-
1
-
-
0034625310
-
Dimethylsulfoxide reductase: An enzyme capable of catalysis with either molybdenum or tungsten at the active site
-
Stewart, L. J.; Bailey, S.; Bennett, B.; Charnock, J. M.; Garner, C. D.; McAlpine, A. S. Dimethylsulfoxide reductase: an enzyme capable of catalysis with either molybdenum or tungsten at the active site J. Mol. Biol. 2000, 299, 593-600
-
(2000)
J. Mol. Biol.
, vol.299
, pp. 593-600
-
-
Stewart, L.J.1
Bailey, S.2
Bennett, B.3
Charnock, J.M.4
Garner, C.D.5
McAlpine, A.S.6
-
2
-
-
0037349399
-
Structural genomics of proteins involved in copper homeostasis
-
Banci, L.; Rosato, A. Structural genomics of proteins involved in copper homeostasis Acc. Chem. Res. 2003, 36, 215-221
-
(2003)
Acc. Chem. Res.
, vol.36
, pp. 215-221
-
-
Banci, L.1
Rosato, A.2
-
3
-
-
0344420004
-
The many highways for intracellular trafficking of metals
-
Luk, E.; Jensen, L. T.; Culotta, V. C. The many highways for intracellular trafficking of metals J. Biol. Inorg. Chem. 2003, 8, 803-809
-
(2003)
J. Biol. Inorg. Chem.
, vol.8
, pp. 803-809
-
-
Luk, E.1
Jensen, L.T.2
Culotta, V.C.3
-
4
-
-
21544440823
-
Order of stability of metal complexes
-
Irving, H.; Williams, R. J. P. Order of stability of metal complexes Nature 1948, 162, 746-747
-
(1948)
Nature
, vol.162
, pp. 746-747
-
-
Irving, H.1
Williams, R.J.P.2
-
6
-
-
57649207910
-
How do bacterial cells ensure that metalloproteins get the correct metal
-
Waldron, K. J.; Robinson, N. J. How do bacterial cells ensure that metalloproteins get the correct metal Nat. Rev. Microbiol. 2009, 7, 25-35
-
(2009)
Nat. Rev. Microbiol.
, vol.7
, pp. 25-35
-
-
Waldron, K.J.1
Robinson, N.J.2
-
7
-
-
37349071628
-
-
University Science Books: Sausalito, CA
-
Bertini, I.; Gray, H. B.; Stiefel, E. I.; Valentine, J. S. Biological Inorganic Chemistry: Structure and Reactivity; University Science Books: Sausalito, CA, 2007.
-
(2007)
Biological Inorganic Chemistry: Structure and Reactivity
-
-
Bertini, I.1
Gray, H.B.2
Stiefel, E.I.3
Valentine, J.S.4
-
8
-
-
34547911052
-
Chemistry of acetyl transfer by histone modifying enzymes: Structure, mechanism, and implications for effector design
-
Hodawadekar, S. C.; Marmorstein, R. Chemistry of acetyl transfer by histone modifying enzymes: structure, mechanism, and implications for effector design Oncogene 2007, 26, 5528-5540
-
(2007)
Oncogene
, vol.26
, pp. 5528-5540
-
-
Hodawadekar, S.C.1
Marmorstein, R.2
-
9
-
-
57749170458
-
The many roles of histone deacetylases in development and physiology: Implications for disease and therapy
-
Haberland, M.; Montgomery, R. L.; Olson, E. N. The many roles of histone deacetylases in development and physiology: implications for disease and therapy Nat. Rev. Genet. 2009, 10, 32-42
-
(2009)
Nat. Rev. Genet.
, vol.10
, pp. 32-42
-
-
Haberland, M.1
Montgomery, R.L.2
Olson, E.N.3
-
10
-
-
33947313218
-
HDACs, histone deacetylation, and gene transcription: From molecular biology to cancer therapeutics
-
Gallinari, P.; di Marco, S.; Jones, P.; Pallaoro, M.; Steinkuhler, C. HDACs, histone deacetylation, and gene transcription: from molecular biology to cancer therapeutics Cell Res. 2007, 17, 195-211
-
(2007)
Cell Res.
