메뉴 건너뛰기




Volumn 6, Issue 6, 1996, Pages 804-812

Novel metal sites in protein structures

Author keywords

[No Author keywords available]

Indexed keywords

COBALAMIN; COBALT; HYDROGENASE; METAL; METALLOPROTEIN; MOLYBDENUM; NICKEL; NITRITE REDUCTASE; QUINONE DERIVATIVE; SULFITE REDUCTASE; TUNGSTEN; UREASE; VANADIUM;

EID: 0030444792     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(96)80011-X     Document Type: Article
Times cited : (21)

References (54)
  • 1
    • 0026410002 scopus 로고
    • Structural aspects of metal liganding to functional groups in proteins
    • Glusker JP: Structural aspects of metal liganding to functional groups in proteins. Adv Protein C/tem 1991, 42:1-76.
    • (1991) Adv Protein C/tem , vol.42 , pp. 1-76
    • Glusker, J.P.1
  • 2
    • 0028822917 scopus 로고
    • Energised (entatic) states of groups and of secondary structures in proteins and metalloproteins
    • Williams RJP: Energised (entatic) states of groups and of secondary structures in proteins and metalloproteins. Eur j Biochsm 1995, 234:363-381. This review explains a number of useful concepts which may help in understanding the mode of action of metalloproteins
    • (1995) Eur J Biochsm , vol.234 , pp. 363-381
    • Williams, R.J.P.1
  • 3
    • 0004281797 scopus 로고
    • Overview of bioinorganic chemistry
    • Mill Valley, CaliforniaUniversity Science Books
    • Lippard SJ, Berg JM: Overview of bioinorganic chemistry. In Principles of Bioinorganic Chemistry. Mill Valley, California: University Science Books; 1994:1-20.
    • (1994) Principles of Bioinorganic Chemistry. , pp. 1-20
    • Lippard, S.J.1    Berg, J.M.2
  • 6
    • 0001901907 scopus 로고
    • Nickel in biologynickel as an essential trace element in the Bioinorganic Chemistry of Nickel
    • B. Ankel-Fuchs D, Thauer R; Nickel in biology: nickel as an essential trace element In The Bioinorganic Chemistry of Nickel. Edited by Lancaster JR Jr. New York: VCH Publishers, Ire: 1988:93-110.
    • (1988) Edited by Lancaster JR Jr. New YorkVCH Publishers, Ire , pp. 93-110
    • Ankel-Fuchs, D.1    Thauer, R.2
  • 7
    • 0028889166 scopus 로고
    • Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas
    • Volbeda A, Charon MH, Piras C, Hatchikian EC, Frey M, Fonlecilla Camps JC: Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas. Nature 1995, 373:580-587. This paper presents the first structure of a Ni-conlaining enzyme, showing the unexpected presence of a second metal (postulated to be Fe) in the active site.
    • (1995) Nature , vol.373 , pp. 580-587
    • Volbeda, A.1    Charon, M.H.2    Piras, C.3    Hatchikian, E.C.4    Frey, M.5    Fonlecilla Camps, J.C.6
  • 8
    • 0029647957 scopus 로고
    • The crystal structure of urease from Klebsiella asrogenes
    • Jabri c, Carr MB, Hausinger RP, Karplus PA: The crystal structure of urease from Klebsiella asrogenes. Science 1995, 268:998-1004. The structure of the first enzyme to be crystallized! The only hydrolase known to use Ni.
