-
1
-
-
35449002141
-
De novo design and synthesis of heme proteins
-
Elsevier
-
Gibney BR, Dutton PL: De novo design and synthesis of heme proteins. In Advances in Inorganic Chemistry, vol 51. Elsevier; 2001:409-455.
-
(2001)
Advances in Inorganic Chemistry
, vol.51
, pp. 409-455
-
-
Gibney, B.R.1
Dutton, P.L.2
-
2
-
-
0035471138
-
Engineering novel metalloproteins: Design of metal-binding sites into native protein scaffolds
-
Lu Y., Berry S.M., Pfister T.D. Engineering novel metalloproteins: design of metal-binding sites into native protein scaffolds. Chem Rev. 101:2001;3047-3080.
-
(2001)
Chem Rev
, vol.101
, pp. 3047-3080
-
-
Lu, Y.1
Berry, S.M.2
Pfister, T.D.3
-
3
-
-
0037388040
-
Biological inorganic chemistry at the beginning of the 21st century
-
Gray H.B. Biological inorganic chemistry at the beginning of the 21st century. Proc Natl Acad Sci USA. 100:2003;3563-3568.
-
(2003)
Proc Natl Acad Sci USA
, vol.100
, pp. 3563-3568
-
-
Gray, H.B.1
-
4
-
-
0014251790
-
Metalloenzymes: The entatic nature of their active sites
-
Vallee B.L., Williams R.J.P. Metalloenzymes: the entatic nature of their active sites. Proc Natl Acad Sci USA. 59:1968;498-505.
-
(1968)
Proc Natl Acad Sci USA
, vol.59
, pp. 498-505
-
-
Vallee, B.L.1
Williams, R.J.P.2
-
5
-
-
0028822917
-
Energised (entatic) states of groups and of secondary structures in proteins and metalloproteins
-
Williams R.J.P. Energised (entatic) states of groups and of secondary structures in proteins and metalloproteins. Eur J Biochem. 234:1995;363-381.
-
(1995)
Eur J Biochem
, vol.234
, pp. 363-381
-
-
Williams, R.J.P.1
-
6
-
-
0037126693
-
Structure-based thermodynamic analysis of a coupled metal binding-protein folding reaction involving a zinc finger peptide
-
Blasie C.A., Berg J.M. Structure-based thermodynamic analysis of a coupled metal binding-protein folding reaction involving a zinc finger peptide. Biochemistry. 41:2002;15068-15073.
-
(2002)
Biochemistry
, vol.41
, pp. 15068-15073
-
-
Blasie, C.A.1
Berg, J.M.2
-
7
-
-
0032835617
-
De novo design and structural characterization of proteins and metalloproteins
-
DeGrado W.F., Summa C.M., Pavone V., Nastri F., Lombardi A. De novo design and structural characterization of proteins and metalloproteins. Annu Rev Biochem. 68:1999;779-819.
-
(1999)
Annu Rev Biochem
, vol.68
, pp. 779-819
-
-
DeGrado, W.F.1
Summa, C.M.2
Pavone, V.3
Nastri, F.4
Lombardi, A.5
-
8
-
-
0038752617
-
Computational design of receptor and sensor proteins with novel functions
-
A computational pre-screen of a huge virtual library enabled these authors to address a sequence library of MBP that is too big to be actually made with current technology. They challenged the virtual library with a variety of small molecules to identify library members that would have altered binding specificity in the substrate-binding pocket. A limited set of protein mutants was all that was required to show that the protein could be tuned to bind specifically the small molecules used in the screen. Not a metalloprotein nor a solution to the protein folding problem, but a tour de force leading the way forward.
-
Looger L.L., Dwyer M.A., Smith J.J., Hellinga H.W. Computational design of receptor and sensor proteins with novel functions. Nature. 423:2003;185-190 A computational pre-screen of a huge virtual library enabled these authors to address a sequence library of MBP that is too big to be actually made with current technology. They challenged the virtual library with a variety of small molecules to identify library members that would have altered binding specificity in the substrate-binding pocket. A limited set of protein mutants was all that was required to show that the protein could be tuned to bind specifically the small molecules used in the screen. Not a metalloprotein nor a solution to the protein folding problem, but a tour de force leading the way forward.
-
(2003)
Nature
, vol.423
, pp. 185-190
-
-
Looger, L.L.1
Dwyer, M.A.2
Smith, J.J.3
Hellinga, H.W.4
-
11
-
-
0037388092
-
Preorganization of molecular binding sites in designed di-iron proteins
-
A landmark in the de novo design of metalloproteins, describing the NMR structure of the apo-form of a designed, dinuclear metal-binding helical bundle. This work nicely completes a design cycle, the authors having already presented structures of the holo-form of these proteins (see [13,14]).
