motif as a probe of the Escherichia coli cytochrome c maturation system
    • Allen JWA, Barker PD, Ferguson SJ. A cytochrome b(562) variant with a c-type cytochrome CXXCH heme-binding motif as a probe of the Escherichia coli cytochrome c maturation system. J Biol Chem 2003;278:52075-52083.
    • (2003) J Biol Chem , vol.278 , pp. 52075-52083
    • Allen, J.W.A.1    Barker, P.D.2    Ferguson, S.J.3
  • 83
    • 0032578852 scopus 로고    scopus 로고
    • Overproduction of the Bradyrhizobium japonicum c-type cytochrome subunits of the cbb(3) oxidase in Escherichia coli
    • Arslan E, Schulz H, Zufferey R, Kunzler P, Thony-Meyer L. Overproduction of the Bradyrhizobium japonicum c-type cytochrome subunits of the cbb(3) oxidase in Escherichia coli. Biochem Biophys Res Commun 1998;251:744-747.
    • (1998) Biochem Biophys Res Commun , vol.251 , pp. 744-747
    • Arslan, E.1    Schulz, H.2    Zufferey, R.3    Kunzler, P.4    Thony-Meyer, L.5
  • 85
    • 33144468377 scopus 로고    scopus 로고
    • Design of a minimal polypeptide unit for bacteriochlorophyll binding and self-assembly based on photosynthetic bacterial light-harvesting proteins
    • Noy D, Dutton PL. Design of a minimal polypeptide unit for bacteriochlorophyll binding and self-assembly based on photosynthetic bacterial light-harvesting proteins. Biochemistry 2006;45: 2103-2113
    • (2006) Biochemistry , vol.45 , pp. 2103-2113
    • Noy, D.1    Dutton, P.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.