-
1
-
-
0026410002
-
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
-
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
-
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
-
4
-
-
0001800033
-
Transition-metal storage, transport and biomineralization
-
Theil EC, Raymond KN: Transition-metal storage, transport and biomineralization. In Bmrnorgariic Chemistry. Edited by Bertini I, Gray HB, Lippard SJ, Valentine JS Mill Valley, California: University Science Books; 1994:1-35,
-
(1994)
In Bmrnorgariic Chemistry. Edited by Bertini I, Gray HB, Lippard SJ, Valentine JS Mill Valley, CaliforniaUniversity Science Books
, pp. 1-35
-
-
Theil, E.C.1
Raymond, K.N.2
-
7
-
-
0028889166
-
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
-
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
-
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
-
10
-
-
0030060169
-
-
Hu Z, Spangler NJ, Anderson ME, Xia J, Ludden PW, Lindahl PA, Munck E: Nature of the C-cluster in Ni-containing ca.bon monoxide dehydrogenases. 1 Am Chem Soc 1996, 118:830-845.
-
(1996)
Nature of the C-cluster in Ni-containing Ca.bon Monoxide Dehydrogenases. 1 Am Chem Soc
, vol.118
, pp. 830-845
-
-
Hu, Z.1
Spangler, N.J.2
Anderson, M.E.3
Xia, J.4
Ludden, P.W.5
Lindahl, P.A.6
Munck, E.7
-
11
-
-
0029066353
-
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
-
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
-
13
-
-
0000959987
-
-
Membre RT, McQueen JS, Day VW: Coupling H2 to electron transfer with a 17-electron heterobimetallic hydride: a "redox switch" model for the H2 activating center of hydrogenase. 1 Am Chem Soc 1996, 118:798-803, A RuFe model compound capable of performing, like hydrogenase, the twoelectron oxidation of H2, followed by two one-electron reductions of suitable acceptors.
-
(1996)
Coupling H2 to Electron Transfer with a 17-electron Heterobimetallic Hydridea "Redox Switch" Model for the H2 Activating Center of Hydrogenase. 1 Am Chem Soc
, vol.118
, pp. 798-803
-
-
Membre, R.T.1
McQueen, J.S.2
Day, V.W.3
-
14
-
-
0027912718
-
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
-
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
-
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
-
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
-
19
-
-
33748588332
-
Crystal structure of the active site of ribulose-bisphosphate carboxylase
-
Andersson I, Knight S, Schneider G, Llndqvist Y, Lindqvist T, Branden C-l, Lorimer GH: Crystal structure of the active site of ribulose-bisphosphate carboxylase. Nature 1989, 337:229-234.
-
(1989)
Nature
, vol.337
, pp. 229-234
-
-
Andersson, I.1
Knight, S.2
Schneider, G.3
Llndqvist, Y.4
Lindqvist, T.5
Branden, C.-L.6
Lorimer, G.H.7
-
20
-
-
0029032588
-
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
-
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
-
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
-
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
-
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
38
-
-
0030584657
-
12 radicals are generatedthe crystal structure of methylmalonylcoenzyme a mutase at 2 Å resolution
-
12 radicals are generated: the crystal structure of methylmalonylcoenzyme A mutase at 2 Å resolution, Structure 1996, 4:339-350, The second X-ray structure of a cobalamm enzyme is presented
-
(1996)
Structure
, vol.4
, pp. 339-350
-
-
Mancia, F.1
Keep, N.H.2
Nakagawa, A.3
Leadlay, P.F.4
McSweeney, S.5
Rasmussen, B.6
Bösecke, P.7
Diat, O.8
Evans, P.R.9
-
40
-
-
0030585060
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
51
-
-
0002486262
-
The coordination sphere of iron-sulfur clusterslessons from sitedirected mutagenesis experiments
-
Moulis JM, Datasse V, Golinelli MP, Meyer J, Quinkal I: The coordination sphere of iron-sulfur clusters: lessons from sitedirected mutagenesis experiments. J Biol Inorg Chem 1 996, 1:2-14.
-
J Biol Inorg Chem 1 996
, vol.1
, pp. 2-14
-
-
Moulis, J.M.1
Datasse, V.2
Golinelli, M.P.3
Meyer, J.4
Quinkal, I.5
-
52
-
-
0030585240
-
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
-
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
-
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
|