-
Maglio O., Nastri F., Pavone V., Lombardi A., DeGrado W.F. Preorganization of molecular binding sites in designed di-iron proteins. Proc Natl Acad Sci USA. 100:2003;3772-3777 A landmark in the de novo design of metalloproteins, describing the NMR structure of the apo-form of a designed, dinuclear metal-binding helical bundle. This work nicely completes a design cycle, the authors having already presented structures of the holo-form of these proteins (see [13,14]).
-
(2003)
Proc Natl Acad Sci USA
, vol.100
, pp. 3772-3777
-
-
Maglio, O.1
Nastri, F.2
Pavone, V.3
Lombardi, A.4
DeGrado, W.F.5
-
12
-
-
0034612192
-
Inaugural article: Retrostructural analysis of metalloproteins: Application to the design of a minimal model for di-iron proteins
-
Lombardi A., Summa C.M., Geremia S., Randaccio L., Pavone V., DeGrado W.F. Inaugural article: retrostructural analysis of metalloproteins: application to the design of a minimal model for di-iron proteins. Proc Natl Acad Sci USA. 97:2000;6298-6305.
-
(2000)
Proc Natl Acad Sci USA
, vol.97
, pp. 6298-6305
-
-
Lombardi, A.1
Summa, C.M.2
Geremia, S.3
Randaccio, L.4
Pavone, V.5
DeGrado, W.F.6
-
13
-
-
0035956544
-
Toward the de novo design of a catalytically active helix bundle: A substrate-accessible carboxylate-bridged dinuclear metal center
-
Di Costanzo L., Wade H., Geremia S., Randaccio L., Pavone V., DeGrado W.F., Lombardi A. Toward the de novo design of a catalytically active helix bundle: a substrate-accessible carboxylate-bridged dinuclear metal center. J Am Chem Soc. 123:2001;12749-12757.
-
(2001)
J Am Chem Soc
, vol.123
, pp. 12749-12757
-
-
Di Costanzo, L.1
Wade, H.2
Geremia, S.3
Randaccio, L.4
Pavone, V.5
DeGrado, W.F.6
Lombardi, A.7
-
14
-
-
0344751050
-
Sliding helix and change of coordination geometry in a model di-MnII protein
-
DeGrado W.F., Di Costanzo L., Geremia S., Lombardi A., Pavone V., Randaccio L. Sliding helix and change of coordination geometry in a model di-MnII protein. Angew Chem Int Ed Engl. 42:2003;417-420.
-
(2003)
Angew Chem Int Ed Engl
, vol.42
, pp. 417-420
-
-
DeGrado, W.F.1
Di Costanzo, L.2
Geremia, S.3
Lombardi, A.4
Pavone, V.5
Randaccio, L.6
-
15
-
-
0036385840
-
Computational de novo design, and characterization of an A(2)B(2) di-iron protein
-
The importance of computational design is highlighted in this next generation of designed helical bundles, where the aim is to remove some of the symmetry (and consequently simplicity) in the molecules. An extremely thorough characterisation of the resulting (real) molecule leaves one convinced of its properties. It also reveals that the time taken to complete the design cycle is dropping dramatically.
-
Summa C.M., Rosenblatt M.M., Hong J.K., Lear J.D., DeGrado W.F. Computational de novo design, and characterization of an A(2)B(2) di-iron protein. J Mol Biol. 321:2002;923-938 The importance of computational design is highlighted in this next generation of designed helical bundles, where the aim is to remove some of the symmetry (and consequently simplicity) in the molecules. An extremely thorough characterisation of the resulting (real) molecule leaves one convinced of its properties. It also reveals that the time taken to complete the design cycle is dropping dramatically.
-
(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
-
16
-
-
0037470553
-
X-ray structure of a Maquette scaffold
-
This is a crystal structure of the apo-form of a designed haem-binding helical bundle that has already been shown to be a good binder of iron(III) haem. I get the impression that the result is not entirely what the authors had wanted, but this hugely important work is crucial to our understanding of haem-binding sites and of how to design and engineer them. Designing well-ordered haem sites is far more challenging than achieving simple binding of 'bare' metal ions.
