-
2
-
-
0019815526
-
15N]lysine and its incorporation into streptothricin F
-
15N]lysine and its incorporation into streptothricin F. J Am Chem Soc 1981, 103:6752-6754.
-
(1981)
J Am Chem Soc
, vol.103
, pp. 6752-6754
-
-
Gould, S.J.1
Thiruvengadam, T.K.2
-
3
-
-
0014939344
-
Lysine 2,3 aminomutase. Purification and properties of a pyridoxal phosphate and S-adenosylmethionine activated enzyme
-
Chirpich TP, Zappia V, Costilow RN, Barker HA: Lysine 2,3 aminomutase. Purification and properties of a pyridoxal phosphate and S-adenosylmethionine activated enzyme. J Biol Chem 1970, 245:1778-1789.
-
(1970)
J Biol Chem
, vol.245
, pp. 1778-1789
-
-
Chirpich, T.P.1
Zappia, V.2
Costilow, R.N.3
Barker, H.A.4
-
4
-
-
0014959650
-
Studies on lysine 2,3-aminomutase. Subunit structure and sulfhydryl groups
-
Zappia V, Barker HA: Studies on lysine 2,3-aminomutase. Subunit structure and sulfhydryl groups. Biochim Biophys Acta 1970, 207:505-513.
-
(1970)
Biochim Biophys Acta
, vol.207
, pp. 505-513
-
-
Zappia, V.1
Barker, H.A.2
-
5
-
-
0027351422
-
Lysine 2,3-aminomutase and the interconversion of lysine and β-lysine
-
Frey PA, Reed GH: Lysine 2,3-aminomutase and the interconversion of lysine and β-lysine. Adv Enzymol Relat Areas Mol Biol 1993, 66:1-39.
-
(1993)
Adv Enzymol Relat Areas Mol Biol
, vol.66
, pp. 1-39
-
-
Frey, P.A.1
Reed, G.H.2
-
7
-
-
0000112024
-
Stereochemistry of lysine 2,3-aminomutase isolated from Clostridium subterminale strain SB4
-
Aberhart DJ, Gould SJ, Lin H-J, Thiruvengadam TK, Weiller BH: Stereochemistry of lysine 2,3-aminomutase isolated from Clostridium subterminale strain SB4. J Am Chem Soc 1983, 105:5461-5470.
-
(1983)
J Am Chem Soc
, vol.105
, pp. 5461-5470
-
-
Aberhart, D.J.1
Gould, S.J.2
Lin, H.-J.3
Thiruvengadam, T.K.4
Weiller, B.H.5
-
8
-
-
0025900906
-
Molecular properties of lysine 2,3-aminomutase
-
Song KB, Frey PA: Molecular properties of lysine 2,3-aminomutase. J Biol Chem 1991, 266:7651-7655.
-
(1991)
J Biol Chem
, vol.266
, pp. 7651-7655
-
-
Song, K.B.1
Frey, P.A.2
-
9
-
-
0025836317
-
Metal cofactors of lysine 2,3-aminomutase
-
Petrovich RM, Ruzicka FJ, Reed GH, Frey PA: Metal cofactors of lysine 2,3-aminomutase. J Biol Chem 1991, 226:7656-7660.
-
(1991)
J Biol Chem
, vol.226
, pp. 7656-7660
-
-
Petrovich, R.M.1
Ruzicka, F.J.2
Reed, G.H.3
Frey, P.A.4
-
10
-
-
0023645851
-
The role of S-adenosylmethionine in the lysine 2,3,-aminomutase reaction
-
Moss ML, Frey PA: The role of S-adenosylmethionine in the lysine 2,3,-aminomutase reaction. J Biol Chem 1987, 262:14859-14862.
-
(1987)
J Biol Chem
, vol.262
, pp. 14859-14862
-
-
Moss, M.L.1
Frey, P.A.2
-
11
-
-
0025119601
-
Activation of lysine 2,3-aminomutase by S-adenosylmethionine
-
Moss ML, Frey PA: Activation of lysine 2,3-aminomutase by S-adenosylmethionine. J Biol Chem 1990, 265:18112-18115.
-
(1990)
J Biol Chem
, vol.265
, pp. 18112-18115
-
-
Moss, M.L.1
Frey, P.A.2
-
13
-
-
0024496311
-
Lysine 2,3-aminomutase. Support for a mechanism of hydrogen transfer involving S-adenosylmethionine
-
Baraniak J, Moss ML, Frey PA: Lysine 2,3-aminomutase. Support for a mechanism of hydrogen transfer involving S-adenosylmethionine. J Biol Chem 1989, 264:1357-1360.
