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Lah, M.S., Dixon, M.M., Pattridge, K.A., Stallings, W.C., Fee, J. A. and Ludwig, M. L. (1995) Structure-function in Escherichia coli iron superoxide dismutase: Comparisons with the manganese enzyme from Thermus thermophilus. Biochemistry, 34, 1646-1660.
http://dx.doi.org/10.1021/bi00005a021

has been cited by the following article:

• TITLE: GroESL protects superoxide dismutase (SOD)— Deficient cells against oxidative stress and is a chaperone for SOD

  AUTHORS: Gary J. Hunter, Thérèse Hunter

  KEYWORDS: Superoxide Dismutase; Chaperone; Heat Shock; Oxidative Stress

  JOURNAL NAME: Health, Vol.5 No.10, October 21, 2013

  ABSTRACT: Superoxide dismutase (SOD)-deficient Escherichia coli OX326Acells are protected against chemically-induced oxidative stress by expression of the chaperonin GroESL. This protection is equivalent to expression of superoxide dismutase even though GroESL has no inherent SOD activity. Co-overexpression of GroESL and SOD in the same cells results in higher protein yields of SOD and greater metallation of SOD when compared with expression of SOD alone. Greater metallation results in the higher specific activity of SOD that is observed in heat shock, and is not due to increased synthesis of SOD mRNA or protein.