메뉴 건너뛰기




Volumn 105, Issue 23, 2008, Pages 7919-7924

Experimental evidence for a link among cupredoxins: Red, blue, and purple copper transformations in nitrous oxide reductase

Author keywords

Blue type 1 copper; Folding; Kinetics; Purple copper CuA; Red type 2 copper

Indexed keywords

COPPER PROTEIN; NITROUS OXIDE REDUCTASE; AZURIN; COPPER; CUPREDOXIN; OXIDOREDUCTASE;

EID: 45849144736     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0711316105     Document Type: Article
Times cited : (40)

References (63)
  • 1
    • 0026411154 scopus 로고
    • Copper protein structures
    • Adman ET (1991) Copper protein structures. Adv Protein Chem 42:145-197.
    • (1991) Adv Protein Chem , vol.42 , pp. 145-197
    • Adman, E.T.1
  • 2
    • 0012953475 scopus 로고    scopus 로고
    • Copper in electron transfer proteins
    • eds Bertini I, Sigel A, Sigel H Dekker, New York, pp
    • Vila AJ, Fernández CO (2001) Copper in electron transfer proteins. Handbook on Metalloproteins, eds Bertini I, Sigel A, Sigel H (Dekker, New York), pp 813-856.
    • (2001) Handbook on Metalloproteins , pp. 813-856
    • Vila, A.J.1    Fernández, C.O.2
  • 4
    • 0002670763 scopus 로고
    • Electron structures of blue copper centers in proteins
    • ed Spiro TG Wiley, New York, pp
    • Gray HB, Solomon EI (1981) Electron structures of blue copper centers in proteins. Copper Proteins, ed Spiro TG (Wiley, New York), pp 1-39.
    • (1981) Copper Proteins , pp. 1-39
    • Gray, H.B.1    Solomon, E.I.2
  • 5
    • 0008684587 scopus 로고
    • Electron transfer processes of blue copper proteins
    • ed Spiro TG Wiley, New York, pp
    • Farver O, Pecht I (1981) Electron transfer processes of blue copper proteins. Copper Proteins, ed Spiro TG (Wiley, New York), pp 151-192.
    • (1981) Copper Proteins , pp. 151-192
    • Farver, O.1    Pecht, I.2
  • 7
    • 0033797723 scopus 로고    scopus 로고
    • Electronic structures of active sites in electron transfer metalloproteins: Contributions to reactivity
    • Solomon EI, Randall DW, Glaser T (2000) Electronic structures of active sites in electron transfer metalloproteins: Contributions to reactivity. Coord Chem Rev 200-202:595-632.
    • (2000) Coord Chem Rev , vol.200-202 , pp. 595-632
    • Solomon, E.I.1    Randall, D.W.2    Glaser, T.3
  • 8
    • 0005811271 scopus 로고    scopus 로고
    • Multi-copper oxidases
    • eds Bertini I, Sigel A, Sigel H Dekker, New York, pp
    • Lindley P (2001) Multi-copper oxidases. Handbook on Metalloproteins, eds Bertini I, Sigel A, Sigel H (Dekker, New York), pp 763-811.
    • (2001) Handbook on Metalloproteins , pp. 763-811
    • Lindley, P.1
  • 9
    • 0001275569 scopus 로고    scopus 로고
    • Plastocyanin
    • eds Messerschmid A, Huber R, Poulos T, Wieghardt K Wiley, Chichester, UK, pp
    • Freeman HC, Guss JM (2001) Plastocyanin. Handbook of Metalloproteins, eds Messerschmid A, Huber R, Poulos T, Wieghardt K (Wiley, Chichester, UK), pp 1153-1169.
    • (2001) Handbook of Metalloproteins , pp. 1153-1169
    • Freeman, H.C.1    Guss, J.M.2
  • 10
    • 2142827168 scopus 로고    scopus 로고
    • Binuclear copper A
    • eds Messerschmid A, Huber R, Poulos T, Wieghardt K Wiley, Chichester, UK, pp
    • Kroneck PMH (2001) Binuclear copper A. Handbook of Metalloproteins, eds Messerschmid A, Huber R, Poulos T, Wieghardt K (Wiley, Chichester, UK), pp 1333-1341.