-
Huang S.S., Gibney B.R., Stayrook S.E., Dutton P.L., Lewis M. X-ray structure of a Maquette scaffold. J Mol Biol. 326:2003;1219-1225 This is a crystal structure of the apo-form of a designed haem-binding helical bundle that has already been shown to be a good binder of iron(III) haem. I get the impression that the result is not entirely what the authors had wanted, but this hugely important work is crucial to our understanding of haem-binding sites and of how to design and engineer them. Designing well-ordered haem sites is far more challenging than achieving simple binding of 'bare' metal ions.
-
(2003)
J Mol Biol
, vol.326
, pp. 1219-1225
-
-
Huang, S.S.1
Gibney, B.R.2
Stayrook, S.E.3
Dutton, P.L.4
Lewis, M.5
-
17
-
-
0030936312
-
Design of a unique protein scaffold for maquettes
-
Gibney B.R., Rabanal F., Skalicky J.J., Wand A.J., Dutton P.L. Design of a unique protein scaffold for maquettes. J Am Chem Soc. 119:1997;2323-2324.
-
(1997)
J Am Chem Soc
, vol.119
, pp. 2323-2324
-
-
Gibney, B.R.1
Rabanal, F.2
Skalicky, J.J.3
Wand, A.J.4
Dutton, P.L.5
-
18
-
-
0032584314
-
Effect of four helix bundle topology on heme binding and redox properties
-
Gibney B.R., Rabanal F., Reddy K.S., Dutton P.L. Effect of four helix bundle topology on heme binding and redox properties. Biochemistry. 37:1998;4635-4643.
-
(1998)
Biochemistry
, vol.37
, pp. 4635-4643
-
-
Gibney, B.R.1
Rabanal, F.2
Reddy, K.S.3
Dutton, P.L.4
-
19
-
-
0034809985
-
Model hemoprotein reduction potentials: The effects of histidine to iron coordination equilibrium
-
Kennedy M.L., Silchenko S., Houndonougbo N., Gibney B.R., Dutton P.L., Rodgers K.R., Benson D.R. Model hemoprotein reduction potentials: the effects of histidine to iron coordination equilibrium. J Am Chem Soc. 123:2001;4635-4636.
-
(2001)
J Am Chem Soc
, vol.123
, pp. 4635-4636
-
-
Kennedy, M.L.1
Silchenko, S.2
Houndonougbo, N.3
Gibney, B.R.4
Dutton, P.L.5
Rodgers, K.R.6
Benson, D.R.7
-
20
-
-
0034610349
-
Heme redox potential control in de novo designed four-α-helix bundle proteins
-
Shifman J.M., Gibney B.R., Sharp R.E., Dutton P.L. Heme redox potential control in de novo designed four-α-helix bundle proteins. Biochemistry. 39:2000;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
-
21
-
-
0031991838
-
Sequence-specific resonance assignments for a designed four-α-helix bundle protein
-
Skalicky J.J., Bieber R.J., Gibney B.R., Rabanal F., Dutton P.L., Wand A.J. Sequence-specific resonance assignments for a designed four-α-helix bundle protein. J Biomol NMR. 11:1998;227-228.
-
(1998)
J Biomol NMR
, vol.11
, pp. 227-228
-
-
Skalicky, J.J.1
Bieber, R.J.2
Gibney, B.R.3
Rabanal, F.4
Dutton, P.L.5
Wand, A.J.6
-
22
-
-
0037197665
-
The C terminus of apocytochrome b562 undergoes fast motions and slow exchange among ordered conformations resembling the folded state
-
D'Amelio N., Bonvin A.M., Czisch M., Barker P., Kaptein R. The C terminus of apocytochrome b562 undergoes fast motions and slow exchange among ordered conformations resembling the folded state. Biochemistry. 41:2002;5505-5514.
-
(2002)
Biochemistry
, vol.41
, pp. 5505-5514
-
-
D'Amelio, N.1
Bonvin, A.M.2
Czisch, M.3
Barker, P.4
Kaptein, R.5
-
23
-
-
0028367050
-
Solution structure of apocytochrome b562
-
Feng Y., Sligar S.G., Wand A.J. Solution structure of apocytochrome b562. Nature. 1:1994;30-34.
-
(1994)
Nature
, vol.1
, pp. 30-34
-
-
Feng, Y.1
Sligar, S.G.2
Wand, A.J.3
-
24
-
-
0037424025
-
-
Reedy CJ, Kennedy ML, Gibney BR: Thermodynamic characterization of ferric and ferrous haem binding to a designed four-α-helix protein. Chem Commun (Camb) 2003:570-571.