    • (1995) Science , vol.268 , pp. 998-1004
    • Carr, M.B.1    Hausinger, R.P.2    Karplus, P.A.3
  • 9
    • 0028886155 scopus 로고
    • A methylnickel intermediate in a bimetallic mechanism of acetyl-coenzyme a synthesis by anaerobic bacteria
    • Kumar M, Qiu D, Spiro TG, Ragsdale SW: A methylnickel intermediate in a bimetallic mechanism of acetyl-coenzyme A synthesis by anaerobic bacteria. Science 1995, 270:628-630. This paper presents resonance Raman speclroscopic evidence for a Ni-CH3 species in the A cluster of carbon monoxide dehydrogenase,
    • (1995) Science , vol.270 , pp. 628-630
    • Kumar, M.1    Qiu, D.2    Spiro, T.G.3    Ragsdale, S.W.4
  • 11
    • 0029066353 scopus 로고
    • Infrared-detectable groups sense changes in charge density on the nickel center in hydrogenase from Chromatium vinosum
    • Bagley KA, Duin EC, Roseboom W, Albracht SPJ, Woodruff WH Infrared-detectable groups sense changes in charge density on the nickel center in hydrogenase from Chromatium vinosum. Biochemistry 1995, 34:5527-5535. The authors report the existence of unusual, strongly bonded nonprotein ligands sensitive to redox changes of the active site ol NiFe hydrogenase.
    • (1995) Biochemistry , vol.34 , pp. 5527-5535
    • Bagley, K.A.1    Duin, E.C.2    Roseboom, W.3    Albracht, S.P.J.4    Woodruff, W.H.5
  • 12
    • 0029891513 scopus 로고    scopus 로고
    • Similarities in the architecture of the active sites of Ni-hydrogenases and Fehydrogenases detected by means of infrared spectroscopy
    • 2 Van der Spek TM, Arendsen AF, Happe RP, Yun S, Bagley KA, Stufkens DJ, Hagen WR, Albracht SPJ: Similarities in the architecture of the active sites of Ni-hydrogenases and Fehydrogenases detected by means of infrared spectroscopy. Eur J Biochern 199S, 237:629-634. This report shows that the unusual active-site ligands first lound in NiFe hydrogenase [7**,11**] may also occur in Fe-only hydrogenases.
    • Eur J Biochern 199S , vol.237 , pp. 629-634
    • Van Der Spek, T.M.1    Arendsen, A.F.2    Happe, R.P.3    Yun, S.4    Bagley, K.A.5    Stufkens, D.J.6    Hagen, W.R.7    Albracht, S.P.J.8
  • 14
    • 0027912718 scopus 로고
    • A nickel metal hydride battery for electric vehicles
    • Ovshinsky SR, Fetcenko MA, Ross J: A nickel metal hydride battery for electric vehicles. Science 1993, 260:176-181.
    • (1993) Science , vol.260 , pp. 176-181
    • Ovshinsky, S.R.1    Fetcenko, M.A.2    Ross, J.3
  • 15
    • 0029647967 scopus 로고
    • At last -the crystal structure of urease
    • Lippard, SJ: At last -the crystal structure of urease. Science 1995, 268:996-997. A clear evaluation of the importance of structural work on urease from a historical perspective.
    • (1995) Science , vol.268 , pp. 996-997
    • Lippard, S.J.1
  • 16
    • 0002487861 scopus 로고    scopus 로고
    • The active site of Ni-Fe hydrogenasesmodel chemistry and crystallographic results
    • Fontecilla-Camps JC: The active site of Ni-Fe hydrogenases: model chemistry and crystallographic results. J Biot Inorg Chem 1996, 1:91-9B. A first attempt to reconcile the experimental information obtained from model chemistry of the NiFe hydrogenase active site with the crystal structure.
    • (1996) J Biot Inorg Chem , vol.1
    • Fontecilla-Camps, J.C.1
  • 18
    • 0029651190 scopus 로고
    • Requirement of carbon dioxide for in vitro assembly of the urease nickel metallocenter
    • Park IS, Hausinger RP: Requirement of carbon dioxide for in vitro assembly of the urease nickel metallocenter. Science 1995. 267:1156-1158.
    • (1995) Science , vol.267 , pp. 1156-1158
    • Park, I.S.1    Hausinger, R.P.2
  • 20
    • 0029032588 scopus 로고
    • Three-dimensional structure of the binuclear metal center of phosphotriesterase
    • Bennmg MM, Kuo JM, Raushel FM, Holden HM: Three-dimensional structure of the binuclear metal center of phosphotriesterase. Biochemistry 1995, 34:7973-7978. A very interesting structure which looks like urease but contains Zn instead of Ni in the active site.
