Биологический каталог




Биоорганическая химия

Автор Г.Дюга, К.Пенни

ion and carboxylate in a carboxvpeptidase model. J. Amer. Chem. Soc. 93, 7096—7097 (1971).

26. Lloyd G. /., Cooperman B. S. Nucleophilic attack by zinc(Il)-pyridine-2-car-baldoxime anion on phosphorylimidazole. A model for enzymatic phosphate transfer. J. Amer. Chem. Soc. 93, 4883—4889 (1971).

27. Sigman D. S., Jorgenren С. T. Models for metalloenzymes. The zinc(II)-catalyzed transesterification of Af-(|3-hydroxyethyl)ethylene-diamine by p-nitro-phenyl picolinate. J. Amer. Chem. Soc. 94, 1724—1730 (1972).

(228. Buckingham D. A., Collman I. P. Hydrolysis of N-terminal peptide bonds and amino acid derivatives by the (3-hydroxoaquotriethylenetetramine co-balt(III)ion. J. Amer. Chem. Soc. 89, 1082—1087 (1967).

E29. Buckingham D. A., Keen F. R., Sargeson A. M. Facile intramolecular hydrolysis of dipeptides and glycinamide. J. Amer. Chem. Soc. 96, 4981—4983

(1974) .

E30. Kimura E. Sequential hydrolysis of peptides with (3-hydroxoaquotriethylene-

tetraminecobalt(III)ion. Inorg. Chem. 13, 951—954 (1974). E31. Frieden F. Non-covalent interactions. J. Chem. Educ. 52, 754—761

(1975) .

E32. Hendrickson W. A. The molecular architecture of oxygen. Carrying proteins

Trends Biochem. Sci. 2, 108—111 (1977). ?33. Kendrew I. C. The three-dimensional structure of a protein molecule. Sci

Amer. 205, December, 96—110 (1961). E34. Epstein E. F., Bernal /., Batch A. L. Activation of molecular oxygen by a

metal complex. The formation and structure of the anion

[Ph3POFe(S2C2{CF3}2)2]©. Chem. Comm. 136—138 (1970). E35. Almog /., Baldwin I. E., Dyer R. I., Peters M. Condensation of tetraaldehy-

des with pyrrole. Direct synthesis of «capped» porphyrins. J. Amer. Chem

Soc. 97, 226—227 (1975). E36. Almog J., Baldwin I. E., Huff J. Reversible oxygenation and autooxidation

of a «capped» porphyrin iron (II) complex. J. Amer. Chem. Soc. 97, 227—228

(1975).

E37. Traylor T. G. Bioorganic Chemistry (E. E. van Tamelen, Ed.), Vol IV pp. 437—468. Academic Press, New York, 1978.

498

Литература

238. Chang С. К-, Traylor Т. G. Synthesis of the myoglobin active site. Proc. Nat Acad. Sci. USA 78, 2647—2650 (1973).

239. (a) Chang С. K., Traylor T. G. Solution behavior of a synthetic myoglobin active site. J. Amer. Chem. Soc. 95, 5810—5811 (1973). (b) Chang С. Traylor T. G. Neighboring group effect in heine-carbon monoxide binding J. Amer. Chem. Soc. 95, 8475—8477 (1973). (c) Chang С. K., Traylor T. G. Proximal base influence on the binding of oxigen and carbon monoxide to heme. J. Amer. Chem. Soc. 95, 8477—8479 (1973).

240. Traylor T. G., Campbell D., Tsuchiya S. Cyclophane porphyrin. 2. Models for steric hindrance to CO ligation in hemoproteins. J. Amer. Chem. Soc. 101, 4748—4749 (1979).

241. Bayer E., Holzbach G. Synthetic homopolymers for reversible binding of molecular oxygen. Angew. Chem., Int. Ed. Engl. 16, 117—118 (1977).

242. Collman I. P. Synthetic models for the oxygen-binding hemoproteins. Acc Chem. Res. 10, 265—272 (1977).

243. Collman J. P., Brauman I. L., Rose E., Suslick K. S. Cooperativity in 02 binding to iron porphyrins. Proc. Nat. Acad. Sci. USA 75, 1052—1055 (1978).

244. Farrell A/., Dolphin D. H., James B. R. Reversible binding of dioxygen to ruthenium(II) porphyrins. J. Amer. Chem. Soc. 100, 324—326 (1978).

