Literature summary for 4.99.1.2 extracted from

Parks, J.M.; Guo, H.; Momany, C.; Liang, L.; Miller, S.M.; Summers, A.O.; Smith, J.C.
Mechanism of Hg-C protonolysis in the organomercurial lyase MerB (2009), J. Am. Chem. Soc., 131, 13278-13285.

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Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P77072	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
RHg+ + H+	-	Escherichia coli	RH + Hg2+	-	?

Synonyms

Synonyms	Comment	Organism
merB	-	Escherichia coli
organomercurial lyase	-	Escherichia coli

General Information

General Information	Comment	Organism
additional information	quantum chemical calculations have been performed to compare the two chief candidate mechanisms for the Hg-C protonolysis catalyzed by the organomercurial lyase, MerB. The coordination of R-Hg(II) by two cysteine thiolates is necessary and sufficient to activate the Hg-C bond toward protonolysis.	Escherichia coli

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Release 2023.1 (January 2023)