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603 related items for PubMed ID: 9485408
1. S-Adenosylmethionine-dependent reduction of lysine 2,3-aminomutase and observation of the catalytically functional iron-sulfur centers by electron paramagnetic resonance. Lieder KW, Booker S, Ruzicka FJ, Beinert H, Reed GH, Frey PA. Biochemistry; 1998 Feb 24; 37(8):2578-85. PubMed ID: 9485408 [Abstract] [Full Text] [Related]
2. Coordination and mechanism of reversible cleavage of S-adenosylmethionine by the [4Fe-4S] center in lysine 2,3-aminomutase. Chen D, Walsby C, Hoffman BM, Frey PA. J Am Chem Soc; 2003 Oct 01; 125(39):11788-9. PubMed ID: 14505379 [Abstract] [Full Text] [Related]
7. How an enzyme tames reactive intermediates: positioning of the active-site components of lysine 2,3-aminomutase during enzymatic turnover as determined by ENDOR spectroscopy. Lees NS, Chen D, Walsby CJ, Behshad E, Frey PA, Hoffman BM. J Am Chem Soc; 2006 Aug 09; 128(31):10145-54. PubMed ID: 16881644 [Abstract] [Full Text] [Related]
12. Role of the [4Fe-4S] cluster in reductive activation of the cobalt center of the corrinoid iron-sulfur protein from Clostridium thermoaceticum during acetate biosynthesis. Menon S, Ragsdale SW. Biochemistry; 1998 Apr 21; 37(16):5689-98. PubMed ID: 9548955 [Abstract] [Full Text] [Related]
13. Binding energy in the one-electron reductive cleavage of S-adenosylmethionine in lysine 2,3-aminomutase, a radical SAM enzyme. Wang SC, Frey PA. Biochemistry; 2007 Nov 13; 46(45):12889-95. PubMed ID: 17944492 [Abstract] [Full Text] [Related]
16. An adaptable spectroelectrochemical titrator: the midpoint reduction potential of the iron-sulfur center in lysine 2,3-aminomutase. Hinckley GT, Frey PA. Anal Biochem; 2006 Feb 01; 349(1):103-11. PubMed ID: 16384547 [Abstract] [Full Text] [Related]
17. The novel structure and chemistry of iron-sulfur clusters in the adenosylmethionine-dependent radical enzyme biotin synthase. Jarrett JT. Arch Biochem Biophys; 2005 Jan 01; 433(1):312-21. PubMed ID: 15581586 [Abstract] [Full Text] [Related]