-
Reedy CJ, Kennedy ML, Gibney BR: Thermodynamic characterization of ferric and ferrous haem binding to a designed four-α-helix protein. Chem Commun (Camb) 2003:570-571.
-
-
-
-
26
-
-
85081196326
-
-
Moore GR, Pettigrew GW: Cytochromes c: Evolutionary, Structural and Physiochemical Aspects. Berlin: Springer-Verlag; 1990.
-
Moore GR, Pettigrew GW: Cytochromes c: Evolutionary, Structural and Physiochemical Aspects. Berlin: Springer-Verlag; 1990.
-
-
-
-
27
-
-
0034684238
-
Nitrophorins and related antihemostatic lipocalins from Rhodnius prolixus and other blood-sucking arthropods
-
Montfort W.R., Weichsel A., Andersen J.F. Nitrophorins and related antihemostatic lipocalins from Rhodnius prolixus and other blood-sucking arthropods. Biochim Biophys Acta. 1482:2000;110-118.
-
(2000)
Biochim Biophys Acta
, vol.1482
, pp. 110-118
-
-
Montfort, W.R.1
Weichsel, A.2
Andersen, J.F.3
-
28
-
-
0032979703
-
The crystal structure of HasA, a hemophore secreted by Serratia marcescens
-
Arnoux P., Haser R., Izadi N., Lecroisey A., Delepierre M., Wandersman C., Czjzek M. The crystal structure of HasA, a hemophore secreted by Serratia marcescens. Nature Struct Biol. 6:1999;516-520.
-
(1999)
Nature Struct Biol
, vol.6
, pp. 516-520
-
-
Arnoux, P.1
Haser, R.2
Izadi, N.3
Lecroisey, A.4
Delepierre, M.5
Wandersman, C.6
Czjzek, M.7
-
29
-
-
0032825215
-
Crystal structure of hemopexin reveals a novel high-affinity heme site formed between two β-propeller domains
-
Paoli M., Anderson B.F., Baker H.M., Morgan W.T., Smith A., Baker E.N. Crystal structure of hemopexin reveals a novel high-affinity heme site formed between two β-propeller domains. Nat Struct Biol. 6:1999;926-931.
-
(1999)
Nat Struct Biol
, vol.6
, pp. 926-931
-
-
Paoli, M.1
Anderson, B.F.2
Baker, H.M.3
Morgan, W.T.4
Smith, A.5
Baker, E.N.6
-
30
-
-
0011045635
-
-
Morgan WT, Smith A: Binding and transport of iron-porphyrins by hemopexin. In Advances in Inorganic Chemistry, vol 51. Elsevier; 2001:205-241.
-
Morgan WT, Smith A: Binding and transport of iron-porphyrins by hemopexin. In Advances in Inorganic Chemistry, vol 51. Elsevier; 2001:205-241.
-
-
-
-
32
-
-
0028587376
-
Construction of a bisaquo heme enzyme and binding by exogenous ligands
-
McRee D.E., Jensen G.M., Fitzgerald M.M., Siegel H.A., Goodin D.B. Construction of a bisaquo heme enzyme and binding by exogenous ligands. Proc Natl Acad Sci USA. 91:1994;12847-12851.
-
(1994)
Proc Natl Acad Sci USA
, vol.91
, pp. 12847-12851
-
-
McRee, D.E.1
Jensen, G.M.2
Fitzgerald, M.M.3
Siegel, H.A.4
Goodin, D.B.5
-
34
-
-
0033573140
-
Still a puzzle: Why is haem covalently attached in c-type cytochromes?
-
Barker P.D., Ferguson S.J. Still a puzzle: why is haem covalently attached in c-type cytochromes? Structure Fold Des. 7:1999;R281-R290.
-
(1999)
Structure Fold Des
, vol.7
-
-
Barker, P.D.1
Ferguson, S.J.2
-
35
-
-
0035471139
-
Peptide-based heme-protein models
-
Lombardi A., Nastri F., Pavone V. Peptide-based heme-protein models. Chem Rev. 101:2001;3165-3189.
-
(2001)
Chem Rev
, vol.101
, pp. 3165-3189
-
-
Lombardi, A.1
Nastri, F.2
Pavone, V.3
-
36
-
-
0034684772
-
Design, synthesis and peroxidase-like activity of three α-helix proteins covalently bound to heme
-
Obataya I., Kotaki T., Sakamoto S., Ueno A., Mihara H. Design, synthesis and peroxidase-like activity of three α-helix proteins covalently bound to heme. Bioorg Med Chem Lett. 10:2000;2719-2722.
