-
5
-
-
0031900123
-
Structural and spectroscopic characterization of a mononuclear hydroperoxo-copper(II) complex with tripodal pyridylamine ligands
-
Wada A., Harata M., Hasegawa K., Jitsukawa K., Masuda H., Mukai M., Kitagawa T., Einaga H. Structural and spectroscopic characterization of a mononuclear hydroperoxo-copper(II) complex with tripodal pyridylamine ligands. Angew Chem Int Ed Engl. 37:1998;798-799.
-
(1998)
Angew Chem Int Ed Engl
, vol.37
, pp. 798-799
-
-
Wada, A.1
Harata, M.2
Hasegawa, K.3
Jitsukawa, K.4
Masuda, H.5
Mukai, M.6
Kitagawa, T.7
Einaga, H.8
-
7
-
-
0001681509
-
2) (R=i-Pr and Ph)
-
2) (R=i-Pr and Ph). J Am Chem Soc. 114:1992;1277-1291.
-
(1992)
J Am Chem Soc
, vol.114
, pp. 1277-1291
-
-
Kitajima, N.1
Fujisawa, K.2
Fujimoto, C.3
Moro-Oka, Y.4
Hashimoto, S.5
Kitagawa, T.6
Toriumi, K.7
Tatsumi, K.8
Nakamura, A.9
-
9
-
-
0029860841
-
Structural, spectroscopic, and theoretical characterization of bis(μ-oxo)dicopper complexes, novel intermediates in copper-mediated dioxygen activation
-
Mahapatra S., Halfen J.A., Wilkinson E.C., Pan G.F., Wang X.D., Young V.G., Cramer C.J., Que L. Jr., Tolman W.B. Structural, spectroscopic, and theoretical characterization of bis(μ-oxo)dicopper complexes, novel intermediates in copper-mediated dioxygen activation. J Am Chem Soc. 118:1996;11555-11574.
-
(1996)
J Am Chem Soc
, vol.118
, pp. 11555-11574
-
-
Mahapatra, S.1
Halfen, J.A.2
Wilkinson, E.C.3
Pan, G.F.4
Wang, X.D.5
Young, V.G.6
Cramer, C.J.7
Que L., Jr.8
Tolman, W.B.9
-
10
-
-
0030848960
-
2+ core: Characterization of a new bis(μ-oxo)dicopper complex stabilized by a sterically hindered dinucleating bis(triazacyclononane) ligand
-
2+ core: characterization of a new bis(μ-oxo)dicopper complex stabilized by a sterically hindered dinucleating bis(triazacyclononane) ligand. Angew Chem Int Ed Engl. 36:1997;130-133.
-
(1997)
Angew Chem Int Ed Engl
, vol.36
, pp. 130-133
-
-
Mahapatra, S.1
Young, V.G.2
Kaderli, S.3
Zuberbühler, A.D.4
Tolman, W.B.5
-
15
-
-
0001744285
-
Making and breaking O-O bonds
-
Tolman W.B. Making and breaking O-O bonds. Accounts Chem Res. 30:1997;227-237.
-
(1997)
Accounts Chem Res
, vol.30
, pp. 227-237
-
-
Tolman, W.B.1
-
16
-
-
0032053562
-
Mechanistic studies of aliphatic ligand hydroxylation of a copper complex by dioxygen: A model reaction for copper monooxygenases
-
Itoh S., Nakao H., Berreau L.M., Kondo T., Komatsu M., Fukuzumi S. Mechanistic studies of aliphatic ligand hydroxylation of a copper complex by dioxygen: a model reaction for copper monooxygenases. J Am Chem Soc. 120:1998;2890-2899.
-
(1998)
J Am Chem Soc
, vol.120
, pp. 2890-2899
-
-
Itoh, S.1
Nakao, H.2
Berreau, L.M.3
Kondo, T.4
Komatsu, M.5
Fukuzumi, S.6
-
17
-
-
0027981519
-
Crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin shows unusual differences
-
Magnus K.A., Hazes B., Tonthat H., Bonaventura C., Bonaventura J., Hol W.G.J. Crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin shows unusual differences. Proteins. 19:1994;302-309.