, vol.17
, pp. 195-211
-
-
Gallinari, P.1
Di Marco, S.2
Jones, P.3
Pallaoro, M.4
Steinkuhler, C.5
-
11
-
-
77953664293
-
Structures of metal-substituted human histone deacetylase 8 provide mechanistic inferences on biological function
-
Dowling, D. P.; Gattis, S. G.; Fierke, C. A.; Christianson, D. W. Structures of metal-substituted human histone deacetylase 8 provide mechanistic inferences on biological function Biochemistry 2010, 49, 5048-5056
-
(2010)
Biochemistry
, vol.49
, pp. 5048-5056
-
-
Dowling, D.P.1
Gattis, S.G.2
Fierke, C.A.3
Christianson, D.W.4
-
12
-
-
33646548638
-
Catalytic activity and inhibition of human histone deacetylase 8 is dependent on the identity of the active site metal ion
-
Gantt, S. L.; Gattis, S. G.; Fierke, C. A. Catalytic activity and inhibition of human histone deacetylase 8 is dependent on the identity of the active site metal ion Biochemistry 2006, 45, 6170-6178
-
(2006)
Biochemistry
, vol.45
, pp. 6170-6178
-
-
Gantt, S.L.1
Gattis, S.G.2
Fierke, C.A.3
-
14
-
-
0014514280
-
Jack bean urease (EC 3.5.1.5). Demonstration of a carbamoyl-transfer reaction and inhibition by hydroxamic acids
-
Blakeley, R. L.; Hinds, J. A.; Kunze, H. E.; Webb, E. C.; Zerner, B. Jack bean urease (EC 3.5.1.5). Demonstration of a carbamoyl-transfer reaction and inhibition by hydroxamic acids Biochemistry 1969, 8, 1991-2000
-
(1969)
Biochemistry
, vol.8
, pp. 1991-2000
-
-
Blakeley, R.L.1
Hinds, J.A.2
Kunze, H.E.3
Webb, E.C.4
Zerner, B.5
-
15
-
-
0035374653
-
Living dangerously: How Helicobacter pylori survives in the human stomach
-
Montecucco, C.; Rappuoli, R. Living dangerously: How Helicobacter pylori survives in the human stomach Nat. Rev. Mol. Cell Biol. 2001, 2, 457-466
-
(2001)
Nat. Rev. Mol. Cell Biol.
, vol.2
, pp. 457-466
-
-
Montecucco, C.1
Rappuoli, R.2
-
16
-
-
0016846997
-
Jack bean urease (EC 3.5.1.5). A metalloenzyme. A simple biological role for nickel?
-
Dixon, N. E.; Gazzola, C.; Blackeley, R.; Zerner, B. Jack bean urease (EC 3.5.1.5). A metalloenzyme. A simple biological role for nickel? J. Am. Chem. Soc. 1975, 97, 4131-4132
-
(1975)
J. Am. Chem. Soc.
, vol.97
, pp. 4131-4132
-
-
Dixon, N.E.1
Gazzola, C.2
Blackeley, R.3
Zerner, B.4
-
17
-
-
84899519638
-
Nonredox nickel enzymes
-
Maroney, A. J.; Ciurli, S. Nonredox nickel enzymes Chem. Rev. 2014, 114, 4206-4228
-
(2014)
Chem. Rev.
, vol.114
, pp. 4206-4228
-
-
Maroney, A.J.1
Ciurli, S.2
-
19
-
-
33747235366
-
Quantum mechanical and molecular dynamics simulations of ureases and Zn β-lactamases
-
Estiu, G.; Suárez, D.; Merz, K. M. Quantum mechanical and molecular dynamics simulations of ureases and Zn β-lactamases J. Comput. Chem. 2006, 27, 1240-1262
-
(2006)
J. Comput. Chem.
, vol.27
, pp. 1240-1262
-
-
Estiu, G.1
Suárez, D.2
Merz, K.M.3
-
20
-
-
84866004794
-
Why urease is a di-nickel enzyme whereas the CcrA β-lactamase is a di-zinc enzyme
-
Valdez, C. E.; Alexandrova, A. N. Why urease is a di-nickel enzyme whereas the CcrA β-lactamase is a di-zinc enzyme J. Phys. Chem. B 2012, 116, 10649-10656
-
(2012)
J. Phys. Chem. B
, vol.116
, pp. 10649-10656
-
-
Valdez, C.E.1
Alexandrova, A.N.2
-
21
-
-
0025358925
-
Helicobacter mustelae -associated gastritis in ferrets: An animal model of Helicobacter pylori gastritis in humans
-
Fox, J. G.; Correa, P.; Taylor, N. S.; Lee, A.; Otto, G.; Murphy, J. C.; Rose, R. Helicobacter mustelae -associated gastritis in ferrets: An animal model of Helicobacter pylori gastritis in humans Gastroenterology 1990, 99, 352-361
-
(1990)
Gastroenterology
, vol.99
, pp. 352-361
-
-
Fox, J.G.1
Correa, P.2
Taylor, N.S.3
Lee, A.4
Otto, G.5
Murphy, J.C.6
Rose, R.7
-
22
-
-
0035132939
-
Emergence of diverse Helicobacter species in the pathogenesis of gastric and enterohepatic diseases
-
Solnick, J.; Schauer, D. B. Emergence of diverse Helicobacter species in the pathogenesis of gastric and enterohepatic diseases Clin. Microbiol. Rev. 2001, 14, 59-97
-
(2001)
Clin. Microbiol. Rev.