-
(2000)
Bioorg Med Chem Lett
, vol.10
, pp. 2719-2722
-
-
Obataya, I.1
Kotaki, T.2
Sakamoto, S.3
Ueno, A.4
Mihara, H.5
-
37
-
-
0035824613
-
The cytochrome c fold can be attained from a compact apo state by occupancy of a nascent heme binding site
-
Wain R., Pertinhez T.A., Tomlinson E.J., Hong L., Dobson C.M., Ferguson S.J., Smith L.J. The cytochrome c fold can be attained from a compact apo state by occupancy of a nascent heme binding site. J Biol Chem. 276:2001;45813-45817.
-
(2001)
J Biol Chem
, vol.276
, pp. 45813-45817
-
-
Wain, R.1
Pertinhez, T.A.2
Tomlinson, E.J.3
Hong, L.4
Dobson, C.M.5
Ferguson, S.J.6
Smith, L.J.7
-
38
-
-
0035826571
-
Proof of principle in a de novo designed protein maquette: An allosterically regulated, charge-activated conformational switch in a tetra-α-helix bundle
-
Grosset A.M., Gibney B.R., Rabanal F., Moser C.C., Dutton P.L. Proof of principle in a de novo designed protein maquette: an allosterically regulated, charge-activated conformational switch in a tetra-α-helix bundle. Biochemistry. 40:2001;5474-5487.
-
(2001)
Biochemistry
, vol.40
, pp. 5474-5487
-
-
Grosset, A.M.1
Gibney, B.R.2
Rabanal, F.3
Moser, C.C.4
Dutton, P.L.5
-
39
-
-
0026321752
-
Construction of new ligand binding sites in proteins of known structure. II. Grafting of a buried transition metal binding site into Escherichia coli thioredoxin
-
Hellinga H.W., Caradonna J.P., Richards F.M. Construction of new ligand binding sites in proteins of known structure. II. Grafting of a buried transition metal binding site into Escherichia coli thioredoxin. J Mol Biol. 222:1991;787-803.
-
(1991)
J Mol Biol
, vol.222
, pp. 787-803
-
-
Hellinga, H.W.1
Caradonna, J.P.2
Richards, F.M.3
-
40
-
-
0026335211
-
Construction of new ligand binding sites in proteins of known structure. I. Computer-aided modeling of sites with pre-defined geometry
-
Hellinga H.W., Richards F.M. Construction of new ligand binding sites in proteins of known structure. I. Computer-aided modeling of sites with pre-defined geometry. J Mol Biol. 222:1991;763-785.
-
(1991)
J Mol Biol
, vol.222
, pp. 763-785
-
-
Hellinga, H.W.1
Richards, F.M.2
-
42
-
-
0037022813
-
Converting a maltose receptor into a nascent binuclear copper oxygenase by computational design
-
Computational design again results in the relatively facile generation of a dinuclear copper site, which the authors have thoroughly characterised and which shows some catalytic oxygenase activity. Although MBP might seem an unlikely scaffold for a metalloprotein, the interesting feature of this system is that the authors can manipulate the conformation so that the position of the metal ligands can be attenuated.
-
Benson D.E., Haddy A.E., Hellinga H.W. Converting a maltose receptor into a nascent binuclear copper oxygenase by computational design. Biochemistry. 41:2002;3262-3269 Computational design again results in the relatively facile generation of a dinuclear copper site, which the authors have thoroughly characterised and which shows some catalytic oxygenase activity. Although MBP might seem an unlikely scaffold for a metalloprotein, the interesting feature of this system is that the authors can manipulate the conformation so that the position of the metal ligands can be attenuated.
-
(2002)
Biochemistry
, vol.41
, pp. 3262-3269
-
-
Benson, D.E.1
Haddy, A.E.2
Hellinga, H.W.3
-
43
-
-
0034863015
-
Manipulation of ligand binding affinity by exploitation of conformational coupling
-
Marvin J.S., Hellinga H.W. Manipulation of ligand binding affinity by exploitation of conformational coupling. Nat Struct Biol. 8:2001;795-798.
-
(2001)
Nat Struct Biol
, vol.8
, pp. 795-798
-
-
Marvin, J.S.1
Hellinga, H.W.2
-
44
-
-
0035942160
-
Conversion of a maltose receptor into a zinc biosensor by computational design
-
Marvin J.S., Hellinga H.W. Conversion of a maltose receptor into a zinc biosensor by computational design. Proc Natl Acad Sci USA. 98:2001;4955-4960.
