Biomaterial Database

Oxidative N-dealkylation reactions by oxoiron(IV) complexes of nonheme and heme ligands. 2007

Kasi Nehru, and Mi Sook Seo, and Jinheung Kim, and Wonwoo Nam

Department of Chemistry, Division of Nano Sciences, and Center for Biomimetic Systems, Ewha Womans University, Seoul 120-750, Korea.

Nonheme and heme iron monooxygenases participate in oxidative N-dealkylation reactions in nature, and high-valent oxoiron(IV) species have been invoked as active oxidants that effect the oxygenation of organic substrates. The present study describes the first example of the oxidative N-dealkylation of N,N-dialkylamines by synthetic nonheme oxoiron(IV) complexes and the reactivity comparisons of nonheme and heme oxoiron(IV) complexes. Detailed mechanistic studies were performed with various N,N-dialkylaniline substrates such as para-substituted N,N-dimethylanilines, para-chloro-N-ethyl-N-methylaniline, para-chloro-N-cyclopropyl-N-isopropylaniline, and deuteriated N,N-dimethylanilines. The results of a linear free-energy correlation, inter- and intramolecular kinetic isotope effects, and product analysis studied with the mechanistic probes demonstrate that the oxidative N-dealkylation reactions by nonheme and heme oxoiron(IV) complexes occur via an electron transfer-proton transfer (ET-PT) mechanism.

UI	MeSH Term	Description	Entries
D007501	Iron	A metallic element with atomic symbol Fe, atomic number 26, and atomic weight 55.85. It is an essential constituent of HEMOGLOBINS; CYTOCHROMES; and IRON-BINDING PROTEINS. It plays a role in cellular redox reactions and in the transport of OXYGEN.	Iron-56,Iron 56
D008024	Ligands	A molecule that binds to another molecule, used especially to refer to a small molecule that binds specifically to a larger molecule, e.g., an antigen binding to an antibody, a hormone or neurotransmitter binding to a receptor, or a substrate or allosteric effector binding to an enzyme. Ligands are also molecules that donate or accept a pair of electrons to form a coordinate covalent bond with the central metal atom of a coordination complex. (From Dorland, 27th ed)	Ligand
D010084	Oxidation-Reduction	A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).	Redox,Oxidation Reduction
D010100	Oxygen	An element with atomic symbol O, atomic number 8, and atomic weight [15.99903; 15.99977]. It is the most abundant element on earth and essential for respiration.	Dioxygen,Oxygen-16,Oxygen 16
D006418	Heme	The color-furnishing portion of hemoglobin. It is found free in tissues and as the prosthetic group in many hemeproteins.	Ferroprotoporphyrin,Protoheme,Haem,Heme b,Protoheme IX
D015394	Molecular Structure	The location of the atoms, groups or ions relative to one another in a molecule, as well as the number, type and location of covalent bonds.	Structure, Molecular,Molecular Structures,Structures, Molecular
D046911	Macromolecular Substances	Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.	Macromolecular Complexes,Macromolecular Compounds,Macromolecular Compounds and Complexes,Complexes, Macromolecular,Compounds, Macromolecular,Substances, Macromolecular
D019159	Nonheme Iron Proteins	Proteins, usually acting in oxidation-reduction reactions, containing iron but no porphyrin groups. (Lehninger, Principles of Biochemistry, 1993, pG-10)	Iron Proteins, Non-Heme,Non-Heme Iron Proteins,Iron Proteins, Non Heme,Iron Proteins, Nonheme,Non Heme Iron Proteins,Proteins, Non-Heme Iron,Proteins, Nonheme Iron