Methane monooxygenase spectroscopic characterization

Liu, K.E., Valentine, A.M., Wang, D., Huynh, B.H. Edmondson, D.E. Salifoglou, A. Lippard, SJ. (1995) Kinetic and spectroscopic characterization of intermediates and component interactions in reactions of methane monooxygenase from Methylococcus capsulatus (Bath), J. Am. Chem. Soc. 117, 10174-10185. 

The two-electron reduction of the diferric forms of hemerythrin (51), ribonucleotide reductase (27, 50), and methane monooxygenase (31) yields dioxygen-sensitive diferrous forms of the proteins. All three can be generated by dithionite treatment of the corresponding diferric forms, although the RRB2 reduction requires methyl viologen as mediator. The Fe(II) oxidation state is more difficult to probe spectroscopically, and only recently have methods been developed that allow this state to be characterized further. 

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