-
(1994)
Proteins
, vol.19
, pp. 302-309
-
-
Magnus, K.A.1
Hazes, B.2
Tonthat, H.3
Bonaventura, C.4
Bonaventura, J.5
Hol, W.G.J.6
-
18
-
-
0031760504
-
Crystal-structure of a plant catechol oxidase containing a dicopper center
-
The crystal structure of the binuclear Cu enzyme catechol oxidase in both its aerobically isolated Cu(II)-Cu(II) state and its fully reduced Cu(I)-Cu(I) state is described. Unlike tyrosinase, this enzyme lacks mono-oxygenase activity, although it oxidizes catechols to o-quinones. Similarities and differences between the three binuclear copper proteins hemocyanin, tyrosinase and catechol oxidase are discussed.
-
Klabunde T., Eicken C., Sacchettini J.C., Krebs B. Crystal-structure of a plant catechol oxidase containing a dicopper center. Nat Struct Biol. 5:1998;1084-1090. The crystal structure of the binuclear Cu enzyme catechol oxidase in both its aerobically isolated Cu(II)-Cu(II) state and its fully reduced Cu(I)-Cu(I) state is described. Unlike tyrosinase, this enzyme lacks mono-oxygenase activity, although it oxidizes catechols to o-quinones. Similarities and differences between the three binuclear copper proteins hemocyanin, tyrosinase and catechol oxidase are discussed.
-
(1998)
Nat Struct Biol
, vol.5
, pp. 1084-1090
-
-
Klabunde, T.1
Eicken, C.2
Sacchettini, J.C.3
Krebs, B.4
-
19
-
-
0033044890
-
Stabilization of copper dioxygen compounds: Design, synthesis and characterization
-
1/2(298K)=50 min].
-
1/2(298K)=50 min].
-
(1999)
Chem Eur J
, vol.5
, pp. 1716-1721
-
-
Borzel, H.1
Comba, P.2
Katsichtis, C.3
Kiefer, W.4
Lienke, A.5
Nagel, V.6
Pritzkow, H.7
-
20
-
-
0032746285
-
6tren) as a ligand
-
2 complex is described. A Cu(II)-superoxo intermediate is observed during formation of the peroxide complex.
-
2 complex is described. A Cu(II)-superoxo intermediate is observed during formation of the peroxide complex.
-
(1999)
Chem Eur J
, vol.5
, pp. 3124-3129
-
-
Becker, M.1
Heinemann, F.2
Schindler, S.3
-
23
-
-
0033518592
-
Self-assembly of a copper-ligating dendrimer that provides a new non-heme metalloprotein mimic: "dendrimer effects'' on stability of the bis(μ-oxo)dicopper(III) core
-
2 species decreased, as anticipated, with the size of the dendritic subunits. The ligands of larger molecular weight show greater thermal stability with the largest complex, ~500 times more stable than its parent. Kinetic analysis of the decay rates attribute the greater stability primarily to the entropy of activation required to appropriately align the N-benzyl groups for oxidative cleavage.
-
2 species decreased, as anticipated, with the size of the dendritic subunits. The ligands of larger molecular weight show greater thermal stability with the largest complex, ~500 times more stable than its parent. Kinetic analysis of the decay rates attribute the greater stability primarily to the entropy of activation required to appropriately align the N-benzyl groups for oxidative cleavage.
-
(1999)
J Am Chem Soc
, vol.121
, pp. 874-875
-
-
Enomoto, M.1
Aida, T.2
-
24
-
-
0032511358
-
Investigation of the reactive oxygen intermediate in an arene hydroxylation reaction performed by xylyl-bridged binuclear copper-complexes
-
Pidcock E., Obias H.V., Zhang C.X., Karlin K.D., Solomon E.I. Investigation of the reactive oxygen intermediate in an arene hydroxylation reaction performed by xylyl-bridged binuclear copper-complexes. J Am Chem Soc. 120:1998;7841-7847.
-
(1998)
J Am Chem Soc
, vol.120
, pp. 7841-7847
-
-
Pidcock, E.1
Obias, H.V.2
Zhang, C.X.3
Karlin, K.D.4
Solomon, E.I.5
-
25
-
-
4243280772
-
2-peroxo)- And bis(μ-oxo)dicopper cores
-
2 species and describes recent efforts made toward understanding the factors influencing the relative stability and reactivity of these cores.
-
2 species and describes recent efforts made toward understanding the factors influencing the relative stability and reactivity of these cores.
-
(1999)
Coord Chem Rev
, vol.192
, pp. 855-869
-
-
Holland, P.L.1
Tolman, W.B.2
-
26
-
-
0033583463
-
Is the bis(μ-oxo)dicopper core capable of hydroxylating an arene?
-
2 species (tyrosinase) raises the question of whether a common intermediate species might be operative in both cases.
