Биологический каталог




Биоорганическая химия

Автор Г.Дюга, К.Пенни

98, 8476—8482 (1976).

283. Irwin A. J., Jones J. B. Regiospecific and enantioselective horse liver alcohol dehydrogenase catalyzed oxidations of some hydroxycyclopentanes. J. Amer. Chem. Soc. 99, 1625—1630 (1977).

284. Jones J. В., Beck J. F. Application of Biochemical Systems in Organic Chemistry, In: Techniques of Chemistry Series (J. B. Jones, C. J. Sih, D. Perlman, Eds.), Part I, pp. 107—401. Wiley, New York, 1976.

285. Prelog V. Specification of the stereochemistry of some oxidoreductases by diamond lattice sections. Pure Appl. Chem. 9, 119—130 (1964).

286. Creighton D. J., Hajdu J., Mooser G., Sigman D. S. Model dehydrogenase reactions. Reduction of N-methylaeridinium ion by reduced nicotinamide adenine dinucleotide and its derivatives. J. Amer. Chem. Soc. 95, 6855—6867 (1973).

287. Brilstlein M., Bruice Т. C. Demonstration of a direct hydrogen transfer between NADH and a deazaflavin. J. Amer. Chem. Soc. 94, 6548—6549 (1972).

288. Fisher J., Walsh C. Enzymatic reduction of 5-deazariboflavine from reduced nicotinamide adenine dinucleotide by direct hydrogen transfer. J. Amer. Chem. Soc. 96, 4345—4346 (1974).

289. Eirich D., Vogels G., Wolfe R. Proposed structure of coenzyme F420 from Methanobacterium. Biochemistry 17, 4583—4593 (1978).

290. Hemmerich P., Massey V., Weber G. Photo-induced benzyl substitution of flavins by phenylacetate: A possible model for Havoprotein catalysis. Nature 213, 728—730 (1967).

291. Sayer J. M., Conlon P., Hupp J., Fancher J., Belanger R., White E. I. Reduction of l,3-dimethyl-5-(p-nitrophenylimino) barbituric acid by thiols. A high-velocity flavin model reaction with an isolable intermediate. J. Amer. Chem. Soc. 101, 1890—1893 (1979).

292. Rastetter W. H., Gadek T. R., Tone J. P., Frost J. W-. Oxidations and oxygen transfer effected by a flavin N(5)-oxide. A model for flavin-dependent mono oxygenases. J. Amer. Chem. Soc. 101, 2228—2231 (1979).

293. Orf H. W., Dolphin D. Oxaziridines as possible intermediates in flavin mono oxygenases. Proc. Nat. Acad. Sci. USA 71, 2646—2650 (1974).

294. Vargo D., Jams M. S. Synthesis of a 4a,5-epoxy-5-deazaflavin derivatives J. Amer. Chem. Soc. 101, 7623—7626 (1979).

295. Jerina D. M., Daly J. W., Witkop В., Zaltzman-Nirenberg S., Udenfriend S. 1,2-Naphthalene oxide as an intermediate in the microsomal hydroxylation of naphthalene. Biochemistry 9, 147—156 (1969).

296. Guroff G., Daly J. W., Jerina D. M., Rensen J., Witkop В., Udenfriend S Hydroxylation-induced migration: The NIH shift. Science 157,1524—1530 (1967).

297. Fox J. L. Chemists attack complex organic mechanisms. Chem. Eng. News May 22, pp. 28—30 (1978).

298. Adam W., Alzerreca A., Liu J. E., Yany F. a-Peroxylactones via dehydrative cyclization of a-hydroperoxy acids. J. Amer. Chem. Soc. 99, 5768—5773 (1977).

299. Kemal C., Bruice Т. C. Simple synthesis of a 4a-hydroperoxy adduct ol 1,5-dihydroflavine: Preliminary studies of a model for bacterial luciferase. Proc. Nat. Acad. Sci. USA 73, 995—999 (1976).

300. Schmidt S. P., Schuster G. B. Dioxetanone chemiluminescence by the chemically initiated electron exchange pathway. Efficient generation of excited singlet states. J. Amer. Chem. Soc. 100, 1966—1968 (1978).