, vol.14
, pp. 59-97
-
-
Solnick, J.1
Schauer, D.B.2
-
23
-
-
80051977680
-
Iron-containing urease in a pathogenic bacterium
-
Carter, E. L.; Tronrud, D. E.; Taber, S. R.; Karplus, P. A.; Hausinger, R. P. Iron-containing urease in a pathogenic bacterium Proc. Natl. Acad. Sci. U. S. A. 2011, 108, 13095-13099
-
(2011)
Proc. Natl. Acad. Sci. U. S. A.
, vol.108
, pp. 13095-13099
-
-
Carter, E.L.1
Tronrud, D.E.2
Taber, S.R.3
Karplus, P.A.4
Hausinger, R.P.5
-
24
-
-
18544384019
-
Oxidation of tartaric acid in presence of iron
-
Fenton, H. J. H. Oxidation of tartaric acid in presence of iron J. Chem. Soc., Trans. 1894, 65, 899-911
-
(1894)
J. Chem. Soc., Trans.
, vol.65
, pp. 899-911
-
-
Fenton, H.J.H.1
-
25
-
-
21544467350
-
A new enzyme of general occurrence in organisms
-
Loew, O. A new enzyme of general occurrence in organisms Science 1900, 11, 701-702
-
(1900)
Science
, vol.11
, pp. 701-702
-
-
Loew, O.1
-
26
-
-
79953896180
-
Iron enzyme ribulose-5-phosphate 3-epimerase in Escherichia coli is rapidly damaged by hydrogen peroxide but can be protected by manganese
-
Sobota, J. M.; Imlay, J. A. Iron enzyme ribulose-5-phosphate 3-epimerase in Escherichia coli is rapidly damaged by hydrogen peroxide but can be protected by manganese Proc. Natl. Acad. Sci. U. S. A. 2011, 108, 5402-5407
-
(2011)
Proc. Natl. Acad. Sci. U. S. A.
, vol.108
, pp. 5402-5407
-
-
Sobota, J.M.1
Imlay, J.A.2
-
27
-
-
79953850801
-
The alternative aerobic ribonucleotide reductase of Escherichia coli, NdrEF, is a manganese-dependent enzyme that enables cell replication during periods of iron starvation
-
Martin, J. E.; Imlay, J. A. The alternative aerobic ribonucleotide reductase of Escherichia coli, NdrEF, is a manganese-dependent enzyme that enables cell replication during periods of iron starvation Mol. Microbiol. 2011, 80, 319-334
-
(2011)
Mol. Microbiol.
, vol.80
, pp. 319-334
-
-
Martin, J.E.1
Imlay, J.A.2
-
28
-
-
0027177564
-
From RNA to DNA, why so many ribonucleotide reductases?
-
Reichard, P. From RNA to DNA, why so many ribonucleotide reductases? Science 1993, 260, 1773-1777
-
(1993)
Science
, vol.260
, pp. 1773-1777
-
-
Reichard, P.1
-
29
-
-
0032539852
-
Ribonucleotide reductases in the twenty-first century
-
Stubbe, J. Ribonucleotide reductases in the twenty-first century Proc. Natl. Acad. Sci. U. S. A. 1998, 95, 2723-2724
-
(1998)
Proc. Natl. Acad. Sci. U. S. A.
, vol.95
, pp. 2723-2724
-
-
Stubbe, J.1
-
30
-
-
77956653207
-
Structural basis for activation of class Ib ribonucleotide reductase
-
Boal, A. K.; Cotruvo, J. A., Jr.; Stubbe, J.; Rosentzweig, A. C. Structural basis for activation of class Ib ribonucleotide reductase Science 2010, 329, 1526-1530
-
(2010)
Science
, vol.329
, pp. 1526-1530
-
-
Boal, A.K.1
Cotruvo, J.A.2
Stubbe, J.3
Rosentzweig, A.C.4
-
31
-
-
84896690021
-
Streptococcus sanguinis Class Ib ribonucleotide reductase. High activity with both iron and manganese cofactors and structural insights
-
Makhlynets, O.; Boal, A. K.; Rhodes, D. V.; Kitten, T.; Rosenzweig, A. C.; Stubbe, J. Streptococcus sanguinis Class Ib ribonucleotide reductase. High activity with both iron and manganese cofactors and structural insights J. Biol. Chem. 2014, 28, 6259-6272
-
(2014)