    • (2001) Handbook of Metalloproteins , pp. 1333-1341
    • Kroneck, P.M.H.1
  • 11
    • 1542378734 scopus 로고    scopus 로고
    • Electronic structures of metal sites in proteins and models: Contributions to function in blue copper proteins
    • Solomon EI, Szilagyi RK, DeBeer George S, Basumallick L (2004) Electronic structures of metal sites in proteins and models: Contributions to function in blue copper proteins. Chem Rev 104:419-458.
    • (2004) Chem Rev , vol.104 , pp. 419-458
    • Solomon, E.I.1    Szilagyi, R.K.2    DeBeer George, S.3    Basumallick, L.4
  • 12
    • 33750317005 scopus 로고    scopus 로고
    • Spectroscopic methods in bioinorganic chemistry: Blue to green to red copper sites
    • Solomon EI (2006) Spectroscopic methods in bioinorganic chemistry: Blue to green to red copper sites. Inorg Chem 45:8012-8025.
    • (2006) Inorg Chem , vol.45 , pp. 8012-8025
    • Solomon, E.I.1
  • 13
    • 0035873518 scopus 로고    scopus 로고
    • Crystal structure of a novel red copper protein from Nitrosomonas europaea
    • Lieberman RL, Arciero DM, Hooper AB, Rosenzweig AC (2001) Crystal structure of a novel red copper protein from Nitrosomonas europaea. Biochemistry 40:5674-5681.
    • (2001) Biochemistry , vol.40 , pp. 5674-5681
    • Lieberman, R.L.1    Arciero, D.M.2    Hooper, A.B.3    Rosenzweig, A.C.4
  • 14
    • 0037065671 scopus 로고    scopus 로고
    • Nitrosocyanin, a red cupredoxin-like protein from Nitrosomonas europaea
    • Arciero DM, Pierce BS, Hendrich MP, Hooper AB (2002) Nitrosocyanin, a red cupredoxin-like protein from Nitrosomonas europaea. Biochemistry 41:1703-1709.
    • (2002) Biochemistry , vol.41 , pp. 1703-1709
    • Arciero, D.M.1    Pierce, B.S.2    Hendrich, M.P.3    Hooper, A.B.4
  • 15
    • 14944379569 scopus 로고    scopus 로고
    • Spectroscopic and density functional studies of the red copper site in nitrosocyanin: Role of the protein in determining active site geometric and electronic structure
    • Basumallick L, et al. (2005) Spectroscopic and density functional studies of the red copper site in nitrosocyanin: Role of the protein in determining active site geometric and electronic structure. J Am Chem Soc 127:3531-3544.
    • (2005) J Am Chem Soc , vol.127 , pp. 3531-3544
    • Basumallick, L.1
  • 16
    • 0028890031 scopus 로고
    • Structure at 2.8 A resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata S, Ostermeier C, Ludwig B, Michel H (1995) Structure at 2.8 A resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature 376:660-669.
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 17
    • 0029652024 scopus 로고
    • Structures of metal sites of oxidized bovine heart cytochrome c oxidase at 2.8 A
    • Tsukihara T, et al. (1995) Structures of metal sites of oxidized bovine heart cytochrome c oxidase at 2.8 A. Science 269:1069-1074.
    • (1995) Science , vol.269 , pp. 1069-1074
    • Tsukihara, T.1
  • 18
    • 0034049124 scopus 로고    scopus 로고
    • Anovel type of catalytic copper cluster in nitrous oxide reductase
    • Brown K, et al. (2000)Anovel type of catalytic copper cluster in nitrous oxide reductase. Nat Struct Biol 7:191-195.
    • (2000) Nat Struct Biol , vol.7 , pp. 191-195
    • Brown, K.1
  • 19
    • 0037270324 scopus 로고    scopus 로고
    • Crystal structure of nitrous oxide reductase from Paracoccus denitrificans at 1.6 A resolution
    • Haltia T, et al. (2003) Crystal structure of nitrous oxide reductase from Paracoccus denitrificans at 1.6 A resolution. Biochem J 369:77-88.