-
(1989)
J Biol Chem
, vol.264
, pp. 1357-1360
-
-
Baraniak, J.1
Moss, M.L.2
Frey, P.A.3
-
14
-
-
0000489779
-
The importance of organic radicals in enzymatic cleavage of unactivated C-H bonds
-
Frey PA: The importance of organic radicals in enzymatic cleavage of unactivated C-H bonds. Chem Rev 1990, 90:1343-1357.
-
(1990)
Chem Rev
, vol.90
, pp. 1343-1357
-
-
Frey, P.A.1
-
15
-
-
0026606405
-
An organic radical in the lysine 2,3-aminomutase reaction
-
Ballinger MD, Reed GH, Frey PA: An organic radical in the lysine 2,3-aminomutase reaction. Biochemistry 1992, 31:949-953.
-
(1992)
Biochemistry
, vol.31
, pp. 949-953
-
-
Ballinger, M.D.1
Reed, G.H.2
Frey, P.A.3
-
16
-
-
0026444094
-
Structure of a substrate radical intermediate in the reaction of lysine 2,3-aminomutase
-
Ballinger MD, Frey PA, Reed GH: Structure of a substrate radical intermediate in the reaction of lysine 2,3-aminomutase. Biochemistry 1992, 31:10782-10789.
-
(1992)
Biochemistry
, vol.31
, pp. 10782-10789
-
-
Ballinger, M.D.1
Frey, P.A.2
Reed, G.H.3
-
17
-
-
0029092235
-
Pulsed electron paramagnetic resonance studies of the lysine 2,3-aminomutase substrate radical: Evidence for the participation of pyridoxal-5′-phosphate in a radical rearrangement
-
Ballinger MD, Frey PA, Reed GH, LoBrullo R: Pulsed electron paramagnetic resonance studies of the lysine 2,3-aminomutase substrate radical: Evidence for the participation of pyridoxal-5′-phosphate in a radical rearrangement Biochemistry 1995, 34:10086-10093.
-
(1995)
Biochemistry
, vol.34
, pp. 10086-10093
-
-
Ballinger, M.D.1
Frey, P.A.2
Reed, G.H.3
LoBrullo, R.4
-
18
-
-
0029736685
-
Lysine 2,3-aminomutase: Rapid mix-freeze-quench electron paramagnetic resonance studies establishing the kinetic competence of a substrate-based radical intermediate
-
cat for lysine 2,3-aminomutase. This established the kinetic competence of this radical to be an intermediate in the isomerization.
-
(1996)
Biochemistry
, vol.35
, pp. 11081-11084
-
-
Chang, C.H.1
Ballinger, M.D.2
Reed, G.H.3
Frey, P.A.4
-
19
-
-
0029089648
-
Observation of a second substrate radical intermediate in the reaction of lysine 2,3-aminomutase: A radical centered on the β-carbon of the alternative substrate 4-thia-L-lysine
-
Wu W, Lieder KW, Reed GH, Frey PA: Observation of a second substrate radical intermediate in the reaction of lysine 2,3-aminomutase: A radical centered on the β-carbon of the alternative substrate 4-thia-L-lysine. Biochemistry 1995, 34:10532-10537.
-
(1995)
Biochemistry
, vol.34
, pp. 10532-10537
-
-
Wu, W.1
Lieder, K.W.2
Reed, G.H.3
Frey, P.A.4
-
20
-
-
0001136531
-
An electron spin resonance investigation of the aziridylcarbinyl and related free radicals
-
Danen WC, West CT: An electron spin resonance investigation of the aziridylcarbinyl and related free radicals. J Am Chem Soc 1974, 96:2447-2453.
-
(1974)
J Am Chem Soc
, vol.96
, pp. 2447-2453
-
-
Danen, W.C.1
West, C.T.2
-
21
-
-
0025644318
-
A chemical model for the pyridoxal 5′-phosphate dependent lysine aminomutases
-
Han O, Frey PA: A chemical model for the pyridoxal 5′-phosphate dependent lysine aminomutases. J Am Chem Soc 1990, 112:8982-8983.
