Catalysis Progress in Research: Proceedings of the NATO by C. Veeger (auth.), Fred Basolo, Robert L. Burwell Jr. (eds.)

By C. Veeger (auth.), Fred Basolo, Robert L. Burwell Jr. (eds.)

This convention on Catalysis was once held below the auspices ofthe NATO technological know-how Committee as a part of its carrying on with attempt to advertise the invaluable growth of technological know-how via overseas cooperation. The technology Committee meetings are intentionally designed and struc­ tured to concentration specialist cognizance on what's now not recognized, instead of what's recognized. The members are conscientiously chosen to compile various complementary viewpoints. via in depth team dialogue, they search to arrive contract on conclusions and suggestions for destiny examine with the intention to be of worth to the clinical group. We think that the endeavour has been rather winning within the pre­ despatched case. a few twenty-five papers, both within the type of reprints or specifically written stories have been contributed by way of the contributors for improve move, to stipulate the state-of-the paintings within the 3 parts ofheterogeneous, homogeneous and metalloenzyme catalysis and to concentration awareness on key difficulties. the provision of this history fabric precluded the necessity for long intro­ ductory displays and accepted swift initiation of interdisciplinary discussions. All members gave generously and enthusiastically in their services and energy throughout the week of the assembly, of ten long gone basic bedtime hours, and we expand to them our deep gratitude.

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Extra info for Catalysis Progress in Research: Proceedings of the NATO Science Committee Conference on Catalysis held at Santa Margherita di Pula, December 1972

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A. and PRESSMAN, D. (1967). Prac. Nat. Acad. Sci. , 58, 280. 16. E. (1958). Proc. Nat. Acad. Sei. , 44, 98. 17. T. M. (1971). Cold Spring Harbor Symposia on Quantitative Biology, 36, 517. 18. E. L. (1960). J. Biol. , 235, 390. 19. F. E. (1963). Prac. Nat. Acad. Sei. , 49, 109. 20. KEILIN, D. and MANN, T. (1940). Biochem. , 34, 1163. 21. H. (1967). Physiol. , 47, 595. 22. O. and STRANDBERG, B. (1971). The Enzymes, Vol. 5, 3rd edition, p. 587. T. (1968). Harvey Lectures 62, p. 191. 23. C. (1964).

C) Nucleophilic attack by Glu 270 upon the carbonyl carbon of the substrate. CATALYSIS BY METALLOENZYMES 17 This would appear to be an example of the metal in a metalloprotein act ing much like it is in the model esterase reaction pictured in equation (1), but its polarizing effect is probably assisted significantly by certain features of the nonaqueous protein environment. Most importantly, however, the rapid catalysis would appear to be made possible by a concerted reaction provided by the two protein reactive groups, Glu 270 and Tyr 248, reacting with the two ends of the peptide bond.

In other words an inorganic sulfide can be assigned to each face of the tetrahedron of 4 Fe atoms, each making 3 equivalent bonds to 3 Fe atoms. 36 JOSEPH E. COLEMAN Fig. 19. Iron-su1fur c1usters in Chromatium iron protein. The cluster is located in what is apparently a highly hydrophobic region of the molecule. AII but two of the apolar side-chains of the molecule lin~ the interface where the two halves of the molecule come together to enclose the cluster. Unless there is some relaxation in the molecule in solution, van der Waals contacts would appear to prevent accessibility of solvent to the cluster.

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