J. Biol. Chem.
, vol.28
, pp. 6259-6272
-
-
Makhlynets, O.1
Boal, A.K.2
Rhodes, D.V.3
Kitten, T.4
Rosenzweig, A.C.5
Stubbe, J.6
-
32
-
-
84860732135
-
The dimanganese(II) site of Baccilus subtilis class Ib ribonucleotide reductase
-
Boal, A. K.; Cotruvo, J. A.; Stubbe, J.; Rosenzweig, A. C. The dimanganese(II) site of Baccilus subtilis class Ib ribonucleotide reductase Biochemistry 2012, 51, 3861-3871
-
(2012)
Biochemistry
, vol.51
, pp. 3861-3871
-
-
Boal, A.K.1
Cotruvo, J.A.2
Stubbe, J.3
Rosenzweig, A.C.4
-
33
-
-
84856718630
-
Evidence that the β subunit of chlamydia trachomatic ribonucleotide reductase is active with the manganase ion of its manganese(IV)/iroon(III) cofactor in site 1
-
Dassama, L. M. K.; Boal, A. K.; Krebs, C.; Rosenzweig, A. C.; Bollinger, J. M., Jr Evidence that the β subunit of chlamydia trachomatic ribonucleotide reductase is active with the manganase ion of its manganese(IV)/iroon(III) cofactor in site 1 J. Am. Chem. Soc. 2012, 134, 2520-2523
-
(2012)
J. Am. Chem. Soc.
, vol.134
, pp. 2520-2523
-
-
Dassama, L.M.K.1
Boal, A.K.2
Krebs, C.3
Rosenzweig, A.C.4
Bollinger, J.M.5
-
34
-
-
0344834199
-
Iron-sulfur clusters in enzymes: Themes and variations
-
Cammack, R. Iron-sulfur clusters in enzymes: Themes and variations Adv. Inorg. Chem. 1992, 38, 281-322
-
(1992)
Adv. Inorg. Chem.
, vol.38
, pp. 281-322
-
-
Cammack, R.1
-
35
-
-
74049141413
-
Understanding rubredoxin redox potentials: Role of H-bonds on model complexes
-
Gamiz-Hernandez, A. P.; Galstyan, A. S.; Knapp, E. W. Understanding rubredoxin redox potentials: Role of H-bonds on model complexes J. Chem. Theory Comput. 2009, 5, 2898-2908
-
(2009)
J. Chem. Theory Comput.
, vol.5
, pp. 2898-2908
-
-
Gamiz-Hernandez, A.P.1
Galstyan, A.S.2
Knapp, E.W.3
-
36
-
-
79952598021
-
Rubredoxin function: Redox behavior from electrostatics
-
Gamiz-Hernandez, A. P.; Kieseritzky, G.; Knapp, E. W. Rubredoxin function: Redox behavior from electrostatics J. Chem. Theory Comput. 2011, 7, 742-752
-
(2011)
J. Chem. Theory Comput.
, vol.7
, pp. 742-752
-
-
Gamiz-Hernandez, A.P.1
Kieseritzky, G.2
Knapp, E.W.3
-
37
-
-
0025984212
-
Superoxide dismutases
-
Beyer, W.; Imlay, J.; Fridovich, I. Superoxide dismutases Prog. Nucleic Acid Res. Mol. Biol. 1991, 40, 221-253
-
(1991)
Prog. Nucleic Acid Res. Mol. Biol.
, vol.40
, pp. 221-253
-
-
Beyer, W.1
Imlay, J.2
Fridovich, I.3
-
38
-
-
0026587335
-
Mitochondrial genetics: A paradigm for aging and degenerative diseases?
-
Wallace, D. C. Mitochondrial genetics: A paradigm for aging and degenerative diseases? Science 1992, 256, 628-632
-
(1992)
Science
, vol.256
, pp. 628-632
-
-
Wallace, D.C.1
-
39
-
-
84898009719
-
Superoxide dismutases and superoxide reductases
-
Sheng, Y.; Abreu, I. A.; Cabelli, D. E.; Maroney, M. J.; Miller, A.; Teixeria, M.; Valentine, J. S. Superoxide dismutases and superoxide reductases Chem. Rev. 2014, 114, 3854-3918
-
(2014)
Chem. Rev.