    • (2003) Biochem J , vol.369 , pp. 77-88
    • Haltia, T.1
  • 20
    • 0031456471 scopus 로고    scopus 로고
    • Cell biology and molecular basis of denitrification
    • Zumft WG (1997) Cell biology and molecular basis of denitrification. Microbiol Mol Biology Rev 61:533-616.
    • (1997) Microbiol Mol Biology Rev , vol.61 , pp. 533-616
    • Zumft, W.G.1
  • 21
    • 0013616365 scopus 로고    scopus 로고
    • Cytochrome c oxidase: The key enzyme of aerobic respiration
    • Ostermeier C, Michel H (1997) Cytochrome c oxidase: the key enzyme of aerobic respiration. Transition Met Microb Metab, 311-328.
    • (1997) Transition Met Microb Metab , pp. 311-328
    • Ostermeier, C.1    Michel, H.2
  • 22
    • 0036400025 scopus 로고    scopus 로고
    • Ceruloplasmin metabolism and function
    • Hellman NE, Gitlin JD (2002) Ceruloplasmin metabolism and function. Annu Rev Nutr 22:439-458.
    • (2002) Annu Rev Nutr , vol.22 , pp. 439-458
    • Hellman, N.E.1    Gitlin, J.D.2
  • 24
    • 34548199002 scopus 로고    scopus 로고
    • Redox properties of blue multi-copper oxidases
    • ed Messerschmid A World Scientific, Singapore
    • Kroneck PMH (1997) Redox properties of blue multi-copper oxidases. Multi-Copper Oxidases, ed Messerschmid A (World Scientific, Singapore), 391-407.
    • (1997) Multi-Copper Oxidases , pp. 391-407
    • Kroneck, P.M.H.1
  • 25
    • 0027529952 scopus 로고
    • Evolution of protein complexity: The blue copper-containing oxidases and related proteins
    • Ryden LG, Hunt LT (1993) Evolution of protein complexity: The blue copper-containing oxidases and related proteins. J Mol Evol 36:41-66.
    • (1993) J Mol Evol , vol.36 , pp. 41-66
    • Ryden, L.G.1    Hunt, L.T.2
  • 26
    • 0001826594 scopus 로고    scopus 로고
    • Metal sites in small blue copper proteins, blue copper oxidases and vanadium-containing enzymes
    • Messerschmidt A (1998) Metal sites in small blue copper proteins, blue copper oxidases and vanadium-containing enzymes. Struct Bonding (Berlin) 90:37-68.
    • (1998) Struct Bonding (Berlin) , vol.90 , pp. 37-68
    • Messerschmidt, A.1
  • 27
    • 0030982183 scopus 로고    scopus 로고
    • Copper A of cytochrome c oxidase, a novel, long-embattled, biological electron-transfer site
    • Beinert H (1997) Copper A of cytochrome c oxidase, a novel, long-embattled, biological electron-transfer site. Eur J Biochem 245:521-532.
    • (1997) Eur J Biochem , vol.245 , pp. 521-532
    • Beinert, H.1
  • 29
    • 0018460106 scopus 로고    scopus 로고
    • Steffens GJ, Buse G (1979) Studies on cytochrome c oxidase, IV: Primary structure and function of subunit II. Hoppe-Seyler's Z Physiol Chem 360:613-619.
    • Steffens GJ, Buse G (1979) Studies on cytochrome c oxidase, IV: Primary structure and function of subunit II. Hoppe-Seyler's Z Physiol Chem 360:613-619.
  • 30
    • 0025640889 scopus 로고
    • Structural features of cytochrome oxidase
    • Saraste M (1990) Structural features of cytochrome oxidase. Q Rev Biophys 23:331-366.
