By Zard S.Z.

This sequence is designed to supply a car within which investigators, who've confirmed a excessive measure of competence in a few point of unfastened radical chemistry, can current a selected niche. The sequence features a wide array of themes that are of present curiosity.

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Commun. 1995,277,1231-1237. 43. ; Nunzi, F; Marquet, A. Biochem. Biophys. Res. Commun. 1997,236,402-406. 44. Duin, E. C; Lafferty, M. ; Grouse, B. ; Allen, R. ; et al. Biochemistry 1977,55,11011-11020. 45. ; Reichard, P. Proc. Natl. Acad. Sci. USA 1995,92,8759-8762. 46. Aberhart, D. J. / Chem. Soc. Perkin Trans. 1988, 7, 343-350. 47. Aberhart, D. J. / Chem. Soc. Perkin Trans. 1988, 7,2119-2122. 48. Orme-Johnson, W. ; Orme-Johnson, N. R. In Iron-Sulfur Proteins-, Spiro, T. ; John Wiley & Sons: New York, 1982; p.

Biochem. Biophys. 1983,222, 333-362. 53. ; Rigus, G. Phys. Rev. Lett. 1985,54,599-602. 54. Holm, R. ; Ibers, J. A. ; Academic Press: New York, 1977; Vol. Ill, p. 246. 55. Petrovich, R. M. D. Thesis, University of Wisconsin-Madison, 1992. 56. ; Neugebauer, F. ; Blaschkowski, H. ; Ganzler, M. Proc. Natl, Acad. ScL USA 1984,8], 1332-1335. 57. Stubbe, J. Annu. Rev. Biochem. 1989,58,257-285. 58. Floriani, C; Calderazzo, E J. Chem. Soc. A 1971,3665-3669. 59. ; Saito,T; Uchida, Y; etal. / Am. Chem. 5oc.

As in the case of the ARR, this would be the active form of the enzyme. Presently, this is not supported by activity assays, since there is no significant difference in in vitro activity among the various enzyme forms [Fe2S2]^% [Ft^S^]'^\ and [Fe4S4]*. ^ The stoichiometry of the biotin synthase reaction with respect to SAM has been investigated in both enzyme systems. When biotin synthase from either E. coli or B. "*^ The products were shown to be 5'-deoxyadenosine and methionine. The authors interpret this as support for the mechanism shown in Scheme 3, in which two hydrogen-atom abstractions are needed to bring about conversion to the final product.

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