-
2 species (tyrosinase) raises the question of whether a common intermediate species might be operative in both cases.
-
(1999)
Angew Chem Int Ed Engl
, vol.38
, pp. 1139-1142
-
-
Holland, P.L.1
Rodgers, K.R.2
Tolman, W.B.3
-
27
-
-
0030005669
-
Reversible cleavage and formation of the dioxygen O-O bond within a dicopper complex
-
Halfen J.A., Mahapatra S., Wilkinson E.C., Kaderli S., Young V.G., Que L. Jr., Zuberbühler A.D., Tolman W.B. Reversible cleavage and formation of the dioxygen O-O bond within a dicopper complex. Science. 271:1996;1397-1400.
-
(1996)
Science
, vol.271
, pp. 1397-1400
-
-
Halfen, J.A.1
Mahapatra, S.2
Wilkinson, E.C.3
Kaderli, S.4
Young, V.G.5
Que L., Jr.6
Zuberbühler, A.D.7
Tolman, W.B.8
-
28
-
-
0000437326
-
2 complexes
-
2 intermediates, with potential implications for the chemistry observed in natural systems.
-
2 intermediates, with potential implications for the chemistry observed in natural systems.
-
(1999)
Inorg Chem
, vol.38
, pp. 2161-2168
-
-
Cahoy, J.1
Holland, P.L.2
Tolman, W.B.3
-
30
-
-
0038021215
-
Ligand effects in the models and mimics of oxyhemocyanin and oxytyrosinase : A density-functional study of reversible dioxygen binding and reversible O-O bond-cleavage
-
Berces A. Ligand effects in the models and mimics of oxyhemocyanin and oxytyrosinase : a density-functional study of reversible dioxygen binding and reversible O-O bond-cleavage. Inorg Chem. 36:1997;4831-4837.
-
(1997)
Inorg Chem
, vol.36
, pp. 4831-4837
-
-
Berces, A.1
-
33
-
-
0002282206
-
Aminoindanes in oxygen transfer reactions ; 2 : Copper-complexes as functional models for dopamine-beta-hydroxylase stereospecific oxygen-atom transfer
-
Blain I., Bruno P., Giorgi M., Lojou E., Lexa D., Reglier M. Aminoindanes in oxygen transfer reactions ; 2 : copper-complexes as functional models for dopamine-beta-hydroxylase stereospecific oxygen-atom transfer. Eur J Inorg Chem. 1998;1297-1304.
-
(1998)
Eur J Inorg Chem
, pp. 1297-1304
-
-
Blain, I.1
Bruno, P.2
Giorgi, M.3
Lojou, E.4
Lexa, D.5
Reglier, M.6
-
34
-
-
0033575068
-
2+ core: Structural implications
-
2 complex with exogenous substrates, such as alcohols and amines, is described. N,N,N′,N′-tetramethyl 1,3-propanediamine yields the best results for alcohol oxidation compared to the related 1,2-ethylenediamine ligands. A correlation between reactivity and structure of these complexes exists. The study shows how subtle changes in the structure of these intermediates can bring about a significant difference in their reactivity.
-
2 complex with exogenous substrates, such as alcohols and amines, is described. N,N,N′,N′-tetramethyl 1,3-propanediamine yields the best results for alcohol oxidation compared to the related 1,2-ethylenediamine ligands. A correlation between reactivity and structure of these complexes exists. The study shows how subtle changes in the structure of these intermediates can bring about a significant difference in their reactivity.
-
(1999)
J Am Chem Soc
, vol.121
, pp. 5583-5584
-
-
Mahadevan, V.1
Dubois, J.L.2
Hedman, B.3
Hodgson, K.O.4
Stack, T.D.P.5
-
35
-
-
0027159780
-
Ligand interactions with galactose oxidase-mechanistic insights
-
Whittaker M.M., Whittaker J.W. Ligand interactions with galactose oxidase-mechanistic insights. Biophys J. 64:1993;762-772.
-
(1993)
Biophys J
, vol.64
, pp. 762-772
-
-
Whittaker, M.M.1
Whittaker, J.W.2
-
36
-
-
7744231498
-
Mechanisms whereby mononuclear copper proteins functionalize organic substrates
-
Klinman J.P. Mechanisms whereby mononuclear copper proteins functionalize organic substrates. Chem Rev. 96:1996;2541-2562.