    • (1990) Q Rev Biophys , vol.23 , pp. 331-366
    • Saraste, M.1
  • 31
    • 33747235363 scopus 로고    scopus 로고
    • Metal-thiolate bonds in bioinorganic chemistry
    • Solomon EI, Gorelsky SI, Dey A (2006) Metal-thiolate bonds in bioinorganic chemistry. J Comput Chem 27:1415-1428.
    • (2006) J Comput Chem , vol.27 , pp. 1415-1428
    • Solomon, E.I.1    Gorelsky, S.I.2    Dey, A.3
  • 32
    • 0000036806 scopus 로고
    • The redesign of a type 2 into a type 1 copper protein: Construction and characterization of yeast copper, zinc superoxide dismutase mutants
    • Lu Y, Gralla EB, Roe JA, Valentine JS (1992) The redesign of a type 2 into a type 1 copper protein: Construction and characterization of yeast copper, zinc superoxide dismutase mutants. J Am Chem Soc 114:3560-3562.
    • (1992) J Am Chem Soc , vol.114 , pp. 3560-3562
    • Lu, Y.1    Gralla, E.B.2    Roe, J.A.3    Valentine, J.S.4
  • 33
    • 0001267614 scopus 로고    scopus 로고
    • New type 2 copper-cysteinate proteins: Copper site histidine-tocysteine mutants of yeast copper-zinc superoxide dismutase
    • Lu Y, et al. (1996) New type 2 copper-cysteinate proteins: Copper site histidine-tocysteine mutants of yeast copper-zinc superoxide dismutase. Inorg Chem 35:1692-1700.
    • (1996) Inorg Chem , vol.35 , pp. 1692-1700
    • Lu, Y.1
  • 34
    • 0031115714 scopus 로고    scopus 로고
    • Synthesis and studies of Cu(II)-thiolato complexes: Bioinorganic perspectives
    • Mandal S, et al. (1997) Synthesis and studies of Cu(II)-thiolato complexes: Bioinorganic perspectives. Coord Chem Rev 160:191-235.
    • (1997) Coord Chem Rev , vol.160 , pp. 191-235
    • Mandal, S.1
  • 35
    • 0033620365 scopus 로고    scopus 로고
    • Kinetics of copper incorporation into an engineered purple azurin
    • Wang X, Ang MC, Lu Y (1999) Kinetics of copper incorporation into an engineered purple azurin. J Am Chem Soc 121:2947-2948.
    • (1999) J Am Chem Soc , vol.121 , pp. 2947-2948
    • Wang, X.1    Ang, M.C.2    Lu, Y.3
  • 36
    • 0037113884 scopus 로고    scopus 로고
    • A new type 2 copper cysteinate azurin: Involvement of an engineered exposed cysteine in copper binding through internal rearrangement
    • van Amsterdam IMC, et al. (2002) A new type 2 copper cysteinate azurin: Involvement of an engineered exposed cysteine in copper binding through internal rearrangement. J Biol Chem 277:44121-44130.
    • (2002) J Biol Chem , vol.277 , pp. 44121-44130
    • van Amsterdam, I.M.C.1
  • 37
    • 0028989629 scopus 로고
    • Introduction of a CuA site into the blue copper protein amicyanin from Thiobacillus versutus
    • Dennison C, et al. (1995) Introduction of a CuA site into the blue copper protein amicyanin from Thiobacillus versutus. FEBS Lett 365:92-94.
    • (1995) FEBS Lett , vol.365 , pp. 92-94
    • Dennison, C.1
  • 38
    • 0030029979 scopus 로고    scopus 로고
    • Construction and characterization of an azurin analog for the purple copper site in cytochrome c oxidase
    • Hay M, Richards JH, Lu Y (1996) Construction and characterization of an azurin analog for the purple copper site in cytochrome c oxidase. Proc Natl Acad Sci USA 93:461-464.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 461-464
    • Hay, M.1    Richards, J.H.2    Lu, Y.3
  • 39
    • 0001676241 scopus 로고    scopus 로고
    • Spectroscopic characterization of an engineered purple CuA center in azurin
    • Hay MT, et al. (1998) Spectroscopic characterization of an engineered purple CuA center in azurin. Inorg Chem 37:191-198.
