Abstract
A new variant of lipoxygenases, one containing manganese instead of iron, is characterized by electron paramagnetic resonance (EPR) at two frequencies. In the manganous state (Se = 5/2), maganese lipoxygenase (MnLO) yields very broad X-band (9.2 GHz) EPR signals, extending over about 800 mT. In contrast, at W-band (94 GHz), the signal is much simplified, consisting of nested transitions centered near the free electrong-value. Computer simulation has been employed to derive estimates of the zero-field splittings for MnLO, with data from these two EPR frequencies. The general features of both X- and W-band spectra are fit, first, by simulations with Se = 5/2, but no nuclear hyperfine splitting. The simulations are then refined by inclusion of the hyperfine splitting. On the basis of the simulations, the ranges of zero-field splitting parameters areD = +0.07 to +0.10 cm−1, andE/D = 0.13 to 0.23. Comparison of the value ofD for MnLO with that of other manga-nese-containing proteins suggests that MnLO has three N-ligands to the metal center and O-ligands in the remainder of 6 coordination positions. The coordination environment of MnLO is similar to that in iron lipoxygenases.
Similar content being viewed by others
References
Su C., Oliw E.H.: J. Biol. Chem.273, 13072–13079 (1998)
Rowley A.F., Kuhn H., Schewe T.: Eicosanoids and Related Compounds in Plants and Enzymes. London: Portland Press Ltd. 1998.
Gaffhey B.J.: Annu. Rev. Biophys. Biomol. Struct.25, 431–59 (1996)
Su C., Sahlin M., Oliw E.H.: J. Biol. Chem.275, 18830–18835 (2000)
Whittaker J.W., Whittaker M.M.: J. Am. Chem. Soc.113, 5528–5540 (1991)
Whiting A.K., Boldt Y.R., Hendrich M.P., Wackett L.P., Que L.: Biochemistry35, 160–170 (1996)
Meirovitch E., Luz Z., Kalb J.: J. Am. Chem. Soc.96, 7538–7542 (1991)
Smithers G.W., Poe M., Latwesen D.G., Reed G.H.: Biochemistry31, 4946–4950 (1992)
Bellew B.F., Halkides C.J., Gerfen G.J., Griffin R.G., Singel D.J.: Biochemistry35, 12186–12193 (1996)
Gaffhey B.J., Maguire B.C., Weber R.T., Maresch G.G.: Appl. Magn. Reson.16, 207–222 (1999)
Gaffney B.J., Silverstone H.J. in: Biological Magnetic Resonance (Berliner L.J., Reuben J., eds.), vol. 13, pp. 1–57. New York: Plenum 1993.
Gaffney B.J., Silverstone H.J.: J. Magn. Reson.134, 57–66 (1998)
Wang D., Hanson G.R.J.: J. Magn. Reson. A117, 1 (1995)
Weger M.: Bell Syst. Tech. J.39, 1013–1112 (1960)
Gaffhey B.J., Mavrophilipos D.V., Doctor K.S.: Biophys. J.64, 773–783 (1993)
Slykehouse T.O., Fee J.A.: J. Biol. Chem.251, 5472–5477 (1976)
Pavlovsky M.A., Zhang Y., Westre T.E., Gan Q.-F., Pavel E.G., Campochiaro C., Hedman B., Hodgson K.O., Solomon E.I.: J. Am. Chem. Soc.117, 4316–4327 (1995)
Author information
Authors and Affiliations
Additional information
An erratum to this article is available at http://dx.doi.org/10.1007/BF03166817.
Rights and permissions
About this article
Cite this article
Gaffney, B.J., Su, C. & Oliw, E.H. Assignment of EPR transitions in a manganese-containing lipoxygenase and prediction of local structure. Appl. Magn. Reson. 21, 411–422 (2001). https://doi.org/10.1007/BF03162417
Received:
Revised:
Issue Date:
DOI: https://doi.org/10.1007/BF03162417