-
(1996)
Chem Rev
, vol.96
, pp. 2541-2562
-
-
Klinman, J.P.1
-
37
-
-
0024557102
-
Resonance raman evidence for tyrosine involvement in the radical site of galactose oxidase
-
Whittaker M.M., DeVito V.L., Asher S.A., Whittaker J.W. Resonance raman evidence for tyrosine involvement in the radical site of galactose oxidase. J Biol Chem. 264:1989;7104-7106.
-
(1989)
J Biol Chem
, vol.264
, pp. 7104-7106
-
-
Whittaker, M.M.1
DeVito, V.L.2
Asher, S.A.3
Whittaker, J.W.4
-
38
-
-
0026084786
-
Novel thioether bond revealed by a 1.7 Å crystal-structure of galactose oxidase
-
Ito N., Phillips S.E.V., Stevens C., Ogel Z.B., McPherson M.J., Keen J.N., Yadav K.D.S., Knowles P.F. Novel thioether bond revealed by a 1.7 Å crystal-structure of galactose oxidase. Nature. 350:1991;87-90.
-
(1991)
Nature
, vol.350
, pp. 87-90
-
-
Ito, N.1
Phillips, S.E.V.2
Stevens, C.3
Ogel, Z.B.4
McPherson, M.J.5
Keen, J.N.6
Yadav, K.D.S.7
Knowles, P.F.8
-
39
-
-
0028290823
-
Crystal-structure of a free radical enzyme: Galactose oxidase
-
Ito N., Phillips S.E.V., Yadav K.D.S., Knowles P.F. Crystal-structure of a free radical enzyme: galactose oxidase. J Mol Biol. 238:1994;794-814.
-
(1994)
J Mol Biol
, vol.238
, pp. 794-814
-
-
Ito, N.1
Phillips, S.E.V.2
Yadav, K.D.S.3
Knowles, P.F.4
-
40
-
-
0030818539
-
Synthetic models of the inactive copper(II)-tyrosinate and active copper(II)-tyrosyl radical forms of galactose and glyoxal oxidases
-
Halfen J.A., Jazdzewski B.A., Mahapatra S., Berreau L.M., Wilkinson E.C., Que L. Jr., Tolman W.B. Synthetic models of the inactive copper(II)-tyrosinate and active copper(II)-tyrosyl radical forms of galactose and glyoxal oxidases. J Am Chem Soc. 119:1997;8217-8227.
-
(1997)
J Am Chem Soc
, vol.119
, pp. 8217-8227
-
-
Halfen, J.A.1
Jazdzewski, B.A.2
Mahapatra, S.3
Berreau, L.M.4
Wilkinson, E.C.5
Que L., Jr.6
Tolman, W.B.7
-
41
-
-
0032556375
-
A 3-coordinate copper(I) phenoxide complex that models the reduced form of galactose-oxidase
-
2 reactivity is similar to that of reduced GO; however, the latter is proposed to exist as a Cu(I):phenol complex.
-
2 reactivity is similar to that of reduced GO; however, the latter is proposed to exist as a Cu(I):phenol complex.
-
(1998)
J Chem Soc Chem Comm
, vol.22
, pp. 2521-2522
-
-
Jazdzewski, B.A.1
Young, V.G.2
Tolman, W.B.3
-
42
-
-
1842365490
-
Phenoxyl radical complexes of Zinc(II)
-
Sokolowski A., Muller J., Weyhermuller T., Schnepf R., Hildebrandt P., Hildenbrand K., Bothe E., Wieghardt K. Phenoxyl radical complexes of Zinc(II). J Am Chem Soc. 119:1997;8889-8900.
-
(1997)
J Am Chem Soc
, vol.119
, pp. 8889-8900
-
-
Sokolowski, A.1
Muller, J.2
Weyhermuller, T.3
Schnepf, R.4
Hildebrandt, P.5
Hildenbrand, K.6
Bothe, E.7
Wieghardt, K.8
-
43
-
-
0030882533
-
Phenoxyl-copper(II) complexes: Models for the active-site of galactose-oxidase
-
Sokolowski A., Leutbecher H., Weyhermuller T., Schnepf R., Both E., Bill E., Hildebrandt P., Wieghardt K. Phenoxyl-copper(II) complexes: models for the active-site of galactose-oxidase. J Biol Inorg Chem. 2:1997;444-453.