    • (1998) Inorg Chem , vol.37 , pp. 191-198
    • Hay, M.T.1
  • 40
    • 27744468899 scopus 로고    scopus 로고
    • Ligand and loop variations at type 1 copper sites: Influence on structure and reactivity
    • Dennison C (2005) Ligand and loop variations at type 1 copper sites: Influence on structure and reactivity. J Chem Soc Dalton Trans 21:3436-3442.
    • (2005) J Chem Soc Dalton Trans , vol.21 , pp. 3436-3442
    • Dennison, C.1
  • 41
    • 1642297119 scopus 로고    scopus 로고
    • Soluble CuA domain of cyanobacterial cytochrome c oxidase
    • Paumann M, et al. (2004) Soluble CuA domain of cyanobacterial cytochrome c oxidase. J Biol Chem 279:10293-10303.
    • (2004) J Biol Chem , vol.279 , pp. 10293-10303
    • Paumann, M.1
  • 42
    • 0029670512 scopus 로고    scopus 로고
    • Water-soluble, recombinant CuA-domain of the cytochrome ba3 subunit II from Thermus thermophilus
    • Slutter CE, et al. (1996) Water-soluble, recombinant CuA-domain of the cytochrome ba3 subunit II from Thermus thermophilus. Biochemistry 35:3387-3395.
    • (1996) Biochemistry , vol.35 , pp. 3387-3395
    • Slutter, C.E.1
  • 43
    • 0027166085 scopus 로고
    • Two cysteines, two histidines, and one methionine are ligands of a binuclear purple copper center
    • Kelly M, et al. (1993) Two cysteines, two histidines, and one methionine are ligands of a binuclear purple copper center. J Biol Chem 268:16781-16787.
    • (1993) J Biol Chem , vol.268 , pp. 16781-16787
    • Kelly, M.1
  • 44
    • 0029102256 scopus 로고
    • Spectroscopic and mutagenesis studies on the CuA centre from the cytochrome-c oxidase complex of Paracoccus denitrificans
    • Farrar JA, et al. (1995) Spectroscopic and mutagenesis studies on the CuA centre from the cytochrome-c oxidase complex of Paracoccus denitrificans. Eur J Biochem 232:294-303.
    • (1995) Eur J Biochem , vol.232 , pp. 294-303
    • Farrar, J.A.1
  • 45
    • 0030615010 scopus 로고    scopus 로고
    • Transformation of the CuA redox site in cytochrome c oxidase into a mononuclear copper center
    • Zickermann V, Wittershagen A, Kolbesen BO, Ludwig B (1997) Transformation of the CuA redox site in cytochrome c oxidase into a mononuclear copper center. Biochemistry 36:3232-3236.
    • (1997) Biochemistry , vol.36 , pp. 3232-3236
    • Zickermann, V.1    Wittershagen, A.2    Kolbesen, B.O.3    Ludwig, B.4
  • 46
    • 0033622166 scopus 로고    scopus 로고
    • Structural investigations of the CuA centre of nitrous oxide reductase from Pseudomonas stutzeri by site-directed mutagenesis and x-ray absorption spectroscopy
    • Charnock JM, et al. (2000) Structural investigations of the CuA centre of nitrous oxide reductase from Pseudomonas stutzeri by site-directed mutagenesis and x-ray absorption spectroscopy. Eur J Biochem 267:1368-1381.
    • (2000) Eur J Biochem , vol.267 , pp. 1368-1381
    • Charnock, J.M.1
  • 47
    • 30944451955 scopus 로고    scopus 로고
    • Spectroscopic characterizations of bridging cysteine ligand variants of an engineered Cu2(SCys)2 CuA azurin
    • Hwang HJ, Nagraj N, Lu Y (2006) Spectroscopic characterizations of bridging cysteine ligand variants of an engineered Cu2(SCys)2 CuA azurin. Inorg Chem 45:102-107.