    • (1995) Biochemistry , vol.34 , pp. 7973-7978
    • Bennmg, M.M.1    Kuo, J.M.2    Raushel, F.M.3    Holden, H.M.4
  • 21
    • 0026748791 scopus 로고
    • Characterization of the zinc metal binding site of bacterial phosphotriesterase
    • Omburo GA, Kuo JM, Mullins LS, Raushel FM: Characterization of the zinc metal binding site of bacterial phosphotriesterase. J BiolChem 1992, 267:13278-13283.
    • (1992) J BiolChem , vol.267 , pp. 13278-13283
    • Omburo, G.A.1    Kuo, J.M.2    Mullins, L.S.3    Raushel, F.M.4
  • 22
    • 0029103501 scopus 로고
    • Freeze-quench resonance Raman spectroscopic evidence for an Fe-CO adduct during acetyl-CoA synthesis and Ni involvement in CO oxidation by carbon monoxide dehydrogenase from Clostridium thermoaceticum
    • Qiu O, Kumar M, Ragsdaie SW, Spiro TG Freeze-quench resonance Raman spectroscopic evidence for an Fe-CO adduct during acetyl-CoA synthesis and Ni involvement in CO oxidation by carbon monoxide dehydrogenase from Clostridium thermoaceticum. 1 Am Chem Soc 1 995, 117:2653-2654. In this paper the use of freeze quenching has allowed the authors to discriminate between CO oxidation and acetyl-CoA synthesis because the two processes occur on different time scales.
    • (1995) 1 Am Chem Soc , vol.117 , pp. 2653-2654
    • Qiu, O.1    Kumar, M.2    Ragsdaie, S.W.3    Spiro, T.G.4
  • 23
    • 0028110887 scopus 로고
    • Organization of clusters and internal electron pathways in CO dehydrogenase from Clostridium thermoaceticum: Relevance to the mechanism of catalysis and cyanide inhibition
    • Anderson ME. Lindahl PA: Organization of clusters and internal electron pathways in CO dehydrogenase from Clostridium thermoaceticum: relevance to the mechanism of catalysis and cyanide inhibition Biochemistry 1994, 33:8702-8711.
    • (1994) Biochemistry , vol.33 , pp. 8702-8711
    • Anderson, M.E.1    Lindahl, P.A.2
  • 24
    • 0028803125 scopus 로고
    • Kovacs JA, Shoner SC, Ellison JJ: Metal-carbon bonds in nature. Science 1995, 270:587-588 This short review discusses and compares C-C bond formation catalyzed by CODH and by synthetic organometallic systems in the light of recent spectroscopic (Raman) studies [9-].
    • (1995) Metal-carbon Bonds in Nature. Science , vol.270 , pp. 587-588
    • Kovacs, J.A.1    Shoner, S.C.2    Ellison, J.J.3
  • 25
    • 0030057102 scopus 로고    scopus 로고
    • Spectroscopic states of the CO oxidation/COj reduction active site of carbon monoxide dehydrogenase and mechanistic implications
    • Anderson ME. Lindah! PA: Spectroscopic states of the CO oxidation/COj reduction active site of carbon monoxide dehydrogenase and mechanistic implications. Biochemistry 1996. 35:8371-8380. The authors propose that the Ni center of the C cluster serves as the mod ulator of the CO/CO2 binding site in CODH
    • (1996) Biochemistry , vol.35 , pp. 8371-8380
    • Anderson, M.E.1    Lindah, P.A.2
  • 26
    • 0026669725 scopus 로고
    • The pterin molybdenum cofactors
    • Rajagopalan KV, Johnson JL: The pterin molybdenum cofactors. J BiolChem 1992, 267:10199-10202.