-
(2001)
Proc Natl Acad Sci USA
, vol.98
, pp. 4955-4960
-
-
Marvin, J.S.1
Hellinga, H.W.2
-
46
-
-
0035979773
-
Design of bioelectronic interfaces by exploiting hinge-bending motions in proteins
-
Benson D.E., Conrad D.W., de Lorimer R.M., Trammell S.A., Hellinga H.W. Design of bioelectronic interfaces by exploiting hinge-bending motions in proteins. Science. 293:2001;1641-1644.
-
(2001)
Science
, vol.293
, pp. 1641-1644
-
-
Benson, D.E.1
Conrad, D.W.2
De Lorimer, R.M.3
Trammell, S.A.4
Hellinga, H.W.5
-
47
-
-
21844445818
-
-
Kurz A, Halliwell CM, Davis JJ, Hill HAO, Canters GW: A fullerene-modified protein. Chem Commun (Camb) 1998:433-434.
-
Kurz A, Halliwell CM, Davis JJ, Hill HAO, Canters GW: A fullerene-modified protein. Chem Commun (Camb) 1998:433-434.
-
-
-
-
48
-
-
0036318488
-
Design, synthesis and photophysical properties of C-60-modified proteins
-
Murakami H., Matsumoto R., Okusa Y., Sagara T., Fujitsuka M., Ito O., Nakashima N. Design, synthesis and photophysical properties Of C-60-modified proteins. J Mater Chem. 12:2002;2026-2033.
-
(2002)
J Mater Chem
, vol.12
, pp. 2026-2033
-
-
Murakami, H.1
Matsumoto, R.2
Okusa, Y.3
Sagara, T.4
Fujitsuka, M.5
Ito, O.6
Nakashima, N.7
-
49
-
-
0034595703
-
Direct comparison of electron transfer properties of two distinct semisynthetic triads with non-protein based triad: Unambiguous experimental evidences on protein matrix effects
-
Hu Y.Z., Takashima H., Tsukiji S., Shinkai S., Nagamune T., Oishi S., Hamachi I. Direct comparison of electron transfer properties of two distinct semisynthetic triads with non-protein based triad: unambiguous experimental evidences on protein matrix effects. Chemistry. 6:2000;1907-1916.
-
(2000)
Chemistry
, vol.6
, pp. 1907-1916
-
-
Hu, Y.Z.1
Takashima, H.2
Tsukiji, S.3
Shinkai, S.4
Nagamune, T.5
Oishi, S.6
Hamachi, I.7
-
50
-
-
12244309473
-
Preparation of artificial metalloenzymes by insertion of chromium(III) Schiff base complexes into apomyoglobin mutants
-
Ohashi M., Koshiyama T., Ueno T., Yanase M., Fujii H., Watanabe Y. Preparation of artificial metalloenzymes by insertion of chromium(III) Schiff base complexes into apomyoglobin mutants. Angew Chem Int Ed Engl. 42:2003;1005-1008.
-
(2003)
Angew Chem Int Ed Engl
, vol.42
, pp. 1005-1008
-
-
Ohashi, M.1
Koshiyama, T.2
Ueno, T.3
Yanase, M.4
Fujii, H.5
Watanabe, Y.6
-
51
-
-
0034704959
-
562 variants: A library for examining redox potential evolution
-
562 variants: a library for examining redox potential evolution. Biochemistry. 39:2000;6075-6082.
-
(2000)
Biochemistry
, vol.39
, pp. 6075-6082
-
-
Springs, S.L.1
Bass, S.E.2
McLendon, G.L.3
-
52
-
-
0037006983
-
A multigeneration analysis of Cytochrome b(562) redox variants: Evolutionary strategies for modulating redox potential revealed using a library approach
-
This comprehensive analysis, including structural analysis, of proteins selected from hierarchical libraries of a naturally evolved haem protein reveals the subtle factors influencing the properties of haem sites.
-
Springs S.L., Bass S.E., Bowman G., Nodelman I., Schutt C.E., McLendon G.L. A multigeneration analysis of Cytochrome b(562) redox variants: evolutionary strategies for modulating redox potential revealed using a library approach. Biochemistry. 41:2002;4321-4328 This comprehensive analysis, including structural analysis, of proteins selected from hierarchical libraries of a naturally evolved haem protein reveals the subtle factors influencing the properties of haem sites.