    • (2006) Inorg Chem , vol.45 , pp. 102-107
    • Hwang, H.J.1    Nagraj, N.2    Lu, Y.3
  • 48
    • 39049122583 scopus 로고    scopus 로고
    • pH dependent copper binding properties of a CuA azurin variant with both bridging cysteines replaced with serines
    • Savelieff MG, Lu Y (2007) pH dependent copper binding properties of a CuA azurin variant with both bridging cysteines replaced with serines. Inorg Chim Acta 361:1087-1094.
    • (2007) Inorg Chim Acta , vol.361 , pp. 1087-1094
    • Savelieff, M.G.1    Lu, Y.2
  • 49
    • 0022336620 scopus 로고
    • Nitrous oxide reductase from denitrifying Pseudomonas perfectomarina: Purification and properties of a novel multicopper enzyme
    • Coyle CL, et al. (1985) Nitrous oxide reductase from denitrifying Pseudomonas perfectomarina: Purification and properties of a novel multicopper enzyme. Eur J Biochem 153:459-467.
    • (1985) Eur J Biochem , vol.153 , pp. 459-467
    • Coyle, C.L.1
  • 50
    • 0024959342 scopus 로고
    • Nitrous oxide reductase from Pseudomonas stutzeri: Redox properties and spectroscopic characterization of different forms of the multicopper enzyme
    • Riester J, Zumft WG, Kroneck PMH (1989) Nitrous oxide reductase from Pseudomonas stutzeri: Redox properties and spectroscopic characterization of different forms of the multicopper enzyme. Eur J Biochem 178:751-762.
    • (1989) Eur J Biochem , vol.178 , pp. 751-762
    • Riester, J.1    Zumft, W.G.2    Kroneck, P.M.H.3
  • 51
    • 0000180764 scopus 로고
    • 2O reductase and in an inactive protein isolated from a mutant deficient in copper-site biosynthesis
    • 2O reductase and in an inactive protein isolated from a mutant deficient in copper-site biosynthesis. Inorg Chem 30:3006-3011.
    • (1991) Inorg Chem , vol.30 , pp. 3006-3011
    • Dooley, D.M.1
  • 52
    • 0041157385 scopus 로고    scopus 로고
    • Alkaline transition of Rhus vernicifera stellacyanin, an unusual blue copper protein
    • Fernandez CO, Sannazzaro AI, Vila AJ (1997) Alkaline transition of Rhus vernicifera stellacyanin, an unusual blue copper protein. Biochemistry 36:10566-10570.
    • (1997) Biochemistry , vol.36 , pp. 10566-10570
    • Fernandez, C.O.1    Sannazzaro, A.I.2    Vila, A.J.3
  • 53
    • 4444276791 scopus 로고    scopus 로고
    • pH-dependent transition between delocalized and trapped valence states of a CuA center and its possible role in proton-coupled electron transfer
    • Hwang HJ, Lu Y (2004) pH-dependent transition between delocalized and trapped valence states of a CuA center and its possible role in proton-coupled electron transfer. Proc Natl Acad Sci USA 101:12842-12847.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 12842-12847
    • Hwang, H.J.1    Lu, Y.2
  • 54
    • 28944434753 scopus 로고    scopus 로고
    • Optical spectroscopic investigation of the alkaline transition in umecyanin from horseradish root
    • Delfino I, et al. (2005) Optical spectroscopic investigation of the alkaline transition in umecyanin from horseradish root. Biochemistry 44:16090-16097.
    • (2005) Biochemistry , vol.44 , pp. 16090-16097
    • Delfino, I.1
  • 55
    • 33644882219 scopus 로고    scopus 로고
    • The alkaline transition of blue copper proteins, Cucumis sativus plastocyanin and Pseudomonas aeruginosa azurin
    • Sakurai T (2006) The alkaline transition of blue copper proteins, Cucumis sativus plastocyanin and Pseudomonas aeruginosa azurin. FEBS Lett 580:1729-1732.