    • (1992) J BiolChem , vol.267 , pp. 10199-10202
    • Rajagopalan, K.V.1    Johnson, J.L.2
  • 27
    • 0027480074 scopus 로고
    • Identification of molybdopterm as the organic component of the tungsten cofactor in four enzymes from hyperthermophilic archaea
    • Johnson JL, Rajagopalan KV, Mukund S, Adams WWW: Identification of molybdopterm as the organic component of the tungsten cofactor in four enzymes from hyperthermophilic archaea. J Bio! Chem 1995. 268:4848-4852.
    • (1995) J Bio! Chem , vol.268 , pp. 4848-4852
    • Johnson, J.L.1    Rajagopalan, K.V.2    Mukund, S.3    Adams, W.W.W.4
  • 28
    • 0028961901 scopus 로고
    • Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase
    • Chan MK, Mukund S, Kietzin A, Adams MWW, Rees D: Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase. Science 1995, 267:1463-1469. The first enzyme structure containing W and the first comprising the molybdopterin cofactor
    • (1995) Science , vol.267 , pp. 1463-1469
    • Chan, M.K.1    Mukund, S.2    Kietzin, A.3    Adams, M.W.W.4    Rees, D.5
  • 29
    • 0028807552 scopus 로고
    • Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas
    • Rornao MJ, Archer M, Moura I, Moura JJG, LeGall J, Engh R, Schneider M, Hof P, Huber R: Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas. Science 1995, 270:11 70-11 76. The first enzyme structure with Wo bound to the MPT cofactor is presented. 30.
    • (1995) Science , vol.270 , pp. 1170-1176
    • Rornao, M.J.1    Archer, M.2    Moura, I.3    Jjg, M.4    LeGall, J.5    Engh, R.6    Schneider, M.7    Hof, P.8    Huber, R.9
  • 30
    • 0030006891 scopus 로고    scopus 로고
    • Crystal structure of DMSO reductaseredoi-linked changes in molybdopterin coordination
    • Schindelin H. Kisker C, Hilton J, Rajagopalan KV, Rees, DC: Crystal structure of DMSO reductase: redoi-linked changes in molybdopterin coordination. Science 1996, 272:1615-1621. This paper describes the second structure of a Mo-MPT enzyme, showing intriguing structural differences between the oxidized and reduced form of the active site.
    • (1996) Science , vol.272 , pp. 1615-1621
    • Schindelin, H.1    Kisker, C.2    Hilton, J.3    Rajagopalan, K.V.4    Rees, D.C.5
  • 31
    • 0029926237 scopus 로고    scopus 로고
    • X-ray absorption spectroscopy of dimethyl sulfoxide reductase from Rhodobacter sphaeroides
    • George GN, Hilton J, Rajagopalan KV: X-ray absorption spectroscopy of dimethyl sulfoxide reductase from Rhodobacter sphaeroides. J Am Cfiem Soc 1996, 118:1113-1117
    • (1996) J Am Cfiem Soc , vol.118 , pp. 1113-1117
    • George, G.N.1    Hilton, J.2    Rajagopalan, K.V.3
  • 32
    • 0029159268 scopus 로고
    • Direct oxygen transfer in the mechanism of action of Rhodobacter sphaeroides dimethyl sulfoxide reductase
    • Schultz BE, Hille R Holm RH: Direct oxygen transfer in the mechanism of action of Rhodobacter sphaeroides dimethyl sulfoxide reductase. J Am Chem Soc 1995, 117:827-828.
    • (1995) J Am Chem Soc , vol.117 , pp. 827-828
    • Schultz, B.E.1    Hille, R.2    Holm, R.H.3
  • 33
    • 0029890901 scopus 로고    scopus 로고
    • Molybdenum bolsters the bioinorganic brigade
    • Stiefel El: Molybdenum bolsters the bioinorganic brigade. Scrence 1996, 272: 1599-1600. A clearly written review on the importance of Mo and DMSO.
    • (1996) Scrence , vol.272 , pp. 1599-1600
    • Stiefel, El.1
  • 34
    • 0029446692 scopus 로고
    • Vanadium-protein interactions
    • Chastesn ND: Vanadium-protein interactions. Met Ions Biol Syst 1995,31:231-247
    • (1995) Met Ions Biol Syst , vol.31 , pp. 231-247
    • Chastesn, N.D.1
  • 35
    • 0029442216 scopus 로고
    • Vanadium-dependent haloperoxidases
    • Vilter H: Vanadium-dependent haloperoxidases. Met Ions Biol Syst 1995. 31:325-362.