-
(1990)
J Am Chem Soc
, vol.112
, pp. 8982-8983
-
-
Han, O.1
Frey, P.A.2
-
22
-
-
0026547534
-
Free radical in pyruvate formate-lyase is located on glycine 734
-
Volker Wagner AF, Frey M, Neugebauer FA, Schäfer W, Knappe J: Free radical in pyruvate formate-lyase is located on glycine 734. Proc Natl Acad Sci USA 1992, 89:996-1000.
-
(1992)
Proc Natl Acad Sci USA
, vol.89
, pp. 996-1000
-
-
Volker Wagner, A.F.1
Frey, M.2
Neugebauer, F.A.3
Schäfer, W.4
Knappe, J.5
-
23
-
-
0027320421
-
Pyruvate formate-lyase mechanism involving the protein-based glycyl radical
-
Knappe J, Elbert S, Frey M, Wagner AFV: Pyruvate formate-lyase mechanism involving the protein-based glycyl radical. Biochem Soc Trans 1993, 21:731-734.
-
(1993)
Biochem Soc Trans
, vol.21
, pp. 731-734
-
-
Knappe, J.1
Elbert, S.2
Frey, M.3
Wagner, A.F.V.4
-
24
-
-
0025363362
-
The anaerobic ribonucleotide reductase from Escherichia coli requires S-adenosylmethionine as activator
-
Eliasson R, Fontecave M, Jörnvall H, Krook M, Pontis E, Reichard P: The anaerobic ribonucleotide reductase from Escherichia coli requires S-adenosylmethionine as activator. Proc Natl Acad Sci USA 1990, 87:3314-3318.
-
(1990)
Proc Natl Acad Sci USA
, vol.87
, pp. 3314-3318
-
-
Eliasson, R.1
Fontecave, M.2
Jörnvall, H.3
Krook, M.4
Pontis, E.5
Reichard, P.6
-
25
-
-
13344279373
-
The free radical of the anaerobic ribonucleotide reductase from Escherichia coli is at glycine 681
-
Sun X, Öllagnier S, Schmidt PP, Atta M, Mulliez E, Lepape L, Eliasson R, Gräslund A, Fontecave M, Reichard P, Söberg BM: The free radical of the anaerobic ribonucleotide reductase from Escherichia coli is at glycine 681. J Biol Chem 1996, 271:6827-6831.
-
(1996)
J Biol Chem
, vol.271
, pp. 6827-6831
-
-
Sun, X.1
Öllagnier, S.2
Schmidt, P.P.3
Atta, M.4
Mulliez, E.5
Lepape, L.6
Eliasson, R.7
Gräslund, A.8
Fontecave, M.9
Reichard, P.10
Söberg, B.M.11
-
26
-
-
0029918138
-
The anaerobic Escherichia coli ribonucleotide reductase. Subunit structure and iron-sulfur center
-
Ollangnier S, Mulliez E, Gaillard J, Eliasson R, Fontecave M, Reichard P: The anaerobic Escherichia coli ribonucleotide reductase. Subunit structure and iron-sulfur center. J Biol Chem 1996, 271:9410-9416.
-
(1996)
J Biol Chem
, vol.271
, pp. 9410-9416
-
-
Ollangnier, S.1
Mulliez, E.2
Gaillard, J.3
Eliasson, R.4
Fontecave, M.5
Reichard, P.6
-
27
-
-
0029048182
-
Formate is the hydrogen donor for the anaerobic ribonucleotide reductase from Escherichia coli
-
Mulliez E, Ollagnier S, Fontecave M, Eliasson R, Reichard P: Formate is the hydrogen donor for the anaerobic ribonucleotide reductase from Escherichia coli. Proc Natl Acad Sci USA 1995, 92:8759-8762.
-
(1995)
Proc Natl Acad Sci USA
, vol.92
, pp. 8759-8762
-
-
Mulliez, E.1
Ollagnier, S.2
Fontecave, M.3
Eliasson, R.4
Reichard, P.5
-
29
-
-
0024378007
-
Protein radical formation in biological catalysis?
-
Stubbe J: Protein radical formation in biological catalysis? Annu Rev Biochem 1989, 58:257-285.
