Literature summary for 1.15.1.1 extracted from

Whittaker, M.M.; Mizuno, K.; Baechinger, H.P.; Whittaker, J.W.
Kinetic analysis of the metal binding mechanism of Escherichia coli manganese superoxide dismutase (2006), Biophys. J., 90, 598-607.

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Metals/Ions

Metals/Ions	Comment	Organism	Structure
Manganese	kinetic study on metal binding mechanism. Apo-enzyme metallation kinetics are gated, zero order in metal ion for both native Mn2+ and nonnative Co2+. Cobalt-binding reveals two exponential kinetic processes. Sensitivity of metallated protein to exogenously added chelator decreases with time, consistent with annealing of an initially formed metalloprotein complex	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	manganese superoxide dismutase	-

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Release 2023.1 (January 2023)