    • (1995) Met Ions Biol Syst , vol.31 , pp. 325-362
    • Vilter, H.1
  • 36
    • 0029446693 scopus 로고
    • Vanadium nitrogenases of Azotobacter
    • Eady RR: Vanadium nitrogenases of Azotobacter. Met tons Biol Syst 1995, 31:363-405,
    • (1995) Met Tons Biol Syst , vol.31 , pp. 363-405
    • Eady, R.R.1
  • 37
    • 0030061093 scopus 로고    scopus 로고
    • X-ray structure of a vanadium-containing enzymechloroperoxidase from the fungus Curvularia inaequalis
    • Messerscfimidt A, Wever R: X-ray structure of a vanadium-containing enzyme: chloroperoxidase from the fungus Curvularia inaequalis. Proc Nat! Acad Sei USA 1996, 93:392-396 The first published struclure of a vanadium containing enzyme.
    • (1996) Proc Nat! Acad Sei USA , vol.93 , pp. 392-396
    • Messerscfimidt, A.1    Wever, R.2
  • 40
    • 0030585060 scopus 로고    scopus 로고
    • The reactivity of B12 cofactorsthe proteins make a difference
    • Ludwig ML, Drennan CL, Matthews RG: The reactivity of B12 cofactors: the proteins make a difference. Structure 1996, 4:505-512. A useful review on the structures of two classes of Bij-dependent enzymes.
    • (1996) Structure , vol.4 , pp. 505-512
    • Ludwig, M.L.1    Drennan, C.L.2    Matthews, R.G.3
  • 41
    • 0000725566 scopus 로고
    • Structure of the 5,6-dimethylbenzimidazoyl-cobalamine coenzyme
    • Lenhert PG, Hodgkm DC: Structure of the 5,6-dimethylbenzimidazoyl-cobalamine coenzyme. Nature 1961, 192:937-938.
    • (1961) Nature , vol.192 , pp. 937-938
    • Lenhert, P.G.1    Hodgkm, D.C.2
  • 42
    • 0028809514 scopus 로고
    • Sulfite reductase structure at 1.6 Åevolution and catalysis for reduction of inorganic anions
    • Crane BR, Siegel LM, Getzoff ED: Sulfite reductase structure at 1.6 Å: evolution and catalysis for reduction of inorganic anions. Science 1995, 270:59-67. A very detailed analysis of the siroheme containing active site is given.
    • (1995) Science , vol.270 , pp. 59-67
    • Crane, B.R.1    Siegel, L.M.2    Getzoff, E.D.3
  • 43
    • 0022926562 scopus 로고
    • The heme and Fe4S,j cluster in the crystallographic structure of Escherichia colt sulfite reductase
    • McRee DE, Richardson DC. Richardson JS, Siegel LM: The heme and Fe4S,j cluster in the crystallographic structure of Escherichia colt sulfite reductase. J Btol Cbem 1986, 261:10277-10281
    • (1986) J Btol Cbem , vol.261 , pp. 10277-10281
    • McRee, D.E.1    Richardson, D.C.2    Richardson, J.S.3    Siegel, L.M.4
  • 44
    • 0029158963 scopus 로고
    • Sulfite reductaseactive site residues are 'noncatalytic'. Comparison of reaction energetics for enzymeand siroheme-catalyzed reduction of 'inorganic substrates
    • Soriano A, Cowan JA: Sulfite reductase: active site residues are 'noncatalytic'. Comparison of reaction energetics for enzymeand siroheme-catalyzed reduction of 'inorganic substrates, j Am Chem Soc 1995, 117:4724-4725. The authors show that the remarkable activity of the isolated siroheme co factor is comparable to that of siroheme-containing enzymes.
