Jay R. Winkler

Earth-abundant hydrogen evolution electrocatalysts

Splitting water to hydrogen and oxygen is a promising approach for storing energy from intermittent renewables, such as solar power. Efficient, scalable solar-driven electrolysis devices require active electrocatalysts made from earth-abundant elements. In this mini-review, we discuss recent investigations of homogeneous and heterogeneous hydrogen evolution electrocatalysts, with emphasis on our own work on cobalt and iron complexes and nickel-molybdenum alloys.

Tryptophan-Accelerated Electron Flow Through Proteins

Energy flow in biological structures often requires submillisecond charge transport over long molecular distances. Kinetics modeling suggests that charge-transfer rates can be greatly enhanced by multistep electron tunneling in which redox-active amino acid side chains act as intermediate donors or acceptors. We report transient optical and infrared spectroscopic experiments that quantify the extent to which an intervening tryptophan residue can facilitate electron transfer between distant metal redox centers in a mutant Pseudomonas aeruginosa azurin. CuI oxidation by a photoexcited ReI-diimine at position 124 on a histidine(124)-glycine(123)-tryptophan(122)-methionine(121) β strand occurs in a few nanoseconds, fully two orders of magnitude faster than documented for single-step electron tunneling at a 19 angstrom donor-acceptor distance.

Protein Folding Triggered by Electron Transfer

Rapid photochemical electron injection into unfolded ferricytochrome c titrated with 2.3 to 4.6 M guanidine hydrochloride (GuHCl) at pH 7 and 40°C produced unfolded ferrocytochrome, which then converted to the folded protein. Two folding phases were observed: a fast process with a time constant of 40 microseconds (4.6 M GuHCl), and a slower phase with a rate constant of 90 ± 20 per second (2.3 M GuHCl). The activation free energy for the slow step varied linearly with GuHCl concentration; the rate constant, extrapolated to aqueous solution, was 7600 per second. Electron-transfer methods can bridge the nanosecond to millisecond measurement time gap for protein folding.

Mechanism of H2 Evolution from a Photogenerated Hydridocobaloxime

Proton transfer from the triplet excited state of brominated naphthol to a difluoroboryl bridged Co(I)-diglyoxime complex, forming Co(III)H, was monitored via transient absorption. The second-order rate constant for Co(III)H formation is in the range (3.5-4.7) × 10(9) M(-1) s(-1), with proton transfer coupled to excited-state deactivation of the photoacid. Co(III)H is subsequently reduced by excess Co(I)-diglyoxime in solution to produce Co(II)H (k(red) = 9.2 × 10(6) M(-1) s(-1)), which is then protonated to yield Co(II)-diglyoxime and H(2).

Proton-coupled electron flow in protein redox machines

Electron transfer (ET) reactions are fundamental steps in biological redox processes. Respiration is a case in point: at least 15 ET reactions are required to take reducing equivalents from NADH, deposit them in O_2, and generate the electrochemical proton gradient that drives ATP synthesis. Most of these reactions involve quantum tunneling between weakly coupled redox cofactors (ET distances > 10 A) embedded in the interiors of folded proteins. Here we review experimental findings that have shed light on the factors controlling these distant ET events. We also review work on a sensitizer-modified copper protein photosystem in which multistep electron tunneling (hopping) through an intervening tryptophan is orders of magnitude faster than the corresponding single-step ET reaction.If proton transfers are coupled to ET events, we refer to the processes as proton coupled ET, or PCET, a term introduced by Huynh and Meyer in 1981. Here we focus on two protein redox machines, photosystem II and ribonucleotide reductase, where PCET processes involving tyrosines are believed to be critical for function. Relevant tyrosine model systems also will be discussed.

Molecular mechanisms of cobalt-catalyzed hydrogen evolution

Several cobalt complexes catalyze the evolution of hydrogen from acidic solutions, both homogeneously and at electrodes. The detailed molecular mechanisms of these transformations remain unresolved, largely owing to the fact that key reactive intermediates have eluded detection. One method of stabilizing reactive intermediates involves minimizing the overall reaction free-energy change. Here, we report a new cobalt(I) complex that reacts with tosylic acid to evolve hydrogen with a driving force of just 30 meV/Co. Protonation of CoI produces a transient CoIII-H complex that was characterized by nuclear magnetic resonance spectroscopy. The CoIII-H intermediate decays by second-order kinetics with an inverse dependence on acid concentration. Analysis of the kinetics suggests that CoIII-H produces hydrogen by two competing pathways: a slower homolytic route involving two CoIII-H species and a dominant heterolytic channel in which a highly reactive CoII-H transient is generated by CoI reduction of CoIII-H.

