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Reactive intermediates in oxygenation reactions with mononuclear nonheme iron catalysts.

ABSTRACT: An advanced intermediate: A nonheme iron(IV) oxo complex [Fe(IV)(O)(bqen)(L)](n+) (bqen = N,N'-dimethyl-N,N'-bis(8-quinolyl)ethane-1,2-diamine, L = CH(3)CN or CF(3)SO(3)(-)) activates the C-H bonds of alkanes and alcohols by a hydrogen-atom abstraction mechanism. The catalytic oxidation of these species is proposed to occur through a nonheme iron(V) oxo species, with a high reactivity in oxidation reactions (see picture).

SUBMITTER: Yoon J

PROVIDER: S-EPMC2863019 | biostudies-literature | 2009

REPOSITORIES: biostudies-literature

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Reactive intermediates in oxygenation reactions with mononuclear nonheme iron catalysts.

Yoon Jihae J Wilson Samuel A SA Jang Yu Kyeong YK Seo Mi Sook MS Nehru Kasi K Hedman Britt B Hodgson Keith O KO Bill Eckhard E Solomon Edward I EI Nam Wonwoo W

Angewandte Chemie (International ed. in English) 20090101 7

An advanced intermediate: A nonheme iron(IV) oxo complex [Fe(IV)(O)(bqen)(L)](n+) (bqen = N,N'-dimethyl-N,N'-bis(8-quinolyl)ethane-1,2-diamine, L = CH(3)CN or CF(3)SO(3)(-)) activates the C-H bonds of alkanes and alcohols by a hydrogen-atom abstraction mechanism. The catalytic oxidation of these species is proposed to occur through a nonheme iron(V) oxo species, with a high reactivity in oxidation reactions (see picture). ...[more]

PMID: 19137521

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Project description:ETHE1 is a member of a growing subclass of nonheme Fe enzymes that catalyzes transformations of sulfur-containing substrates without a cofactor. ETHE1 dioxygenates glutathione persulfide (GSSH) to glutathione (GSH) and sulfite in a reaction which is similar to that of cysteine dioxygenase (CDO), but with monodentate (vs bidentate) substrate coordination and a 2-His/1-Asp (vs 3-His) ligand set. In this study, we demonstrate that GSS- binds directly to the iron active site, causing coordination unsaturation to prime the site for O2 activation. Nitrosyl complexes without and with GSSH were generated and spectroscopically characterized as unreactive analogues for the invoked ferric superoxide intermediate. New spectral features from persulfide binding to the FeIII include the appearance of a low-energy FeIII ligand field transition, an energy shift of a NO- to FeIII CT transition, and two new GSS- to FeIII CT transitions. Time-dependent density functional theory calculations were used to simulate the experimental spectra to determine the persulfide orientation. Correlation of these spectral features with those of monodentate cysteine binding in isopenicillin N synthase (IPNS) shows that the persulfide is a poorer donor but still results in an equivalent frontier molecular orbital for reactivity. The ETHE1 persulfide dioxygenation reaction coordinate was calculated, and while the initial steps are similar to the reaction coordinate of CDO, an additional hydrolysis step is required in ETHE1 to break the S-S bond. Unlike ETHE1 and CDO, which both oxygenate sulfur, IPNS oxidizes sulfur through an initial H atom abstraction. Thus, factors that determine oxygenase vs oxidase reactivity were evaluated. In general, sulfur oxygenation is thermodynamically favored and has a lower barrier for reactivity. However, in IPNS, second-sphere residues in the active site pocket constrain the substrate, raising the barrier for sulfur oxygenation relative to oxidation via H atom abstraction.

Dataset Information

Reactive intermediates in oxygenation reactions with mononuclear nonheme iron catalysts.

Publications

Reactive intermediates in oxygenation reactions with mononuclear nonheme iron catalysts.

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