Literature summary for 2.8.1.6 extracted from

Tao, L.; Stich, T.A.; Fugate, C.J.; Jarrett, J.T.; Britt, R.D.
EPR-derived structure of a paramagnetic intermediate generated by biotin synthase BioB (2018), J. Am. Chem. Soc., 140, 12947-12963 .

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P12996	-	-

Cofactor

Cofactor	Comment	Organism	Structure
[2Fe-2S]-center	a reaction intermediate includes Arg260 as a deprotonated guanidino group, coordinated to the ferrous iron of the auxiliary [2Fe-2S] cluster as a monodentate ligand. The 9-mercaptodethiobiotin C9 is covalently coordinated to the auxiliary [2Fe-2S] cluster, which maintains the geometric and electronic structure characteristics of a typical reduced [2Fe-2S]+ cluster, with most of the spin density localized on the cluster and only a small positive spin density residing on the 9-mercaptodethiobiotin ligand via through-bond (C9 and my-thiolate) spin delocalization. C6, the target of the second hydrogen-atom abstraction, is now located in close proximity to the newly acquired thiolate sulfur	Escherichia coli

General Information

General Information	Comment	Organism
physiological function	a semistable intermediate in the formation of the first C-S bond is 9-mercaptodethiobiotin linked to a paramagnetic [2Fe-2S] cluster through one of its bridging sulfides. C6, the target of the second hydrogen-atom abstraction, is now in close proximity to the nascent thioether sulfur and is ideally positioned for the second C-S bond forming event	Escherichia coli

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Release 2023.1 (January 2023)