    • (1995) J Am Chem Soc , vol.117 , pp. 4724-4725
    • Soriano, A.1    Cowan, J.A.2
  • 46
    • 0028783950 scopus 로고
    • 2- Bound and with type II copper depleted
    • 2- bound and with type II copper depleted. J Biol Chem 1995, 270:27458-27474. The structural characterization of many states of copper-nitrite reductase which show only minor differences.
    • (1995) J Biol Chem , vol.270 , pp. 27458-27474
    • Adman, E.T.1    Godden, J.W.2    Turley, S.3
  • 47
    • 0027914978 scopus 로고
    • Electronic structure contributions to function in bioinorganic chemistry
    • Solomon El, Lowery MD: Electronic structure contributions to function in bioinorganic chemistry. Science 1993, 259:1575-1581.
    • (1993) Science , vol.259 , pp. 1575-1581
    • Solomon, El.1    Lowery, M.D.2
  • 48
    • 0029645871 scopus 로고
    • Crystal structure of a quinoenzymecopper amine oxidase of Escherichia coli at 2A resolution
    • Parsons MR, Convery MA, Wilmot CM, Yadav KDS, Blakeley V, .. Corner AS, Phillips SEV, WcPherson Mi, Knowles PF: Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2A resolution. Structure 1995, 3:11 71 -1184. This paper presents first structures of a TPQ containing enzyme, reported in both an active and an inactive form, which show intriguing differences.
    • (1995) Structure , vol.3 , pp. 1171-1184
    • Parsons, M.R.1    Convery, M.A.2    Wilmot, C.M.3    Yadav, K.D.S.4    Blakeley, V.5    Corner, A.S.6    Phillips, S.E.V.7    WcPherson, M.8    Knowles, P.F.9
  • 49
    • 0028244179 scopus 로고
    • Mu DQuinoenzymes in biology
    • Klinman JP. Mu D: Quinoenzymes in biology. Anna Rev Brachem 1994,63:299-344.
    • (1994) Anna Rev Brachem , vol.63 , pp. 299-344
    • Klinman, J.P.1
  • 50
    • 0029645895 scopus 로고
    • Copper amine oxidasea novel use for a tyrosine
    • Fnntecave M, Eklund H: Copper amine oxidase: a novel use for a tyrosine. Structure 1995, 3:1127-1129. The authors propose a plausible mechanism for the formation of the activesite topa quinone (TPQ), which involves a tyrosyl radical.
    • (1995) Structure , vol.3 , pp. 1127-1129
    • Fnntecave, M.1    Eklund, H.2
  • 52
    • 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 Aresolution
    • Iwata S, Saynovits M, Link TA, Michel H: 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 Aresolution. Structure 1996, 4:567-579. This paper presents the second crystal structure example, after hydrogenase, of histidine binding to an IFe-S] cluster.
    • (1996) Structure , vol.4 , pp. 567-579
    • Iwata, S.1    Saynovits, M.2    Link, T.A.3    Michel, H.4
  • 53
    • 0026244229 scopus 로고
    • MOLSCRIPTa program to produce both detailed and schematic plots of protein structures
    • Kraulis P: MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl dystallogr 1991, 24:946-950.
    • (1991) J Appl Dystallogr , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 54
    • 0030481349 scopus 로고    scopus 로고
    • Structure of the [NiFe] hydrogenase active siteevidence for biologically uncommon Fe ligands
    • in press
    • Volbeda A, Garcin E, Piras C, De Lacey AL, Fernandez VM, Hatchikian EC, Frey M, Fontecilla-Camps JC: Structure of the [NiFe] hydrogenase active site: evidence for biologically uncommon Fe ligands. J Am Chem Soc 199B, in press. New cryslallographic and IR spectroscopic results show the presence of three intrisic redox-sensitive diatomic ligands at the active site of the enryme
    • J Am Chem Soc 199B
    • Volbeda, A.1    Garcin, E.2    Piras, C.3    De Lacey, A.L.4    Fernandez, V.M.5    Hatchikian, E.C.6    Frey, M.7    Fontecilla-Camps, J.C.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.