A functional nitric oxide reductase model
by: James P. Collman, Ying Yang, Abhishek Dey, Richard A. Decréau, Somdatta Ghosh, Takehiro Ohta, Edward I. Solomon
Proceedings of the National Academy of Sciences, Vol. 105, No. 41. (14 October 2008), pp. 15660-15665, doi:10.1073/pnas.0808606105 Key: citeulike:12127891
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Abstract
A functional heme/nonheme nitric oxide reductase (NOR) model is presented. The fully reduced diiron compound reacts with two equivalents of NO leading to the formation of one equivalent of N2O and the bis-ferric product. NO binds to both heme Fe and nonheme Fe complexes forming individual ferrous nitrosyl species. The mixed-valence species with an oxidized heme and a reduced nonheme FeB does not show NO reduction activity. These results are consistent with a so-called “trans” mechanism for the reduction of NO by bacterial NOR.
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