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本文引用的文献
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The [4Fe-4S](2+) cluster in reconstituted biotin synthase binds S-adenosyl-L-methionine.
J Am Chem Soc. 2002 Nov 27;124(47):14006-7. doi: 10.1021/ja0283044.
2
An anchoring role for FeS clusters: chelation of the amino acid moiety of S-adenosylmethionine to the unique iron site of the [4Fe-4S] cluster of pyruvate formate-lyase activating enzyme.
J Am Chem Soc. 2002 Sep 25;124(38):11270-1. doi: 10.1021/ja027078v.
3
Electron-nuclear double resonance spectroscopic evidence that S-adenosylmethionine binds in contact with the catalytically active [4Fe-4S](+) cluster of pyruvate formate-lyase activating enzyme.
J Am Chem Soc. 2002 Mar 27;124(12):3143-51. doi: 10.1021/ja012034s.
4
Reductive cleavage of S-adenosylmethionine by biotin synthase from Escherichia coli.
J Biol Chem. 2002 Apr 19;277(16):13449-54. doi: 10.1074/jbc.M111324200. Epub 2002 Feb 7.
5
Coordination of adenosylmethionine to a unique iron site of the [4Fe-4S] of pyruvate formate-lyase activating enzyme: a Mössbauer spectroscopic study.
J Am Chem Soc. 2002 Feb 13;124(6):912-3. doi: 10.1021/ja017562i.
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Structural evidence that the methionyl aminopeptidase from Escherichia coli is a mononuclear metalloprotease.
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Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods.
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