301. Lowe J. N., Ingraham L. L. An Introduction to Biochemical Reactions Mechanisms, Chap. 3. Foundation of Molecular Biology Series. Prentice-Hall, Eng-lewood Cliffs, New Jersey, 1974.

Литература

501

302. Gansow О. A., Holm R. И. A proton resonance investigation of equilibra, solute structures, and transamination in the aqueous systems pyridoxamine-pyruvate-zinc(II) and aluminium (III). J. Amer. Chem. Soc. 91, 5984—5993 (1969).

B03. Blum M., Thanassi J. W. Metal ion induced reaction specific in vitamin B6 model systems. Bioorg. Chem. 6, 31—41 (1977).

B04. Belleau В., Burba I. The stereochemistry of the enzymic decarboxylation of amino acids. J. Amer. Chem. Soc. 82, 5751—5752 (1960).

|S05. Dunathan H. C., Davis L., Kury P. G., Kaplan M. The stereochemistry of enzymatic transamination. Biochemistry 7, 4532—4536 (1968).

1306. Dunathan H. C., Voet I. G. Stereochemical evidence for the evolution of pyridoxal-phosphate enzymes of various function from a common ancestor. Proc. Nat. Acad. Sci. USA, 71, 3888—3891 (1974).

fe07. Roitenan J. N-, Cram D. J. Electrophilic substitution at saturated carbon. XLV. Dissection of mechanisms of base-catalyzed hydrogen-deuterium exchange of carbon acids into inversion, isoinversion, and racemization pathways. J. Amer. Chem. Soc. 90 ,2225—2230 (1971).

B08. Roitenan J. N., Cram D. J. Electrophilic substitution at saturated carbon. XLVI. Crown ethers' ability to alter role of metal cations in control of stereochemical fate of carbanions. J. Amer. Chem. Soc. 90, 2231—2241 (1971).

B09. Cram D. J., Ford W. Т., Gosser L. Electrophilic substitution and saturated carbon. XXXVIII. Survey of substituent effects on stereochemical fate of fluorenyl carbanions. J. Amer. Chem. Soc. 90, 2598—2606 (1968).

B10. Broadhurst M. D., Cram D. J. A model for the proton transfer stages of the biological transaminations and isotopic exchange reactions of amino acids. J. Amer. Chem. Soc. 96, 581—583 (1974).

fell. Jaeger D. A., Broadhurst M. D., Cram D. J. Electrophilic substitution at saturated carbon. 52. A model for the proton transfer steps of biological transamination and the effect of a 4-pyridyl group on the base-catalyzed racemization of a carbon acid. J. Amer. Chem. Soc. 101, 717—732 (1979).

В12. Baker B. R. Design of Active-Site-Directed Irreversible Enzyme Inhibitors. Wiley, New York, 1967.

B13. Abeles R. H., Maycock A. L. Suicide enzyme inactivators. Acc. Chem. Res. 9, 313—319 (1976).

В14. Schoellmann G., Shaw E. Direct evidence for the presence of histidine in

the active center of chymotrypsin. Biochemistry 2, 252—255 (1963). 315. Walsh C. Chemical approaches to the study of enzymes catalyzing redox

transformations. Annu. Rev. Biochem. 47, 881—931 (1978). B16. Chowdhry V., Westheimer F. H. Photoaffinity labeling of biological systems.

Annu. Rev. Biochem. 48, 293—325 (1979). В17. Stryer L. Fluorescence energy transfer as a spectroscopic ruler. Annu. Rev.

Biochem. 47, 819—846 (1978). 318. Rando R. R. Mechanisms of action of naturally occuring irreversible enzyme

inhibitors. Acc. Chem. Res. 8, 281—288 (1975). B19. Rando R. R. Chemistry and enzymology of kcat inhibitors. Science 185,

320—324 (1974).

B20. Fasella P., John R. Substrate analogues as specific inhibitors of pyridoxal-dependent enzymes. Proc. 4th Int. Congr. Pharmacol. 5, 184—186 (1969).

321. Morino Y., Okamoto M. Labeling of the active site of cytoplasmic aspartate amino transferase by R-chloro-L-alanine. Biochem. Biophys. Res. Commun. 50, 1061—1067 (1973).