-
(1989)
Annu Rev Biochem
, vol.58
, pp. 257-285
-
-
Stubbe, J.1
-
33
-
-
0029841914
-
Electron paramagnetic resonance investigations of a kinetically competent intermediate formed in ribonucteotide reduction: Evidence for a thiyl radical-cob(II)alamin interaction
-
Gerfen GJ, Licht S, Willems J-P, Hoffman BM, Stubbe J: Electron paramagnetic resonance investigations of a kinetically competent intermediate formed in ribonucteotide reduction: Evidence for a thiyl radical-cob(II)alamin interaction. J Am Chem Soc 1996, 118:8192-8197. The electron paramagnetic resonance spectrum arising from freeze-quench experiments with adenosylcobalamin-dependent ribonucleotide reductase is quantitatively analyzed. The spectrum is satisfactorily simulated assuming a thiyl radical is coupled to cob(II)alamin by dipolar interactions and electron-electron exchange. Other radical coupling models did not allow the spectrum to be satisfactorily simulated.
-
(1996)
J Am Chem Soc
, vol.118
, pp. 8192-8197
-
-
Gerfen, G.J.1
Licht, S.2
Willems, J.-P.3
Hoffman, B.M.4
Stubbe, J.5
-
35
-
-
0027488863
-
The synthetic substrate succinyl[carbadethia]-CoA generates cob(II)alamin on adenosylcobalamin-dependent methylmalonyl CoA mutase
-
Keep NH, Smith GA, Evans MCW, Diakun GP, Leadlay PF: The synthetic substrate succinyl[carbadethia]-CoA generates cob(II)alamin on adenosylcobalamin-dependent methylmalonyl CoA mutase. Biochem J 1993, 295:387-392.
-
(1993)
Biochem J
, vol.295
, pp. 387-392
-
-
Keep, N.H.1
Smith, G.A.2
Evans, M.C.W.3
Diakun, G.P.4
Leadlay, P.F.5
-
36
-
-
0028097047
-
Electron paramagnetic resonance studies of the methylmalonyl-CoA mutase reaction. Evidence for radical intermediates using natural and artificial substrates as well as the competitive inhibitor 3-carboxypropylCoA
-
Zhao Y, Abend A, Such P, Rétey J: Electron paramagnetic resonance studies of the methylmalonyl-CoA mutase reaction. Evidence for radical intermediates using natural and artificial substrates as well as the competitive inhibitor 3-carboxypropylCoA. Eur J Biochem 1994, 225:891-896.
-
(1994)
Eur J Biochem
, vol.225
, pp. 891-896
-
-
Zhao, Y.1
Abend, A.2
Such, P.3
Rétey, J.4
-
37
-
-
0028899970
-
Evidence from electron paramagnetic resonance spectroscopy of the participation of radical intermediates in the reaction catalyzed by methylmalonyl coenzyme a mutase
-
Padmakumar R, Banerjee R: Evidence from electron paramagnetic resonance spectroscopy of the participation of radical intermediates in the reaction catalyzed by methylmalonyl coenzyme A mutase. J Biol Chem 1995, 270:9295-9300.
-
(1995)
J Biol Chem
, vol.270
, pp. 9295-9300
-
-
Padmakumar, R.1
Banerjee, R.2
-
38
-
-
33947087284
-
Polarographic and optical absorption studies of radicals produced in the pulse radiolysis of aqueous solutions of ethylene glycol
-
Bansal KM, Grätzel M, Henglein A, Janata E: Polarographic and optical absorption studies of radicals produced in the pulse radiolysis of aqueous solutions of ethylene glycol. J Phys Chem 1973, 77:16-19.
-
(1973)
J Phys Chem
, vol.77
, pp. 16-19
-
-
Bansal, K.M.1
Grätzel, M.2
Henglein, A.3
Janata, E.4
-
39
-
-
0030891240
-
Studies on the mechanism of ribonucleotide reductases
-
-1 in 1 M triethylammonium acetate at pH 7.
-
(1997)
J Am Chem Soc
, vol.119
, pp. 2784-2794
-
-
Lenz, R.1
Giese, B.2
-
40
-
-
0030896265
-
Evidence that cobalt-carbon bond homolysis is coupled to hydrogen atom abstraction from substrate in methylmalonyl-CoA nrtutase
-
3 malonyl CoA proceeded at one-twentieth the rate of methyl malonyl CoA.
-
(1997)
Biochemistry
, vol.36
, pp. 3713-3718
-
-
Padmakumar, Ru.1
Padmakumar, Ra.2
Banerjee, R.3
-
41
-
-
0014027350
-
Studies on the mechanism of cobamide coenzymes. Chemical properties of the enzyme-coenzyme complex
-
Wagner OW, Lee HA, Frey PA, Abeles RH: Studies on the mechanism of cobamide coenzymes. Chemical properties of the enzyme-coenzyme complex. J Biol Chem 1966, 211:1751-1762.
