Strong Closed-Shell Interactions in Inorganic Chemistry.

The coordination chemistry of pyrazole-derived ligands

Synthesis of propylene oxide from propylene and hydrogen peroxide catalyzed by titanium silicalite

Redox reactions play important roles in almost all biological processes, including photosynthesis and respiration, which are two essential energy processes that sustain all life on earth. It is thus not surprising that biology employs redox-active metal ions in these processes. It is largely the redox activity that makes metal ions uniquely qualified as biological cofactors and makes bioinorganic enzymology both fun to explore and challenging to study.

Even though most metal ions are redox active, biology employs a surprisingly limited number of them for electron transfer (ET) processes. Prominent members of redox centers involved in ET processes include cytochromes, iron–sulfur clusters, and cupredoxins. Together these centers cover the whole range of reduction potentials in biology (Figure ​(Figure1).1). Because of their importance, general reviews about redox centers1−77 and specific reviews about cytochromes,8,24,78−90 iron–sulfur proteins,91−93 and cupredoxins94−104 have appeared in the literature. In this review, we provide both classification and description of each member of the above redox centers, including both native and designed proteins, as well as those proteins that contain a combination of these redox centers. Through this review, we examine structural features responsible for their redox properties, including knowledge gained from recent progress in fine-tuning the redox centers. Computational studies such as DFT calculations become more and more important in understanding the structure–function relationship and facilitating the fine-tuning of the ET properties and reduction potentials of metallocofactors in proteins. Since this aspect has been reviewed extensively before,105−110 and by other reviews in this thematic issue,2000,2001,2002 it will not be covered here.






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Figure 1


Reduction potential range of redox centers in electron transfer processes.

Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers.

Publisher Summary This chapter discusses the reduction potentials involving inorganic free radicals in aqueous solution. Because free radicals are usually transients, knowing their thermodynamic properties is primarily useful in mechanistic studies. Thus, the useful redox couples associated with a given free radical correspond to plausible elementary steps in reaction mechanisms. All potentials are expressed against the normal hydrogen electrode (NHE). Apart from the NHE, the standard state for all solutes is the unit molar solution at 25 °C. This violates the usual convention for species, such as O 2 that occur as gases, but because the rates of bimolecular reactions in solution are significant, the unit molar standard state is most convenient. The emphasis is on electron transfer reactions in which no bonds are formed or broken, electron transfer reactions in which concerted electron transfer and bond cleavage could occur, and certain atom transfer reactions. The chapter also presents a tabulation of ∆ f G ° values for all the radicals. A common approach in estimating the thermochemistry of aqueous free radicals is to use gas-phase data with approximations of solvation energies.

Reduction potentials involving inorganic free radicals in aqueous solution

Metal ion catalysis of oxygen-transfer reactions. II. Vanadium and molybdenum chelates as catalysts in the epoxidation of cycloalkenes

The dinuclear Mn III , Mn IV model for the reactive center in photosystem II (PS II), [(bipy) 2 Mn III (O) 2 Mn IV (bipy) 2 ] 3+ undergoes rapid reductions by ascorbate, hydroquinone, and HSO 3 - to 2Mn 2+ (aq) in aqueous media buffered by bipy-bipy H + . Net changes of 3e - occur in each case

Electron transfer. 118. Proton-coupled reductions of a dinuclear dimanganese (III, IV) model for the reactive center in photosystem II

Redox chemistry of chromium (IV) complexes

Homogeneous vs. heterogeneous catalysis oxidation of liquid cyclohexene catalyzed by ions and oxides of transition metals

The chelated (carboxylato)chromium(V) anion bis(2-hydroxy-2-ethylbutyrato)oxochromate(V) (I), ((Lig)/sub 2/Cr(O))/sup -/, reacts with oxovanadium(IV) to form a strongly absorbing species (lambda/sub max/ = 515 nm; epsilon = 1.7 x 10/sup 3/ M/sup -1/) in the presence of 2-hydroxy-2-ethylbutyric acid buffers (pH 2-4). EPR data support 1:1 stoichiometry with VO/sup 2 +/ in deficiency, indicating the formation of a chromium(IV) species by reduction. With excess VO/sup 2 +/ a chromium(III) product was obtained. Spectral and ion-exchange properties of this product correspond to those observed for the titanium(III) and iron(II) reductions of chromium(V) and are consistent with the formulation of the product as a bis(hydroxycarboxylate) chelate of (H/sub 2/O)/sub 2/Cr/sup III/. With excess vanadium(IV), the reaction exhibits triphasic kinetics. The remaining step of the reaction is the reduction of the chromium(IV) intermediate with VO/sup 2 +/. Rates for all steps increase with decreasing (H/sup +/) and level off at low (H/sup +/). The limiting rate constants for the formation of the chromium(IV) intermediate by the (Lig)/sub 3/Cr(O)/sup 2 -/ and (Lig)/sub 2/Cr(O)/sup -/ pathways are 2.8 x 10/sup 3/ and 2.2 x 10/sup 2/ M/sup -1/s/sup -1/. The bimolecular limiting rate constant for the reduction of chromium(IV) is computed to be 7.7 x 10/supmore » 2/ M/sup -1/ s/sup -1/. 33 references, 7 tables.« less

Edwin S. Gould

Papers

Metal ion catalysis of oxygen-transfer reactions. II. Vanadium and molybdenum chelates as catalysts in the epoxidation of cycloalkenes

Electron transfer. 118. Proton-coupled reductions of a dinuclear dimanganese (III, IV) model for the reactive center in photosystem II

Redox chemistry of chromium (IV) complexes

Homogeneous vs. heterogeneous catalysis oxidation of liquid cyclohexene catalyzed by ions and oxides of transition metals

Electron transfer. 75. Reduction of carboxylato-bound chromium(V) with vanadium(IV). Intervention of chromium(IV)