, vol.114
, pp. 3854-3918
-
-
Sheng, Y.1
Abreu, I.A.2
Cabelli, D.E.3
Maroney, M.J.4
Miller, A.5
Teixeria, M.6
Valentine, J.S.7
-
40
-
-
74449091635
-
Superoxide dismutases: A review of the metal-associated mechanistic variations
-
Abreu, I. A.; Cabelli, D. E. Superoxide dismutases: A review of the metal-associated mechanistic variations Biochim. Biophys. Acta 2010, 1804, 263-274
-
(2010)
Biochim. Biophys. Acta
, vol.1804
, pp. 263-274
-
-
Abreu, I.A.1
Cabelli, D.E.2
-
41
-
-
84859976622
-
Battles with iron: Manganese in oxidative stress protection
-
Aguirre, J. D.; Culotta, V. C. Battles with iron: Manganese in oxidative stress protection J. Biol. Chem. 2012, 287, 13451-13548
-
(2012)
J. Biol. Chem.
, vol.287
, pp. 13451-13548
-
-
Aguirre, J.D.1
Culotta, V.C.2
-
42
-
-
0029849183
-
Differential expression of superoxide dismutases containing Ni and Fe/Zn in Streptomyces coelicolor
-
Kim, F. J.; Kim, H. P.; Hah, Y. C.; Roe, J. H. Differential expression of superoxide dismutases containing Ni and Fe/Zn in Streptomyces coelicolor Eur. J. Biochem. 1996, 241, 178-185
-
(1996)
Eur. J. Biochem.
, vol.241
, pp. 178-185
-
-
Kim, F.J.1
Kim, H.P.2
Hah, Y.C.3
Roe, J.H.4
-
43
-
-
0003483645
-
-
Meunier, B. Imperial College Press: London
-
Cabelli, D. E.; Riley, D.; Rodriguez, J. A.; Valentine, J. S.; Zhu, H. In Biomimetic Oxidations Catalyzed by Transition Metal Complexes; Meunier, B., Ed.; Imperial College Press: London, 2000.
-
(2000)
Biomimetic Oxidations Catalyzed by Transition Metal Complexes
-
-
Cabelli, D.E.1
Riley, D.2
Rodriguez, J.A.3
Valentine, J.S.4
Zhu, H.5
-
44
-
-
17644414093
-
Spectroscopic and computational studies of Ni superoxide dismutase: Electronic structure contributions to enzymatic function
-
Fiedler, A. T.; Bryngelson, P. A.; Maroney, M. J.; Brunold, T. C. Spectroscopic and computational studies of Ni superoxide dismutase: Electronic structure contributions to enzymatic function J. Am. Chem. Soc. 2005, 127, 5449-5462
-
(2005)
J. Am. Chem. Soc.
, vol.127
, pp. 5449-5462
-
-
Fiedler, A.T.1
Bryngelson, P.A.2
Maroney, M.J.3
Brunold, T.C.4
-
45
-
-
3042613718
-
Nickel superoxide dismutase structure and mechanism
-
Barondeau, D. P.; Kassmann, C. J.; Bruns, C. K.; Tainer, J. A.; Getzoff, E. D. Nickel superoxide dismutase structure and mechanism Biochemistry 2004, 43, 8038-8047
-
(2004)
Biochemistry
, vol.43
, pp. 8038-8047
-
-
Barondeau, D.P.1
Kassmann, C.J.2
Bruns, C.K.3
Tainer, J.A.4
Getzoff, E.D.5
-
46
-
-
2942556712
-
Crystal structure of nickel containing superoxide dismutase reveals another type of active site
-
Wuerges, J.; Lee, J.; Yim, Y.; Yim, H.; Kang, S.; Carugo, K. D. Crystal structure of nickel containing superoxide dismutase reveals another type of active site Proc. Natl. Acad. Sci. U. S. A. 2004, 101, 8569-8574
-
(2004)
Proc. Natl. Acad. Sci. U. S. A.
, vol.101
, pp. 8569-8574
-
-
Wuerges, J.1
Lee, J.2
Yim, Y.3
Yim, H.4
Kang, S.5
Carugo, K.D.6
-
47
-
-
84884294235
-
The prokaryotic Mo/W-bisPGD enzymes family: A catalytic workhorse in bioenergetic
-
Grimaldi, S.; Schoepp-Cothenet, B.; Ceccaldi, P.; Guigliarelli, B.; Magalon, A. The prokaryotic Mo/W-bisPGD enzymes family: a catalytic workhorse in bioenergetic Biochim. Biophys. Acta 2013, 1827, 1048-1085
-
(2013)
Biochim. Biophys. Acta
, vol.1827
, pp. 1048-1085
-
-
Grimaldi, S.1
Schoepp-Cothenet, B.2
Ceccaldi, P.3
Guigliarelli, B.4
Magalon, A.5
-
48
-
-
0021831306
-
Fermentation of acetylene by an obligate anaerobe, Pelobacter acetylenicus sp. Nov
-
Schink, B. Fermentation of acetylene by an obligate anaerobe, Pelobacter acetylenicus sp. nov Arch. Microbiol. 1985, 142, 295-301
-
(1985)
Arch. Microbiol.