-
(1997)
J Biol Inorg Chem
, vol.2
, pp. 444-453
-
-
Sokolowski, A.1
Leutbecher, H.2
Weyhermuller, T.3
Schnepf, R.4
Both, E.5
Bill, E.6
Hildebrandt, P.7
Wieghardt, K.8
-
44
-
-
0033578664
-
Oxidation of benzyl alcohol with Cu-II and Zn-II complexes of the phenoxyl radical as a model of the reaction of galactose oxidase
-
In this paper, the stoichiometric oxidation of benzyl alcohol by Cu(II) and Zn(II) phenoxyl radical complexes is described, along with the reaction kinetics.
-
Itoh S., Taki M., Takayama S., Nagatomo S., Kitagawa T., Sakurada N., Arakawa R., Fukuzumi S. Oxidation of benzyl alcohol with Cu-II and Zn-II complexes of the phenoxyl radical as a model of the reaction of galactose oxidase. Angew Chem Int Ed Engl. 38:1999;2774-2776. In this paper, the stoichiometric oxidation of benzyl alcohol by Cu(II) and Zn(II) phenoxyl radical complexes is described, along with the reaction kinetics.
-
(1999)
Angew Chem Int Ed Engl
, vol.38
, pp. 2774-2776
-
-
Itoh, S.1
Taki, M.2
Takayama, S.3
Nagatomo, S.4
Kitagawa, T.5
Sakurada, N.6
Arakawa, R.7
Fukuzumi, S.8
-
45
-
-
0343085283
-
Syntheses ; Structures and electrochemistry of copper(II) salicylaldehyde/tris(3-phenylpyrazolyl)borate complexes as models for the radical copper oxidases
-
Halcrow M.A., Chia L., Liu X.M., McInnes E., Yellowlees L.J., Mabbs F.E., Scowen I.J., McPartlin M., Davies J.E. Syntheses ; structures and electrochemistry of copper(II) salicylaldehyde/tris(3-phenylpyrazolyl)borate complexes as models for the radical copper oxidases. J Chem Soc Dalton Trans. 11:1999;1753-1762.
-
(1999)
J Chem Soc Dalton Trans
, vol.11
, pp. 1753-1762
-
-
Halcrow, M.A.1
Chia, L.2
Liu, X.M.3
McInnes, E.4
Yellowlees, L.J.5
Mabbs, F.E.6
Scowen, I.J.7
McPartlin, M.8
Davies, J.E.9
-
46
-
-
0030476115
-
Galactose oxidase model complexes: Catalytic reactivities
-
Wang Y., Stack T.D.P. Galactose oxidase model complexes: catalytic reactivities. J Am Chem Soc. 118:1996;13097-13098.
-
(1996)
J Am Chem Soc
, vol.118
, pp. 13097-13098
-
-
Wang, Y.1
Stack, T.D.P.2
-
47
-
-
37049084868
-
Oxidations of primary alcohols with a copper(II) complex as a possible galactose-oxidase model
-
Kitajima N., Whang K., Moro-oka Y., Uchida A., Sasada Y. Oxidations of primary alcohols with a copper(II) complex as a possible galactose-oxidase model. J Chem Soc Chem Comm. 1986;1504-1505.
-
(1986)
J Chem Soc Chem Comm
, pp. 1504-1505
-
-
Kitajima, N.1
Whang, K.2
Moro-Oka, Y.3
Uchida, A.4
Sasada, Y.5
-
48
-
-
0342541252
-
The role of oxygen in chemistry and biochemistry
-
W. Ando, & Y. Moro-oka. Amsterdam: Elsevier Science Publishers
-
Groves J.T., Park K.T. The role of oxygen in chemistry and biochemistry. Ando W., Moro-oka Y. Studies in Organic Chemistry. 1988;542-548 Elsevier Science Publishers, Amsterdam.
-
(1988)
Studies in Organic Chemistry
, pp. 542-548
-
-
Groves, J.T.1
Park, K.T.2
-
49
-
-
0000717295
-
A functional-model of galactose-oxidase: Catalytic-oxidation of primary alcohols with a one-electron oxidized copper(II) complex
-
Saintaman E., Menage S., Pierre J.L., Defrancq E., Gellon G. A functional-model of galactose-oxidase: catalytic-oxidation of primary alcohols with a one-electron oxidized copper(II) complex. New J Chem. 22:1998;393-394.
-
(1998)
New J Chem
, vol.22
, pp. 393-394
-
-
Saintaman, E.1
Menage, S.2
Pierre, J.L.3
Defrancq, E.4
Gellon, G.5
-
50
-
-
0032559208
-
Catalytic galactose oxidase models: Biomimetic Cu(II)-phenoxyl radical reactivity
-
Wang Y., DuBois J.L., Hedman B., Hodgson K.O., Stack T.D.P. Catalytic galactose oxidase models: biomimetic Cu(II)-phenoxyl radical reactivity. Science. 279:1998;537-540.