-
(2002)
Biochemistry
, vol.41
, pp. 4321-4328
-
-
Springs, S.L.1
Bass, S.E.2
Bowman, G.3
Nodelman, I.4
Schutt, C.E.5
McLendon, G.L.6
-
53
-
-
0032583439
-
Effects of ligation and folding on reduction potentials of heme proteins
-
Tezcan F.A., Winkler J.R., Gray H.B. Effects of ligation and folding on reduction potentials of heme proteins. J Am Chem Soc. 120:1998;13383-13388.
-
(1998)
J Am Chem Soc
, vol.120
, pp. 13383-13388
-
-
Tezcan, F.A.1
Winkler, J.R.2
Gray, H.B.3
-
54
-
-
0037021299
-
Examining reactivity and specificity of cytochrome c peroxidase by using combinatorial mutagenesis
-
Wilming M., Iffland A., Tafelmeyer P., Arrivoli C., Saudan C., Johnsson K. Examining reactivity and specificity of cytochrome c peroxidase by using combinatorial mutagenesis. Chembiochem. 3:2002;1097-1104.
-
(2002)
Chembiochem
, vol.3
, pp. 1097-1104
-
-
Wilming, M.1
Iffland, A.2
Tafelmeyer, P.3
Arrivoli, C.4
Saudan, C.5
Johnsson, K.6
-
55
-
-
0037423522
-
-
Wilson JR, Caruana DJ, Gilardi G: Engineering redox functions in a nucleic acid binding protein. Chem Commun (Camb) 2003:356-357.
-
Wilson JR, Caruana DJ, Gilardi G: Engineering redox functions in a nucleic acid binding protein. Chem Commun (Camb) 2003:356-357.
-
-
-
-
56
-
-
0037040613
-
Molecular basis of proton motive force generation: Structure of formate dehydrogenase-N
-
Jormakka M., Tornroth S., Byrne B., Iwata S. Molecular basis of proton motive force generation: structure of formate dehydrogenase-N. Science. 295:2002;1863-1868.
-
(2002)
Science
, vol.295
, pp. 1863-1868
-
-
Jormakka, M.1
Tornroth, S.2
Byrne, B.3
Iwata, S.4
-
57
-
-
0348150715
-
Architecture of succinate dehydrogenase and reactive oxygen species generation
-
Yankovskaya V., Horsefield R., Tornroth S., Luna-Chavez C., Miyoshi H., Leger C., Byrne B., Cecchini G., Iwata S. Architecture of succinate dehydrogenase and reactive oxygen species generation. Science. 299:2003;700-704.
-
(2003)
Science
, vol.299
, pp. 700-704
-
-
Yankovskaya, V.1
Horsefield, R.2
Tornroth, S.3
Luna-Chavez, C.4
Miyoshi, H.5
Leger, C.6
Byrne, B.7
Cecchini, G.8
Iwata, S.9
-
58
-
-
0036905068
-
The crystal structure of the hexadeca-heme cytochrome Hmc and a structural model of its complex with cytochrome c(3)
-
Czjzek M., ElAntak L., Zamboni V., Morelli X., Dolla A., Guerlesquin F., Bruschi M. The crystal structure of the hexadeca-heme cytochrome Hmc and a structural model of its complex with cytochrome c(3). Structure (Camb). 10:2002;1677-1686.
-
(2002)
Structure (Camb)
, vol.10
, pp. 1677-1686
-
-
Czjzek, M.1
ElAntak, L.2
Zamboni, V.3
Morelli, X.4
Dolla, A.5
Guerlesquin, F.6
Bruschi, M.7
-
59
-
-
0034641342
-
Interruption and time-resolution of catalysis by a flavoenzyme using fast scan protein film voltammetry
-
Jones A.K., Camba R., Reid G.A., Chapman S.K., Armstrong F.A. Interruption and time-resolution of catalysis by a flavoenzyme using fast scan protein film voltammetry. J Am Chem Soc. 122:2000;6494-6495.
-
(2000)
J Am Chem Soc
, vol.122
, pp. 6494-6495
-
-
Jones, A.K.1
Camba, R.2
Reid, G.A.3
Chapman, S.K.4
Armstrong, F.A.5
-
60
-
-
0037157123
-
Electron-transfer mechanisms through biological redox chains in multicenter enzymes
-
This is an insightful analysis of electron transfer mechanisms in multicofactor enzymes using state-of-the-art protein electrochemical methods. Convincing evidence, for me at least, that nature has made conducting wires, a feature that many metalloprotein engineers would wish to design.
-
Jeuken L.J.C., Jones A.K., Chapman S.K., Cecchini G., Armstrong F.A. Electron-transfer mechanisms through biological redox chains in multicenter enzymes. J Am Chem Soc. 124:2002;5702-5713 This is an insightful analysis of electron transfer mechanisms in multicofactor enzymes using state-of-the-art protein electrochemical methods. Convincing evidence, for me at least, that nature has made conducting wires, a feature that many metalloprotein engineers would wish to design.