, vol.142
, pp. 295-301
-
-
Schink, B.1
-
49
-
-
0036477181
-
Tungsten-containing enzymes
-
L"vov, N. P.; Nosikov, A. N.; Antipov, A. N. Tungsten-containing enzymes Biokhimiya (Moscow) 2002, 67, 196-200
-
(2002)
Biokhimiya (Moscow)
, vol.67
, pp. 196-200
-
-
Lvov, N.P.1
Nosikov, A.N.2
Antipov, A.N.3
-
50
-
-
4243627847
-
Tungstoenzymes
-
Johnson, M. K.; Rees, D. C.; Adams, M. W. W. Tungstoenzymes Chem. Rev. 1996, 96, 2817-2839
-
(1996)
Chem. Rev.
, vol.96
, pp. 2817-2839
-
-
Johnson, M.K.1
Rees, D.C.2
Adams, M.W.W.3
-
51
-
-
77951096477
-
Understanding selectivity of hard and soft metal cations within biological systems using the subvalence concept. 1. Application to blood coagulation: Direct cation-protein electronic effects versus indirect interactions through water networks
-
de Courcy, B.; Pedersen, L. G.; Parisel, O.; Gresh, N.; Silvi, B.; Pilme, J.; Piquemal, J.-P. Understanding selectivity of hard and soft metal cations within biological systems using the subvalence concept. 1. Application to blood coagulation: Direct cation-protein electronic effects versus indirect interactions through water networks J. Chem. Theory Comput. 2010, 6, 1048-1063
-
(2010)
J. Chem. Theory Comput.
, vol.6
, pp. 1048-1063
-
-
De Courcy, B.1
Pedersen, L.G.2
Parisel, O.3
Gresh, N.4
Silvi, B.5
Pilme, J.6
Piquemal, J.-P.7
-
52
-
-
0030668554
-
The natural selection of the chemical elements
-
Williams, R. J. The natural selection of the chemical elements Cell. Mol. Life Sci. 1997, 53, 816-829
-
(1997)
Cell. Mol. Life Sci.
, vol.53
, pp. 816-829
-
-
Williams, R.J.1
-
53
-
-
0026485429
-
A molybdenum and a tungsten isoenzyme of formylmethanofuran dehydrogenase in the thermophilic archaeon Methanobacterium wolfei
-
Schmitz, R. A.; Albracht, S. P. J.; Thauer, R. K. A molybdenum and a tungsten isoenzyme of formylmethanofuran dehydrogenase in the thermophilic archaeon Methanobacterium wolfei Eur. J. Biochem. 1992, 209, 1013-1018
-
(1992)
Eur. J. Biochem.
, vol.209
, pp. 1013-1018
-
-
Schmitz, R.A.1
Albracht, S.P.J.2
Thauer, R.K.3
-
54
-
-
0032933144
-
Enzymatic and physiological properties of the tungsten-substituted molybdenum TMAO reductase from Escherichia coli
-
Buc, J.; Santini, C. L.; Giordani, R.; Czjzek, M.; Wu, L. F.; Giordano, G. Enzymatic and physiological properties of the tungsten-substituted molybdenum TMAO reductase from Escherichia coli Mol. Microbiol. 1999, 32, 159-168
-
(1999)
Mol. Microbiol.
, vol.32
, pp. 159-168
-
-
Buc, J.1
Santini, C.L.2
Giordani, R.3
Czjzek, M.4
Wu, L.F.5
Giordano, G.6
-
55
-
-
4344661337
-
How calcium inhibits the magnesium-dependent enzyme human phosphoserine phosphatase?
-
Peeraer, Y.; Rabijns, A.; Collet, J. F.; Van Schaftingen, E.; De Ranter, C. How calcium inhibits the magnesium-dependent enzyme human phosphoserine phosphatase? Eur. J. Biochem. 2004, 271, 3421-3427
-
(2004)
Eur. J. Biochem.
, vol.271
, pp. 3421-3427
-
-
Peeraer, Y.1
Rabijns, A.2
Collet, J.F.3
Van Schaftingen, E.4
De Ranter, C.5
-
56
-
-
84865969490
-
Why calcium inhibits magnesium-dependent enzyme phosphoserine phosphatase? A theoretical study
-
Yang, L.; Liao, R.-Z.; Ding, W.-J.; Liu, K.; Yu, J.-G.; Liu, R.-Z. Why calcium inhibits magnesium-dependent enzyme phosphoserine phosphatase? A theoretical study Theor. Chem. Acc. 2012, 131, 1275
-
(2012)
Theor. Chem. Acc.