-
(1998)
Science
, vol.279
, pp. 537-540
-
-
Wang, Y.1
Dubois, J.L.2
Hedman, B.3
Hodgson, K.O.4
Stack, T.D.P.5
-
52
-
-
0031678724
-
From structural models of galactose-oxidase to homogeneous catalysis: Efficient aerobic oxidation of alcohols
-
This paper presents the aerobic oxidation of primary as well as secondary alcohols to their carbonyl products by a binuclear, biphenoxyl-radical Cu(II) complex. In addition, certain secondary alcohols undergo radical-based C-C coupling reactions to generate 1,2-diols. The enhanced reactivity of these model complexes relative to GO is consistent with a different radical-based mechanism.
-
Chaudhuri P., Hess M., Florke U., Wieghardt K. From structural models of galactose-oxidase to homogeneous catalysis: efficient aerobic oxidation of alcohols. Angew Chem Int Ed Engl. 37:1998;2217-2220. This paper presents the aerobic oxidation of primary as well as secondary alcohols to their carbonyl products by a binuclear, biphenoxyl-radical Cu(II) complex. In addition, certain secondary alcohols undergo radical-based C-C coupling reactions to generate 1,2-diols. The enhanced reactivity of these model complexes relative to GO is consistent with a different radical-based mechanism.
-
(1998)
Angew Chem Int Ed Engl
, vol.37
, pp. 2217-2220
-
-
Chaudhuri, P.1
Hess, M.2
Florke, U.3
Wieghardt, K.4
-
53
-
-
0033583557
-
Aerobic oxidation of primary alcohols by a new mononuclear Cu-II-radical catalyst
-
A mononuclear copper catalyst is generated for efficient oxidation of alcohols. In addition, the isolation and characterization of the first end-on Cu(II) superoxide complex is reported.
-
Chaudhuri P., Hess M., Weyhermuller T., Wieghardt K. Aerobic oxidation of primary alcohols by a new mononuclear Cu-II-radical catalyst. Angew Chem Int Ed Engl. 38:1999;1095-1098. A mononuclear copper catalyst is generated for efficient oxidation of alcohols. In addition, the isolation and characterization of the first end-on Cu(II) superoxide complex is reported.
-
(1999)
Angew Chem Int Ed Engl
, vol.38
, pp. 1095-1098
-
-
Chaudhuri, P.1
Hess, M.2
Weyhermuller, T.3
Wieghardt, K.4
-
54
-
-
0032732642
-
Aerobic oxidation of primary alcohols (including methanol) by copper(II)- And zinc(II)-phenoxyl radical catalysts
-
Cu(II) and Zn(II) complexes of a bisphenol ligand with five different oxidation states are presented and their oxidation behaviour discussed. Selective oxidation of primary aliphatic alcohols is achieved and large KIEs are reported for the HA-based mechanism.
-
Chaudhuri P., Hess M., Muller J., Hildenbrand K., Bill E., Weyhermuller T., Wieghardt K. Aerobic oxidation of primary alcohols (including methanol) by copper(II)- and zinc(II)-phenoxyl radical catalysts. J Am Chem Soc. 121:1999;9599-9610. Cu(II) and Zn(II) complexes of a bisphenol ligand with five different oxidation states are presented and their oxidation behaviour discussed. Selective oxidation of primary aliphatic alcohols is achieved and large KIEs are reported for the HA-based mechanism.
-
(1999)
J Am Chem Soc
, vol.121
, pp. 9599-9610
-
-
Chaudhuri, P.1
Hess, M.2
Muller, J.3
Hildenbrand, K.4
Bill, E.5
Weyhermuller, T.6
Wieghardt, K.7
-
55
-
-
0030043941
-
Molecular modeling studies on oxidation of hexopyranoses by galactose-oxidase : An active-site topology apparently designed to catalyze radical reactions ; Either concerted or stepwise
-
Wachter R.M., Branchaud B.P. Molecular modeling studies on oxidation of hexopyranoses by galactose-oxidase : an active-site topology apparently designed to catalyze radical reactions ; either concerted or stepwise. J Am Chem Soc. 118:1996;2782-2789.
-
(1996)
J Am Chem Soc
, vol.118
, pp. 2782-2789
-
-
Wachter, R.M.1
Branchaud, B.P.2
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