322. lung M. J., Metcalf B. W. Catalytic inhibition of y-aminobutyric acid a-keto-glutarate transaminase of bacterial origin by 4-aminohex-5ynoic acid, a substrate analog. Biochem. Biophys. Res. Commun. 67, 301—306 (1975).

323. Rando R. R., de Mairena J. Propargyl amine-induced irreversible inhibition of non-flavin-linked amine oxidases. Biochem. Pharmacol. 23, 463—466 (1974).

[324. Breslow R. On the mechanism of thiamine action. IV. Evidence from studies on model systems. J. Amer. Chem. Soc. 80, 3719—3726 (1958).

502

Литература

325. Gatlo A. A., Sable Н. Z. Coenzyme interactions. VIII. 13C-NMR studies of thiamine and related compounds. J. Biol. Chem. 249, 1382—1389 (1974).

326. Jordan F., Mariam Y. H. W-Methylthiaminium diiodide. Model study on the effect of a coenzyme bound positive charge on reaction mechanism requiring thiamine pyrophosphate. J. Amer. Chem. Soc 100, 2534—2541 (1978).

327. White F., Ingraham L. L. Mechanism of thiamine action: A model of 2-acyl-thiamine. J. Amer. Chem. Soc. 84, 3109—3111 (1962).

328. Bruice Т. C, Benkovic S. Bioorganic Mechanisms. Vol. 2, Chap. 8, p. 217 Benjamin, New York, 1966.

329. Rastetter W. H., Adams J., Frost J. W., Nummy L. J., Frommer J. ?., Roberts К. B. On the involvement of lipoic acid in a-keto acid dehydrogenase complexes. J. Amer. Chem. Soc. 101, 2752—2753 (1979).

330. Bruice Т. C, Hegarty A. F. Biotin-bound C02 and the mechanism of enzymatic carboxylation reactions. Proc. Nat. Acad. Sci. USA 65, 805—809 (1970).

331. Caplow M., Yager M. Studies on the mechanism of biotin catalysis. H.J. Amer. Chem. Soc. 89, 4513—4521 (1976).

332. Guchhait R. В., Polakis S. E., Hollis D., Fenselau C., Lane M. D. Acetyl coenzyme A carboxylase system of E. coli. Site of carboxylation of biotin and enzymatic reactivity of I'-N-(ureido)-carboxybiotin derivatives. J. Biol. Chem. 249, 6646—6656 (1974).

333. Whitney P. A., Cooper T. G. Urea carboxylase and allophanate hydroxylase Two components of ATP: Urea-lyase in 5. cerevisiae. J. Biol. Chem. 247, 1349—1353 (1972).

334. Kluger R., Davis P., Adawadkar P. D. Mechanism of urea participation in phosphonate ester hydrolysis. Mechanistic and stereochemical criteria for enzymic formation and reaction of phosphorylated biotin. J. Amer. Chem. Soc. 101, 5995—6000 (1979).

335 Arigoni D., Lynen F., Retey J. Stereochemie der enzymatischen Carboxylie-rung von (2R)-2-3H-Propionyl-CoA. Helv. Chim. Acta 49, 311—316 (1966).

336. Retey J., Lynen F. Zur biochemischen Funktion des Biotins. IX Der steri-sche Verlauf der Carboxylierung von Propionyl-CoA. Biochem. Z 342, 256— 271 (1965).

337. Kluger R., Pike D. C. Chemical synthesis of a proposed enzymegenerated «reactive intermediate analogue* derived fiom thiamine diphosphate. Self-activation of pyruvate dehydrogenase by conversion of the analogue in its components. J. Amer. Chem. Soc. 101, 6425—6428 (1979).

338. Moss /., Lane M. D. The biotin-dependent enzymes. Adv. Enzymol. 35, 321—442 (1971).

339. Wood H. G., Burden R. E Biotin enzymes. Annu. Rev. Biochem. 46, 385—413 (1977).

340. Mildvan A. S. Magnetic resonance studies of the conformations of enzyme-bound substrates. Acc. Chem. Res. 10, 246—252 (1977).

341. Klu

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