, vol.131
, pp. 1275
-
-
Yang, L.1
Liao, R.-Z.2
Ding, W.-J.3
Liu, K.4
Yu, J.-G.5
Liu, R.-Z.6
-
57
-
-
0037366128
-
Principles governing Mg, Ca, and Zn binding and selectivity in proteins
-
Dudev, T.; Lim, C. Principles governing Mg, Ca, and Zn binding and selectivity in proteins Chem. Rev. 2003, 103, 773-788
-
(2003)
Chem. Rev.
, vol.103
, pp. 773-788
-
-
Dudev, T.1
Lim, C.2
-
58
-
-
34447130835
-
Structures and metal-ion-binding properties of the Ca2+-binding helix-loop-helix EF-hand motifs
-
Gifford, J. L.; Walsh, M. P.; Vogel, H. J. Structures and metal-ion-binding properties of the Ca2+-binding helix-loop-helix EF-hand motifs Biochem. J. 2007, 405, 199-221
-
(2007)
Biochem. J.
, vol.405
, pp. 199-221
-
-
Gifford, J.L.1
Walsh, M.P.2
Vogel, H.J.3
-
59
-
-
0038287034
-
Catechol-O-methyltransferase (COMT): Biochemistry, molecular biology, pharmacology, and clinical efficacy of the new selective COMT inhibitors
-
Männistö, P. T.; Kaakkola, S. Catechol-O-methyltransferase (COMT): Biochemistry, molecular biology, pharmacology, and clinical efficacy of the new selective COMT inhibitors Pharmacol. Rev. 1999, 51, 593-628
-
(1999)
Pharmacol. Rev.
, vol.51
, pp. 593-628
-
-
Männistö, P.T.1
Kaakkola, S.2
-
60
-
-
0016829492
-
Catechol-O-methyl transferase: Pharmacological aspects and physiological role
-
Guldberg, H. C.; Marsden, C. A. Catechol-O-methyl transferase: Pharmacological aspects and physiological role Pharmacol. Rev. 1975, 27, 135-140
-
(1975)
Pharmacol. Rev.
, vol.27
, pp. 135-140
-
-
Guldberg, H.C.1
Marsden, C.A.2
-
61
-
-
0028918413
-
Kinetics of human soluble and membrane-bound catechol O-methyltransferase: A revised mechanism and description of the thermolabile variant of the enzyme
-
Lotta, T.; Vidgren, J.; Tilgmann, C.; Ulmanen, I.; Melen, K. Kinetics of human soluble and membrane-bound catechol O-methyltransferase: a revised mechanism and description of the thermolabile variant of the enzyme Biochemistry 1995, 34, 4202-4210
-
(1995)
Biochemistry
, vol.34
, pp. 4202-4210
-
-
Lotta, T.1
Vidgren, J.2
Tilgmann, C.3
Ulmanen, I.4
Melen, K.5
-
62
-
-
44649191697
-
Crystal structures of human 108V and 108M catechol O-methyltransferase
-
Rutherford, K.; Trong, I. L.; Stenkamp, R.; Parson, W. Crystal structures of human 108V and 108M catechol O-methyltransferase J. Mol. Biol. 2008, 380, 120-130
-
(2008)
J. Mol. Biol.
, vol.380
, pp. 120-130
-
-
Rutherford, K.1
Trong, I.L.2
Stenkamp, R.3
Parson, W.4
-
63
-
-
0028210328
-
Crystal structure of catechol O-methyltransferase
-
Vidgren, J.; Svensson, L. A.; Liljas, A. Crystal structure of catechol O-methyltransferase Nature 1994, 368, 354-358
-
(1994)
Nature
, vol.368
, pp. 354-358
-
-
Vidgren, J.1
Svensson, L.A.2
Liljas, A.3
-
64
-
-
70449228544
-
Enzymatic O-methylation of epinephrine and other catechols
-
Axelrod, J.; Tomchick, R. Enzymatic O-methylation of epinephrine and other catechols J. Biol. Chem. 1958, 233, 702-705
-
(1958)
J. Biol. Chem.
, vol.233
, pp. 702-705
-
-
Axelrod, J.1
Tomchick, R.2
-
65
-
-
84867313446
-
How metal substitution affects the enzymatic activity of catechol-O-methyl transferse
-
Sparta, M.; Alexandrova, A. N. How metal substitution affects the enzymatic activity of catechol-O-methyl transferse PLoS One 2012, 7 e47172
-
(2012)
PLoS One
, vol.7
, pp. e47172
-
-
Sparta, M.1
Alexandrova, A.N.2
-
66
-
-
84883869257
-
-
Reedijk, J. Poppelmeier, K. R. Elsevier: Oxford
-
Martin-Diaconescu, V.; Maroney, M. J. In Comprehensive Inorganic Chemistry II; Reedijk, J.; Poppelmeier, K. R., Eds.; Elsevier: Oxford, 2013.
