Hydrogen atom transfer reactions (HAT) are a class of proton-coupled electron transfer (PCET) reactions used in biology to promote substrate oxidation. The driving force for such reactions depend on both the oxidation potential of the catalyst and the pKa of the proton acceptor site. Both high-valent transition-metal oxo M(IV)=O (M= Fe, Mn) and lower-valent transition-metal hydroxo compounds M(III)–OH (M= Fe, Mn) have been shown to promote these reactions. Herein we describe the synthesis, structure and reactivity properties of a series of Mn(III)-OR compounds (R= pNO2Ph(5), Ph(6), Me(7), H(8)), some of which abstract H-atoms. The Mn(III)-OH complex 8 is water-soluble and represents a rare example of a stable mononuclear Mn(III)-OH. In water, the redox potential of 8 was found to be pH-dependent and the Pourbaix (Ep,c vs pH) diagram has a slope (52 mV/pH) that is indicative of the transfer a single proton with each electron (ie, PCET). The two compounds with the lowest oxidation potential, hydroxide and methoxide-bound 7 and 8 are found to oxidize TEMPOH, whereas the compounds with the highest oxidation potential, phenol-ligated 5 and 6, are shown to be unreactive. Hydroxide-bound 8 reacts with TEMPOH an order of magnitude faster than methoxide-bound 7. Kinetic data (kH/kD= 3.1 (8), kH/kD= 2.1 (7)) are consistent with concerted H-atom abstraction. The reactive species 8 can be aerobically regenerated in H2O, and at least 10 turnovers can be achieved without significant degradation of the “catalyst”. The linear correlation between redox potential and pH, obtained from the Pourbaix diagram, was used to calculate the BDFE= 74.0±0.5 kcal/mol for Mn(II)-OH2 in water, and in MeCN its BDFE was estimated to be (70.1 kcal/mol). The reduced protonated derivative of 8, [MnII(SMe2N4(tren))(H2O)]+ (9), was estimated to have a pKa of 21.2 in MeCN. The ability (7) and inability (5 and 6) of the other members of the series to abstract a H-atom from TEMPOH was used to estimate either an upper or lower limit to the Mn(II)-O(H)R pKa based on their experimentally determined redox potentials. The trend in pKa (21.2(R=H) > 16.2(R=Me) > 13.5(R=Ph) > 12.2(R=pNO2Ph)) is shown to oppose that of oxidation potential Ep,c (−220(R= pNO2Ph) > −300(R= Ph) > −410(R= Me) > −600(R= H) mV vs Fc+/0) for this particular series.

Toxic superoxide radicals, generated via adventitious reduction of dioxygen, have been implicated in a number of disease states. The cysteinate-ligated non-heme iron enzyme superoxide reductase (SOR) degrades superoxide via reduction. Biomimetic analogues which provide insight into why nature utilizes a trans-thiolate to promote SOR function are described. Spectroscopic and/or structural characterization of the first examples of thiolate-ligated Fe (III)-peroxo complexes provides important benchmark parameters for the identification of biological intermediates. Oxidative addition of superoxide is favored by low redox potentials. The trans influence of the thiolate appears to significantly weaken the Fe-O peroxo bond, favoring proton-induced release of H 2O 2 from a high-spin Fe(III)-OOH complex.

A series of five-coordinate thiolate-ligated complexes [M II (tren)N 4 S Me2 ] + (M = Mn, Fe, Co, Ni, Cu, Zn; tren = tris(2-aminoethyl)amine) are reported, and their structural, electronic, and magnetic properties are compared. Isolation of dimeric [Ni II (SN 4 (tren)-RS dang )] 2 ("dang"= dangling, uncoordinated thiolate supported by H-bonds) using the less bulky [(tren)N 4 S] 1− ligand, pointed to the need for gem-dimethyls adjacent to the sulfur in order to sterically prevent dimerization. All of the gem-dimethyl derivatized complexes are monomeric, and with the exception of [Ni II (S Me2 N 4 (tren)] + , are isostructural and adopt a tetragonally distorted trigonal bipyramidal geometry favored by ligand constraints. The nickel complex uniquely adopts an approximately ideal square pyramidal geometry, and resembles the active site of Ni-superoxide dismutase (Ni-SOD). Even in coordinating solvents such as MeCN, only five-coordinate structures are observed. The M II -S thiolate bonds systematically decrease in length across the series (Mn-S > Fe-S > Co-S > Ni-S ~ Cu-S < Zn-S) with exceptions occurring upon the occupation of σ* orbitals. The copper complex, [Cu II (S Me2 N 4 (tren)] + , represents a rare example of a stable Cu II -thiolate, and models the perturbed "green" copper site of nitrite reductase. In contrast to the intensely colored, low-spin Fe (III)-thiolates, the M(II)-thiolates described herein are colorless to moderately colored, and highspin (in cases where more than one spin-state is possible), reflecting the poorer energy match between the metal d-and sulfur-orbitals upon reduction of the metal ion. As the d-orbitals drop in energy proceeding across the across the series M 2+ (M= Mn, Fe, Co, Ni, Cu), the sulfur-to-metal charge transfer transition moves into the visible region, and the redox potentials cathodically shift. The reduced M +1 oxidation state is only accessible with copper, and the more oxidized M +4 oxidation state is only accessible for manganese.

The cover picture shows the role played by synthetic metalloenzyme analogues in uncovering the relationship between metalloenzyme active site structure, properties, and function at the molecular level. Details are presented in the Microreview by L. M. Brines and J. A. Kovacs on p. 29 ff.

Understanding the metal ion properties that favor O−H bond formation versus cleavage should facilitate the development of catalysts tailored to promote a specific reaction, e.g., C−H activation or H2O oxidation. The first step in H2O oxidation involves the endothermic cleavage of a strong O−H bond (BDFE = 122.7 kcal/mol), promoted by binding the H2O to a metal ion, and by coupling electron transfer to proton transfer (PCET). This study focuses on details regarding how a metal ion’s electronic structure and ligand environment can tune the energetics of M(HO−H) bond cleavage. The synthesis and characterization of an Fe(II)−H2O complex, 1, that undergoes PCET in H2O to afford a rare example of a monomeric Fe(III)−OH, 7, is described. High-spin 7 is also reproducibly generated via the addition of H2O to {[FeIII(OMe2N4(tren))]2-(µ-O)}2+ (8). The O−H bond BDFE of Fe(II)−H2O (1) (68.6 kcal/mol) is calculated using linear fits to its Pourbaix diagram and shown to be 54.1 kcal/mol less than that of H2O and 10.9 kcal/mol less than that of [Fe(II)(H2O)6]2+. The O−H bond of 1 is noticeably weaker than the majority of reported Mn+(HxO−H) (M = Mn, Fe; n+ = 2+, 3+; x = 0, 1) complexes. Consistent with their relative BDFEs, Fe(II)−H2O (1) is found to donate a H atom to TEMPO•, whereas the majority of previously reported Mn+−O(H) complexes, including [MnIII(SMe2N4(tren))(OH)]+ (2), have been shown to abstract H atoms from TEMPOH. Factors responsible for the weaker O−H bond of 1, such as differences in the electron-donating properties of the ligand, metal ion Lewis acidity, and electronic structure, are discussed.