-
(1966)
J Biol Chem
, vol.211
, pp. 1751-1762
-
-
Wagner, O.W.1
Lee, H.A.2
Frey, P.A.3
Abeles, R.H.4
-
43
-
-
33747193400
-
Thermolysis of adenosylcobalamin: A product, kinetic, and Co-C5′ bond dissociation energy study
-
Finke RJ, Hay BP: Thermolysis of adenosylcobalamin: A product, kinetic, and Co-C5′ bond dissociation energy study. Inorg Chem 1984, 23:3041-3043.
-
(1984)
Inorg Chem
, vol.23
, pp. 3041-3043
-
-
Finke, R.J.1
Hay, B.P.2
-
44
-
-
0030912979
-
12-dependent methylmalonyl-CoA mutase
-
12-dependent methylmalonyl-CoA mutase. J Am Chem Soc 1997, 119:3057-3067. The paper reports that 1-methylimidazole as the lower axial ligand for adenosylcobinamide accelerates the thermal homolysis of the Co-C5′ bond relative to dimethylbenzimidazole. This pertains to the finding by Mancia et al. (1996) (45••) in the structure of methylmalonyl Coenzyme A mutase that the dimethylbenzimidazole of adenosylcobalamin is displaced by the imidazole ring of histidine.
-
(1997)
J Am Chem Soc
, vol.119
, pp. 3057-3067
-
-
Sirovatka, J.M.1
Finke, R.G.2
-
45
-
-
0030584657
-
How coenzyme B12 radicals are generated: The crystal structure of methylmalonyl-coenzyme a mutase at 2 a resolution
-
Mancia F, Keep NH, Nakagawa A, Leadlay PF, McSweeney S, Rasmussen B, Bösecke P, Diat O, Evans PR: How coenzyme B12 radicals are generated: the crystal structure of methylmalonyl-coenzyme A mutase at 2 A resolution. Structure 1996, 4:339-350. The three dimensional structure of methylmalonyl Coenzyme A (CoA) mutase with cob(II)alamin bound to the active site is reported. Major conformational changes accompany the binding of methylmalonyl CoA to this enzyme. In the enzyme substrate complex, the methylmalonyl group is very deeply buried and protected from the solvent.
-
(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
-
46
-
-
0000239991
-
Dioxygen activation by enzymes containing binuclear non-heme iron clusters
-
Waller BJ, Lipscomb JD: Dioxygen activation by enzymes containing binuclear non-heme iron clusters. Chem Rev 1996, 96: 2625-2657. This is a comprehensive review of the title subject.
-
(1996)
Chem Rev
, vol.96
, pp. 2625-2657
-
-
Waller, B.J.1
Lipscomb, J.D.2
-
47
-
-
0027913094
-
Crystal structure of a bacterial non-haem iron hydroxylase that catalyzes the biological oxidation of methane
-
Rosenzweig AC, Frederick CA, Lippard SJ, Nordlund P: Crystal structure of a bacterial non-haem iron hydroxylase that catalyzes the biological oxidation of methane. Nature 1993, 366:537-543.
-
(1993)
Nature
, vol.366
, pp. 537-543
-
-
Rosenzweig, A.C.1
Frederick, C.A.2
Lippard, S.J.3
Nordlund, P.4
-
48
-
-
0030943755
-
Crystal structure of the hydroxylase component of methane monooxygenase from Methylosinus trichosporium
-
Elango N, Radjakrishman R, Froland WA, Wallar BJ, Earhart CA, Lipscomb JD, Ohlendorf DH: Crystal structure of the hydroxylase component of methane monooxygenase from Methylosinus trichosporium. Protein Sci 1997, 6:556-568.
-
(1997)
Protein Sci
, vol.6
, pp. 556-568
-
-
Elango, N.1
Radjakrishman, R.2
Froland, W.A.3
Wallar, B.J.4
Earhart, C.A.5
Lipscomb, J.D.6
Ohlendorf, D.H.7
-
49
-
-
0025005005
-
Methane monooxygenase catalyzed-oxygenation of 1,1-dimethylcyclopropane. Evidence for radical and carbocationic intermediates
-
Ruzicka F, Huang D-S, Donnelly MI, Frey PA: Methane monooxygenase catalyzed-oxygenation of 1,1-dimethylcyclopropane. Evidence for radical and carbocationic intermediates. Biochemistry 1990, 29:1696-1700.