-
(2013)
Comprehensive Inorganic Chemistry II
-
-
Martin-Diaconescu, V.1
Maroney, M.J.2
-
67
-
-
0033556385
-
One protein, two enzymes
-
Dai, Y.; Wensink, P. C.; Abeles, R. H. One protein, two enzymes J. Biol. Chem. 1999, 274, 1193-1195
-
(1999)
J. Biol. Chem.
, vol.274
, pp. 1193-1195
-
-
Dai, Y.1
Wensink, P.C.2
Abeles, R.H.3
-
68
-
-
84954572280
-
Nickel in acireductone dioxygenase
-
Sigel, A. Sigel, H. Sigel, R. K. O. John Wiley & Sons, Ltd. Chichester
-
Pochapsky, T. C.; Ju, T.; Dang, M.: Nickel in acireductone dioxygenase. In Nickel and Its Surprising Impact in Nature; Sigel, A.; Sigel, H.; Sigel, R. K. O., Eds.; John Wiley & Sons, Ltd.: Chichester, 2007; Vol. 2.
-
(2007)
Nickel and Its Surprising Impact in Nature
, vol.2
-
-
Pochapsky, T.C.1
Ju, T.2
Dang, M.3
-
69
-
-
84861165004
-
Electronic structure analysis of the oxygen-activation mechanism by FeII- and α-ketoglutarate (αKG)-dependent dioxygenases
-
Ye, S.; Riplinger, C.; Hansen, A.; Krebs, C.; Bollinger, J. M. J.; Neese, F. Electronic structure analysis of the oxygen-activation mechanism by FeII- and α-ketoglutarate (αKG)-dependent dioxygenases Chem.-Eur. J. 2012, 18, 6555-6567
-
(2012)
Chem.-Eur. J.
, vol.18
, pp. 6555-6567
-
-
Ye, S.1
Riplinger, C.2
Hansen, A.3
Krebs, C.4
Bollinger, J.M.J.5
Neese, F.6
-
70
-
-
84859371314
-
Oxygen activation in extradiol catecholate dioxygenases-a density functional study
-
Christian, J. G.; Ye, S.; Neese, F. Oxygen activation in extradiol catecholate dioxygenases-a density functional study Chem. Sci. 2012, 3, 1600-1611
-
(2012)
Chem. Sci.
, vol.3
, pp. 1600-1611
-
-
Christian, J.G.1
Ye, S.2
Neese, F.3
-
71
-
-
0035967509
-
Mechanistic studies of two dioxygenases in the methionine salvage pathway of Klebsiella pneumonia
-
Dai, Y.; Pochapsky, T. C.; Abeles, H. R. Mechanistic studies of two dioxygenases in the methionine salvage pathway of Klebsiella pneumonia Biochemistry 2001, 40, 6379-6387
-
(2001)
Biochemistry
, vol.40
, pp. 6379-6387
-
-
Dai, Y.1
Pochapsky, T.C.2
Abeles, H.R.3
-
72
-
-
84872570216
-
Regioselective aliphatic carbon-carbon bond cleavage by a model system of relevance to iron-containing acireductone dioxygenase
-
Allpress, C. J.; Grubel, K.; Szajna-Fuller, E.; Arif, M. A.; Berreau, L. Regioselective aliphatic carbon-carbon bond cleavage by a model system of relevance to iron-containing acireductone dioxygenase J. Am. Chem. Soc. 2013, 135, 659-668
-
(2013)
J. Am. Chem. Soc.
, vol.135
, pp. 659-668
-
-
Allpress, C.J.1
Grubel, K.2
Szajna-Fuller, E.3
Arif, M.A.4
Berreau, L.5
-
73
-
-
84880916609
-
Metal-dependent activity of Fe and Ni acireductone dioxygenases: How two electrons reroute the catalytic pathway
-
Sparta, M.; Valdez, C. E.; Alexandrova, A. N. Metal-dependent activity of Fe and Ni acireductone dioxygenases: How two electrons reroute the catalytic pathway J. Mol. Biol. 2013, 245, 3007-3018
-
(2013)
J. Mol. Biol.
, vol.245
, pp. 3007-3018
-
-
Sparta, M.1
Valdez, C.E.2
Alexandrova, A.N.3
-
75
-
-
84861717687
-
Biocatalysis
-
Thayer, A. M. Biocatalysis Chem. Eng. News 2012, 90, 13-18
-
(2012)
Chem. Eng. News
, vol.90
, pp. 13-18
-
-
Thayer, A.M.1
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