Electron flow through metalloproteins

Electron transfers in photosynthesis and respiration commonly occur between metal-containing cofactors that are separated by large molecular distances. Understanding the underlying physics and chemistry of these biological electron transfer processes is the goal of much of the work in our laboratories. Employing laser flash-quench triggering methods, we have shown that 20A, coupling-limited Fe(II) to Ru(III) and Cu(I) to Ru(III) electron tunneling in Ru-modified cytochromes and blue copper proteins can occur on the microsecond timescale both in solutions and crystals; and, further, that analysis of these rates suggests that distant donor-acceptor electronic couplings are mediated by a combination of sigma and hydrogen bonds in folded polypeptide structures. Redox equivalents can be transferred even longer distances by multistep tunneling, often called hopping, through intervening amino acid side chains. In recent work, we have found that 20A hole hopping through an intervening tryptophan is several hundred-fold faster than single-step electron tunneling in a Re-modified blue copper protein.

Electron-tunneling pathways in cytochrome C.

Distant Fe2+-Ru3+ electronic couplings have been extracted from intramolecular electrontransfer rates in Ru(histidinex) (where X = 33, 39, 62, and 72) derivatives of cytochrome c. The couplings increase according to 62 (0.0060) < 72 (0.057) < 33 (0.097) < 39 (0.11 per wave numbers); however, this order is out of line with the histidine to heme edge-edge distances [62 (14.8) > 39 (12.3) > 33 (11.1) > 72 (8.4 angstroms)]. The rates (and the couplings) correlate with the lengths of σ-tunneling pathways comprised of covalent bonds, hydrogen bonds, and through-space jumps from the histidines to the heme group. Space jumps greatly decrease couplings: One from Pro71 to Met80 extends the σ-tunneling length of the His72 pathway by roughly 10 covalent-bond units.

Highly active mixed-metal nanosheet water oxidation catalysts made by pulsed-laser ablation in liquids.

Surfactant-free mixed-metal hydroxide water oxidation nanocatalysts were synthesized by pulsed-laser ablation in liquids. In a series of [Ni-Fe]-layered double hydroxides with intercalated nitrate and water, [Ni1-xFex(OH)2](NO3)y(OH)x-y·nH2O, higher activity was observed as the amount of Fe decreased to 22%. Addition of Ti(4+) and La(3+) ions further enhanced electrocatalysis, with a lowest overpotential of 260 mV at 10 mA cm(-2). Electrocatalytic water oxidation activity increased with the relative proportion of a 405.1 eV N 1s (XPS binding energy) species in the nanosheets.

Kinetics of electron transfer reactions of H2-evolving cobalt diglyoxime catalysts.

Co-diglyoxime complexes catalyze H(2) evolution from protic solutions at modest overpotentials. Upon reduction to Co(I), a Co(III)-hydride is formed by reaction with a proton donor. Two pathways for H(2) production are analyzed: one is a heterolytic route involving protonation of the hydride to release H(2) and generate Co(III); the other is a homoytic pathway requiring association of two Co(III)-hydrides. Rate constants and reorganization parameters were estimated from analyses of laser flash-quench kinetics experiments (Co(III)-Co(II) self-exchange k = 9.5 x 10(-8) - 2.6 x 10(-5) M(-1) s(-1); lambda = 3.9 (+/-0.3) eV: Co(II)-Co(I) self-exchange k = 1.2 (+/-0.5) x 10(5) M(-1) s(-1); lambda = 1.4 (+/-0.05) eV). Examination of both the barriers and driving forces associated with the two pathways indicates that the homolytic reaction (Co(III)H + Co(III)H --> 2 Co(II) + H(2)) is favored over the route that goes through a Co(III) intermediate (Co(III)H + H(+) --> Co(III) + H(2)).