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Diamond core structure, methane monooxygenase

Shu LJ, Nesheim JC, Kauffmann K, Miinck E, Lipscomb JD, Que L. An Fe2IV02 diamond core structure for the key intermediate Q of methane monooxygenase. Science. 1997 275 515-8. [Pg.376]

If these calculations prove correct, the high reactivity of the "activated" O2 (i.e. H-abstraction from unactivated C-H bonds) may be associated with Mdging rather than terminal oxo-ligands. We note that the most recent proposal for the reactive interm ate of methane monooxygenase features a "Fe2(li-0)2 diamond core structure" much like the one shown in Figure 2. [19]... [Pg.1086]

Hsu, H., Dong, Y., Shu, L.,Young, J., V. G., and Que, J., L., 1999, Crystal structure of a synthetic high-valent complex with an Fc2(p-0)2 diamond core. Implications for the core structures of methane monooxygenase intermediate Q and ribonucleotide reductase intermediate X, J. Am. Chem. Soc. 121 5230n5237. [Pg.273]

Dioxygen diiron complexes have been synthesized by mimicking the probable intermediate structures in methane monooxygenase oxygenations. Examples are summarized in the recent review. One is the Fc2(i7-0)2 diamond core type and the other is the Fe2(tJ-02) peroxo type. Recently, an unusual Fe"-X-Fe (tl -02) species has been suggested in the reaction of O2 with carboxylate-bridged diiron(II,II) paddlewheel complexes, but its role in the oxygenation has not been clarified. ... [Pg.187]


See other pages where Diamond core structure, methane monooxygenase is mentioned: [Pg.42]    [Pg.66]    [Pg.276]    [Pg.409]    [Pg.178]    [Pg.362]   
See also in sourсe #XX -- [ Pg.258 , Pg.259 ]




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