    • (2006) FEBS Lett , vol.580 , pp. 1729-1732
    • Sakurai, T.1
  • 56
    • 0035918556 scopus 로고    scopus 로고
    • pH-induced conformational transition in the soluble CuA domain of Paracoccus denitrificans cytochrome oxidase
    • Gupta S, Warne A, Saraste M, Mazumdar S (2001) pH-induced conformational transition in the soluble CuA domain of Paracoccus denitrificans cytochrome oxidase. Biochemistry 40:6180-6189.
    • (2001) Biochemistry , vol.40 , pp. 6180-6189
    • Gupta, S.1    Warne, A.2    Saraste, M.3    Mazumdar, S.4
  • 57
    • 10044257577 scopus 로고    scopus 로고
    • Role of cofactors in folding of the blue-copper protein azurin
    • Wittung-Stafshede P (2004) Role of cofactors in folding of the blue-copper protein azurin. Inorg Chem 43:7926-7933.
    • (2004) Inorg Chem , vol.43 , pp. 7926-7933
    • Wittung-Stafshede, P.1
  • 58
    • 0030585240 scopus 로고    scopus 로고
    • Structure of a water soluble fragment of the "Rieske" iron-sulfur protein of the bovine heart mitochondrial cytochrome bc1 complex determined by MAD phasing at 1.5 Å resolution
    • Iwata S, Saynovits M, Link TA, Michel H (1996) Structure of a water soluble fragment of the "Rieske" iron-sulfur protein of the bovine heart mitochondrial cytochrome bc1 complex determined by MAD phasing at 1.5 Å resolution. Structure (London) 4:567-579.
    • (1996) Structure (London) , vol.4 , pp. 567-579
    • Iwata, S.1    Saynovits, M.2    Link, T.A.3    Michel, H.4
  • 59
    • 0035067008 scopus 로고    scopus 로고
    • First expression and characterization of a recombinant CuA-containing subunit II from an archaeal terminal oxidase complex
    • Komorowski L, Anemuller S, Schafer G (2001) First expression and characterization of a recombinant CuA-containing subunit II from an archaeal terminal oxidase complex. J Bionenerg Biomembr 33:27-34.
    • (2001) J Bionenerg Biomembr , vol.33 , pp. 27-34
    • Komorowski, L.1    Anemuller, S.2    Schafer, G.3
  • 60
    • 0036820458 scopus 로고    scopus 로고
    • Copper chaperones for cytochrome c oxidase and human disease
    • Hamza I, Gitlin JD (2002) Copper chaperones for cytochrome c oxidase and human disease. J Bionenerg Biomembr 34:381-388.
    • (2002) J Bionenerg Biomembr , vol.34 , pp. 381-388
    • Hamza, I.1    Gitlin, J.D.2
  • 61
    • 0037310426 scopus 로고    scopus 로고
    • Requirements for CuA and Cu-S center assembly of nitrous oxide reductase deduced from complete periplasmic enzyme maturation in the nondenitrifier Pseudomonas putida
    • Wunsch P, et al. (2003) Requirements for CuA and Cu-S center assembly of nitrous oxide reductase deduced from complete periplasmic enzyme maturation in the nondenitrifier Pseudomonas putida. J Bacteriol 185:887-896.
    • (2003) J Bacteriol , vol.185 , pp. 887-896
    • Wunsch, P.1
  • 62
    • 33744466028 scopus 로고    scopus 로고
    • Biogenesis of the bacterial respiratory CuA, Cu-S enzyme nitrous oxide reductase
    • Zumft WG (2005) Biogenesis of the bacterial respiratory CuA, Cu-S enzyme nitrous oxide reductase. J Mol Microbiol Biotechnol 10:154-166.
    • (2005) J Mol Microbiol Biotechnol , vol.10 , pp. 154-166
    • Zumft, W.G.1
  • 63
    • 26644459497 scopus 로고    scopus 로고
    • Human Sco1 and Sco2 function as copper-binding proteins
    • Horng Y-C, et al. (2005) Human Sco1 and Sco2 function as copper-binding proteins. J Biol Chem 280:34113-34122.
    • (2005) J Biol Chem , vol.280 , pp. 34113-34122
    • Horng, Y.-C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.