Catalytic oxidation of hydrocarbons by dinuclear iron complexes

Technical Report · Wed Jan 01 00:00:00 EST 1992

DOI:https://doi.org/10.2172/6728523· OSTI ID:6728523

Caradonna, J P

Our efforts during the past eight months were directed towards characterizing synthetic complexes that model the electronic and reactivity properties of the active site of methane monooxygenase (MMO), a metalloenzyme found in methanotrophic bacteria responsible for the biological oxidation of methane to methanol. We have investigated the structural/electronic and reactivity properties of a series of dinuclear model complexes that can function as oxygen atom transfer catalysts. In particular, our studies focused on [Fe[sup 2+][sub 2](H[sub 2]Hbab)[sub 2](N-MeIm)[sub 2]], its DMF solvated form, [Fe[sup 2+][sub 2](H[sub 2]Hbab)[sub 2](DMF)[sub 2](MeIm)], and the mixed valent species [Fe[sup 2+]Fe[sup 3+](H[sub 2]Hbab)[sub 2](DMF)[sub 4]][sup +], (H[sub 4]Hbab = 1,2-bis(2-hydroxybenzamido) benzene). We have also examined [Fe[sup 3+][sub 2](H[sub 2]Hbab)[sub 2](DMF)[sub 4]][sup 2+], [Fe[sup 3+][sub 2](H[sub 2]Hbab)[sub 2](OMe)[sub 2]], and [mu]-oxo-[Fe[sup 3+][sub 2](H[sub 2]Hbab)[sub 2](DMF)[sub 2]], which are unable to act as oxygen atom transfer catalysts.

• Research Organization: Yale Univ., New Haven, CT (United States)
• Sponsoring Organization: USDOE; USDOE, Washington, DC (United States)
• DOE Contract Number: FG02-92ER14279
• OSTI ID: 6728523
• Report Number(s): DOE/ER/14279-1; ON: DE93010071
• Country of Publication: United States
• Language: English

Related Subjects

09 BIOMASS FUELS
59 BASIC BIOLOGICAL SCIENCES
IRON COMPLEXES
CATALYTIC EFFECTS
METHANE
BIODEGRADATION
OXYGENASES
PROTEIN ENGINEERING
BIOCHEMICAL REACTION KINETICS
BIOMIMETIC PROCESSES
BIOTECHNOLOGY
PROGRESS REPORT
ALKANES
CHEMICAL REACTIONS
COMPLEXES
DECOMPOSITION
DOCUMENT TYPES
ENZYMES
HYDROCARBONS
KINETICS
ORGANIC COMPOUNDS
OXIDOREDUCTASES
PROTEINS
REACTION KINETICS
TRANSITION ELEMENT COMPLEXES
090900* - Biomass Fuels- Processing- (1990-)
550200 - Biochemistry