245. Molinaro F. S., Little R. G., Ibers J. A. Oxygen binding to a model for the active site in cobalt-substituted hemoglobin. J. Amer. Chem. Soc. 99, 5628— 5632 (1977).

246. Collman J. P., Brauman I. I., Doxsee К. M., Halbert T. R., Hayes S. E., Suslick K. S. Oxygen binding to cobalt porphyrins. J. Amer Chem. Soc. 100, 2761—2766 (1978).

247. Wasielewski M. R., Svec W. A., Cope В. T. Bis (chlorophyll) cyclophanes, new models of special pair chlorophyll. J. Amer. Chem. Soc. 100, 1961—1962

(1978) .

248. Malkin R. Iron-Sulfur Proteins, Vol. II, Academic Press, New York, 1973.

249. Holm R. H. Synthetic approaches to the active sites of iron-sulfur proteins. Acc. Chem. Res. 10, 427—434 (1977).

250. Eichhorn G. L. Inorganic Biochemistry, Vols. 1 and 2, Elsevier, New York, 1973.

251. Amundsen A. R., Whelan J., Bosnich B. Biological analogues. On the nature of the binding sites of copper-containing proteins. J. Amer. Chem. Soc. 99, 6730—6739 (1977).

252. Gagne R. R., Allison J. L., Gall R. S., Koval C. A. Models for copper-containing proteins: Structure and properties of novel five-coordinate copper (I) complexes. J. Amer Chem. Soc. 99, 7170—7178 (1977).

253. Buckingham D. A., Gunter M. J., Mander L. N. Synthetic models for bis-metallo active sites, A prophyrin capped by a tetrakis(pyridine) ligand system. J. Amer. Chem. Soc. 100, 2899—2901 (1978).

254. Agnus Y., Louis R., Weiss R. Bimetallic copper(I) and (II) macrocyclic complexes as mimics for type 3 copper pairs in copper enzymes. J. Amer. Chem. Soc. 101, 3381—3384 (1979).

255. Coughlin P. Dewan J. C., Lippard S. J., Watanabe ?., Lehn J.-M. Synthesis and structure of the imidazolate bridged dicopper (II)ion incorporated into a circular cryptate macrocycle. J. Amer. Chern. Soc. 101, 265—266

(1979) .

256. Abeles R. H., Dolphin D. The vitamin B|2 coenzyme. Acc. Chem Res. 9, 114—120 (1974).

257. Rctey J., Ulmani-Ronchi A., Seibl J., Arigoni D. Zum mechanismus der Pro-pandioldehydrase-Reaktion. Experentia 22, 502—503 (1966).

258. Schrauzer G. N. Organocobalt chemistry of vitamin BI2 model compounds (cobaloximes). Acc. Chem. Res. 1, 97—103 (1968).

259. Schrauzer G. N. New developments in the field of vitamin Bi2: Reactions of the cobalt atom in corrins and in vitamin B12 model compounds. Angew'. Chem., Int. Ed. Engl. 15, 417—426 (1976).

Литература

499

КО. Schrauzer G. N. New developments in the field of vitamin B12: Enzymatic reactions dependent upon corrins and coenzyme Bi2. Angew. Chem., Int. Ed. I Engl. 16, 233—244 (1977). j61. Silverman R. В., Dolphin D. A direct method for cobalt-carbon bond formation in cobalt(III)-containing cobalamins and cobaloximes. Further support I for cobalt(Ill) я-complexes in coenzyme Bi2 dependent rearrangements. \ J. Amer. Chem. Soc. 95, 1686—1688 (1973).

162. Silverman R. В., Dolphin D. Reaction of vinyl ethers with cobalamins and I cobaloximes. J. Amer. Chem. Soc. 96, 7094—7096 (1974).

163. Silverman R. В., Dolphin D., Carty T. Л, Krodel E. K., Abeles R. H. Formyl-[ methylcobalamin. J. Amer. Chem. Soc. 96, 7096—7097 (Ш74).

