Thermus thermophilus superoxide dismutase

M.S. Lah, M.M. Dixon, K.A. Pattridge, W.C. Stallings, J.A. Fee, and M.L. Ludwig, Structure-function in Escherichia coli iron superoxide dismutase comparisons with the manganese enzyme from Thermus thermophilus. Biochemistry. 34, 1646-1660 (1995). 

Manganese can also be a catalyst. Manganese [as Mn(III)] in superoxide dismutase from Thermus thermophilus (Stallings et al., 1984, 1985) is surrounded by three histidines, one aspartate oxygen, and water in a trigonal bipyramidal arrangement. The fifth coordination site is occupied by a water molecule. In copper, zinc-superoxide dismutase (Cu,Zn = SOD), as described later, there are two metals (copper and zinc). Each bonds to and are separated by this same histidine group. 

Stallings WC, Patteidge KA, Strong RK and Ludwig ML (1985) The structure of manganese superoxide dismutase from Thermus thermophilus HB8 at 2.4-A resolution. J Biol Chem 260 16424-16432. 

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