Abstract
Although manganese has been long recognized as an essential micronutrient for a variety of organisms (I), the physiological basis for this metal requirement remained obscure for many years. Thus, despite the demonstration that numerous enzymes which exhibit a requirement for activation by Me2+, e.g., kinases, synthetases, some dehydrogenases, can utilize Mn2+ at lower concentrations than Mg2, the relative concentrations of these two metal ions present in most tissues and species (2) indicate that Mg2+ is likely to serve as the activating metal ion under in vivo conditions. The recent discovery of bound manganese as a component of several proteins has provided a rationale for the unique biological role of this metal ion. Nuclear magnetic resonance (NMR) studies were responsible for providing the first indication of the existence of protein-bound manganese. In these studies pyruvate carboxylase from chicken liver was found to cause a marked increase in the longitudinal nuclear magnetic relaxation rate (1/T1) of water protons indicating the presence of a bound paramagnetic component in this enzyme.
Acquisition of the unpublished data to which reference is made in this article as well as the preparation of the article were aided by National Science Foundation Grant No. GB-30223 and by USPHS Grant No. RR0542. G.H.R. is a recipient of a Career Development Award (IK04-AM70134) from the National Institute of Arthritis, Metabolic and Digestive Diseases.
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Scrutton, M.C., Reed, G.H., Mildvan, A.S. (1973). Application of Physical Methods to the Study of Enzymes Containing Bound Manganese: Problems and Prospects. In: Dhar, S.K. (eds) Metal Ions in Biological Systems. Advances in Experimental Medicine and Biology, vol 40. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-3240-4_5
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