164. Dowd P., Trivedi В. K., Shapiro M., Marwaha L. K. Vitamin B12 model studies. Migration of the acrylate fragment in the carbon-skeleton rearrangement leading to a-methyleneglutaric acid. J. Amer. Chem. Soc. 98, 7875—7877 (1976).

|65. Salem L., Eisentein O., Anh N. Т., Burgi H. В., Devaquet A., Segal G., Veil-I lard A. Enzymatic catalysis. A theoretically derived transition state for coen-I zyme B12-catalyzed reaction. Nouv. J. Chim. 1, 335—347 (1977). 1б6. Flohr H., Paunhorst N., Retey J. Synthesis, structure determination, and rearrangement of a model for the active site of methylmalonyl-CoA mutase with incorporated substrate. Angew. Chem., Int. Ed. Engl. 15, 561—562 (1976). ¦67. Breslow R., Khanna P. L. An intramolecular model for the enzymatic insertion of coenzyme B12 into unactivated carbon-hydrogen bonds. J. Amer. Chem. * Soc. 98, 1297—1299 (1976). ¦68. Corey E. J., Cooper N. J., Green M. L. H. Biochemical catalysis involving coenzyme Bi2: A rational stepwise mechanistic interpretation of vicinal interim change rearrangements. Proc. Nat. Acad. Sci. USA 74, 811—815 (1977). J69. Toraya Т., Krodel E., Mildran A S., Abeles R. H. Role of peripheral side chains of vitamin B12 coenzymes in the reaction catalyzed by dioldehydrase. -Biochemistry 18, 417—426 (1979). fro. Sato K., Hiei E., Shimizu S., Abeles R. Affinity chromatography of W5-methyl-' tetrahydrofolate-homocysteine methyltransferase on a cobalamin-Sepharose. 1 FEBS Lett. 85, 73—76 (1978). ¦71. Wood J. M. Biological cycles for toxic elements in the environment. Science

183, 1049—1052 (1974). 172. Thayer I. S. Teaching bio-organometal chemistry. II. The metals. J. Chem.

I Educ. 54, 662—665 (1977). ¦73. Metzler A. E. Biochemistry, The Chemical Reactions of Living Cells, Chap. 8.

I Academic Press, New York, 1977. ¦74. DiSabato G. Adducts of diphosphopyridine nucleotide and carbonyl compo-

I unds. Biochemistry 9, 4594—4600 (1970). ¦75. Greighton D. I., Sigman D. S. A model for alcohol dehydrogenase. The zinc ion catalyzed reduction of l,10-phenanthroline-2-carboxaldehyde by N-pro-pyl-l,4-dihydronicotinamide. J. Amer. Chem. Soc. 93, 6314—6316 (1971). ¦76. Grau U., Kapmeyer H., Trommer W. E. Combined coenzyme-substrate analogues of various dehydrogenases. Synthesis of (3S)- and (3R)-5-(3-carboxy-3-hydroxypropyl) nicotinamide adenine dinucleotide and their interaction with (S)-and (R)-lactate-specific dehydrogenases. Biochemistry 17, 4621—4626 (1978).

¦77. van Bergen J. Т., Kellogg R. M. A crown ether NAD(P)H mimic. Complexation with cations and enhanced hydride donating ability toward sulfonium salts. J. Amer. Chem. Soc. 99, 3882—3884 (1977).

p78. Behr J. P., Lehn J. M. Enhanced rates of dehydropyridine to pyridinium hydrogen transfer in complexes of an active macrocyclic receptor molecule. Chem. Comm. 143—146 (1978).

¦79. Hamilton G. A. Progress in Bioorganic Chemistry (E. T. Kaiser, T. J. Kezdy, Eds.), Vol. 1, pp. 83—137. Wiley-Interscience. New York, 1971. 80. Eklund H., Nordstrom В., Zeppezauer E., Soderlund G., Ohlsson /., Boiwe Г., Soderberg В. O., Tapia O., Branden С. I. Three-dimensional structure of

500

Литература

horse liver alcohol dehydrogenase at 2.4 A resolution. J. Mol. Biol. 102, 27—59 (1976).

281. Suckling C. J., Wood H. C. S. Should organic chemistry meddle in biochemistry? Chem. Br. 5, 243—248 (1979).

282. Irwin A. J., Jones J. B. Stereoselective horse liver alcohol dehydrogenase catalyzed oxidoreductions of some bicyclic [2.2.1] and [3.2.1] ketones and also-hols. J. Amer. Chem. Soc.

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