-
(2002)
J Am Chem Soc
, vol.124
, pp. 5702-5713
-
-
Jeuken, L.J.C.1
Jones, A.K.2
Chapman, S.K.3
Cecchini, G.4
Armstrong, F.A.5
-
61
-
-
0037389858
-
A redox switch in CopC: An intriguing copper trafficking protein that binds copper(I) and copper(II) at different sites
-
A high-quality NMR structure of an intriguing copper-binding protein that shows how nature can select for copper (I) or copper (II) using completely different sites that construct different coordination spheres. This should become the subject of many an undergraduate lecture in bioinorganic chemistry for years to come.
-
Arnesano F., Banci L., Bertini I., Mangani S., Thompsett A.R. A redox switch in CopC: An intriguing copper trafficking protein that binds copper(I) and copper(II) at different sites. Proc Natl Acad Sci USA. 100:2003;3814-3819 A high-quality NMR structure of an intriguing copper-binding protein that shows how nature can select for copper (I) or copper (II) using completely different sites that construct different coordination spheres. This should become the subject of many an undergraduate lecture in bioinorganic chemistry for years to come.
-
(2003)
Proc Natl Acad Sci USA
, vol.100
, pp. 3814-3819
-
-
Arnesano, F.1
Banci, L.2
Bertini, I.3
Mangani, S.4
Thompsett, A.R.5
-
62
-
-
0037993832
-
Transition metal speciation in the cell: Insights from the chemistry of metal ion receptors
-
Finney L.A., O'Halloran T.V. Transition metal speciation in the cell: Insights from the chemistry of metal ion receptors. Science. 300:2003;931-936.
-
(2003)
Science
, vol.300
, pp. 931-936
-
-
Finney, L.A.1
O'Halloran, T.V.2
-
64
-
-
0037374820
-
Ni-Zn-[Fe4-S4] and Ni-Ni-[Fe4-S4] clusters in closed and open subunits of acetyl-CoA synthase/carbon monoxide dehydrogenase
-
Darnault C., Volbeda A., Kim E.J., Legrand P., Vernede X., Lindahl P.A., Fontecilla-Camps J.C. Ni-Zn-[Fe4-S4] and Ni-Ni-[Fe4-S4] clusters in closed and open subunits of acetyl-CoA synthase/carbon monoxide dehydrogenase. Nat Struct Biol. 10:2003;271-279.
-
(2003)
Nat Struct Biol
, vol.10
, pp. 271-279
-
-
Darnault, C.1
Volbeda, A.2
Kim, E.J.3
Legrand, P.4
Vernede, X.5
Lindahl, P.A.6
Fontecilla-Camps, J.C.7
-
65
-
-
0037727718
-
Acetate C-C bond formation and decomposition in the anaerobic world: The structure of a central enzyme and its key active-site metal cluster
-
Grahame D.A. Acetate C-C bond formation and decomposition in the anaerobic world: the structure of a central enzyme and its key active-site metal cluster. Trends Biochem Sci. 28:2003;221-224.
-
(2003)
Trends Biochem Sci
, vol.28
, pp. 221-224
-
-
Grahame, D.A.1
-
66
-
-
0031570299
-
Crystal structure of nitrile hydratase reveals a novel iron centre in a novel fold
-
Huang W., Jia J., Cummings J., Nelson M., Schneider G., Lindqvist Y. Crystal structure of nitrile hydratase reveals a novel iron centre in a novel fold. Structure. 5:1997;691-699.
-
(1997)
Structure
, vol.5
, pp. 691-699
-
-
Huang, W.1
Jia, J.2
Cummings, J.3
Nelson, M.4
Schneider, G.5
Lindqvist, Y.6
-
67
-
-
0037497251
-
Chaperonin-mediated stabilisation and ATP-triggered release of semiconductor nanoparticles
-
Ishii Y., Kinbara K., Ishida Y., Ishii N., Okochi M., Yohda M., Aida T. Chaperonin-mediated stabilisation and ATP-triggered release of semiconductor nanoparticles. Nature. 423:2003;628-632.
-
(2003)
Nature
, vol.423
, pp. 628-632
-
-
Ishii, Y.1
Kinbara, K.2
Ishida, Y.3
Ishii, N.4
Okochi, M.5
Yohda, M.6
Aida, T.7
|