-
(1990)
Biochemistry
, vol.29
, pp. 1696-1700
-
-
Ruzicka, F.1
Huang, D.-S.2
Donnelly, M.I.3
Frey, P.A.4
-
50
-
-
0000353336
-
Radical clock substrate probes and kinetic isotope effect studies of the hydroxylation of hydrocarbons by methane monooxygenase
-
Liu KE, Johnson CC, Newcomb M, Lippard SJ: Radical clock substrate probes and kinetic isotope effect studies of the hydroxylation of hydrocarbons by methane monooxygenase. J Am Chem Soc 1993, 115:939-947.
-
(1993)
J Am Chem Soc
, vol.115
, pp. 939-947
-
-
Liu, K.E.1
Johnson, C.C.2
Newcomb, M.3
Lippard, S.J.4
-
51
-
-
0000765007
-
Cryptic stereospecificity of methane monoxygenase
-
Priestly ND, Floss HG, Froland WA, Lipscomb JD, Williams PG, Morimoto H: Cryptic stereospecificity of methane monoxygenase. J Am Chem Soc 1992, 114:7561-7562.
-
(1992)
J Am Chem Soc
, vol.114
, pp. 7561-7562
-
-
Priestly, N.D.1
Floss, H.G.2
Froland, W.A.3
Lipscomb, J.D.4
Williams, P.G.5
Morimoto, H.6
-
52
-
-
0030993949
-
Tritiated chiral alkanes as substrates for soluble methane monoxygenase from Methylococcus capsulatus (Bath): Probes for the mechanism of hydroxylation
-
-1, too fast for a discrete intermediate. They postulated a nonsynchronous concerted mechanism of oxygenation. Whether the rotational barrier in a homogeneous medium applies to the active site of MMO is open to question. A higher barrier, owing to the effect of a local magnetic field at the active site, would invalidate the calculated rebound rate constants and compel the adoption of lower values.
-
(1997)
J Am Chem Soc
, vol.119
, pp. 1818-1827
-
-
Valentine, A.M.1
Wilkinson, B.2
Liu, K.E.3
Komar-Panicucci, S.4
Priestly, N.D.5
Williams, P.G.6
Morimoto, H.7
Floss, H.G.8
Lippard, S.J.9
-
53
-
-
33947300410
-
Homoallylic rarrangement and electron spin resonance of cyclopropylcarbinyl radicals
-
Kochi JK, Kusic PJ, Eaton DR: Homoallylic rarrangement and electron spin resonance of cyclopropylcarbinyl radicals. J Am Chem Soc 1969, 91:1877-1879.
-
(1969)
J Am Chem Soc
, vol.91
, pp. 1877-1879
-
-
Kochi, J.K.1
Kusic, P.J.2
Eaton, D.R.3
-
55
-
-
0029836348
-
Cis-trans isomerization of a cyclopropyl radical trap catalyzed by extradiol catechol dioxygenases: Evidence for a semiquinone intermediate
-
Spence EL, Langley GJ, Bugg TDH: Cis-trans isomerization of a cyclopropyl radical trap catalyzed by extradiol catechol dioxygenases: Evidence for a semiquinone intermediate. J Am Chem Soc 1996, 118:939-947. For use in studies of the reaction of (2,3-dihydroxyphenyl)propionate 1,2-dioxygenase, cis- and trans-2-(2,3dihydroxyphenyl)cyclopropane-1-carboxylate were synthesized. Cis-trans isomerizalion of the cyclopropyl rings in these substrates was observed, but no ring-opened products were detected. It was concluded that the radical intermediate underwent cyclopropyl ring opening and reclosing, without trapping of the homoallylic radicals.
-
(1996)
J Am Chem Soc
, vol.118
, pp. 939-947
-
-
Spence, E.L.1
Langley, G.J.2
Bugg, T.D.H.3
-
57
-
-
0028172124
-
12-dependent ribonucleotide reductase: Evidence for the participation of five cysteine residues in ribonucleotide reduction
-
12-dependent ribonucleotide reductase: Evidence for the participation of five cysteine residues in ribonucleotide reduction. Biochemistry 1994, 33:12679-12685.
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(1994)
Biochemistry
, vol.33
, pp. 12679-12685
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Booker, S.1
Licht, S.2
Broderick, J.3
Stubbe, J.4
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