alexa Magnetic circular dichroism study of a dicobalt(II) methionine aminopeptidase fumagillin complex and dicobalt II-II and II-III model complexes.
Genetics & Molecular Biology

Genetics & Molecular Biology

Journal of Genetic Syndromes & Gene Therapy

Author(s): Larrabee JA, Chyun SA, Volwiler AS

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Abstract The dicobalt form of the metallohydrolase methionine aminopeptidase from Escherichia coli (CoCo EcMetAP) has an active site with one 5-coordinate Co (II) and a more weakly bound 6-coordinate Co (II). These metal ions are bridged by two carboxylate amino acid side chains and water or hydroxide, potentially enabling magnetic exchange coupling between the metals. We used variable-temperature, variable-field magnetic circular dichroism to determine whether such coupling occurs. CoCo EcMetAP's MCD spectrum shows distinct d-d transitions at 495 and 567 nm caused by 6- and 5-coordinate Co (II), respectively. The magnetization curves for 5- and 6-coordinate Co (II) are very different, indicating that their electronic ground states vary considerably, ruling out any coupling. When the fungal metabolite fumagillin binds to the CoCoEcMetAP, the qualitative MCD spectrum is unchanged; however, VTVH MCD data show that 5- and 6-coordinate Co (II) ions have similarly shaped magnetization curves, indicating that the Co (II) ions now share the same electronic ground state. Fitting the VTVH MCD data to a model in which dimer wave functions are calculated using a spin Hamiltonian with zero-field splitting showed the Co (II) ions to be weakly ferromagnetically coupled, with J = 2.9 cm (-1). Ferromagnetic coupling is unusual for dinuclear Co (II); therefore, to support the CoCoEcMetAP/fumagillin complex results, we also analyzed VTVH MCD data from a matched pair of dinuclear cobalt complexes, 1 and 2. Complex 1 shares the carboxylate and hydroxide-bridged dicobalt(II) structural motif with the active site of CoCo EcMetAP. Complex 2 contains a nearly isostructural Co (II) ion, but the Co (III) is diamagnetic, so any magnetic coupling is switched off, while the spectral features of the Co (II) ion remain. Magnetization data for 1, fitted to the dimer model, showed that the Co (II) ions were weakly ferromagnetically coupled, with J = 1.7 cm (-1). Magnetization data for Co (II) ions in 2, however, reflect loss of magnetic exchange coupling. This article was published in Inorg Chem and referenced in Journal of Genetic Syndromes & Gene Therapy

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