Twisted molecular wires polarize spin currents at room temperature.

A critical spintronics challenge is to develop molecular wires that render efficiently spin-polarized currents. Interplanar torsional twisting, driven by chiral binucleating ligands in highly conjugated molecular wires, gives rise to large near-infrared rotational strengths. The large scalar product of the electric and magnetic dipole transition moments ([Formula: see text]), which are evident in the low-energy absorptive manifolds of these wires, makes possible enhanced chirality-induced spin selectivity-derived spin polarization. Magnetic-conductive atomic force microscopy experiments and spin-Hall devices demonstrate that these designs point the way to achieve high spin selectivity and large-magnitude spin currents in chiral materials.

Electron transfer rate modulation with mid-IR in butadiyne-bridged donor-bridge-acceptor compounds.

Controlling electron transfer (ET) processes in donor-bridge-acceptor (DBA) compounds by mid-IR excitation can enhance our understanding of the ET dynamics and may find practical applications in molecular sensing and molecular-scale electronics. Alkyne moieties are attractive to serve as ET bridges, as they offer the possibility of fast ET and present convenient vibrational modes to perturb the ET dynamics. Yet, these bridges introduce complexity because of the strong torsion angle dependence of the ET rates and transition dipoles among electronic states and a shallow torsion barrier. In this study, we implemented ultrafast 3-pulse laser spectroscopy to investigate how the ET from the dimethyl aniline (D) electron donor to the N-isopropyl-1,8-napthalimide (NAP) electron acceptor can be altered by exciting the CC stretching mode (νCC) of the butadiyne bridge linking the donor and acceptor. The electron transfer was initiated by electronically exciting the acceptor moiety at 400 nm, followed by vibrational excitation of the alkyne, νCC, and detecting the changes in the absorption spectrum in the visible spectral region. The experiments were performed at different delay times t1 and t2, which are the delays between UV-mid-IR and mid-IR-Vis pulses, respectively. Two sets of torsion-angle conformers were identified, one featuring a very fast mean ET time of 0.63 ps (group A) and another featuring a slower mean ET time of 4.3 ps (group B), in the absence of the mid-IR excitation. TD-DFT calculations were performed to determine key torsion angle dependent molecular parameters, including the electronic and vibrational transition dipoles, transition frequencies, and electronic couplings. To describe the 3-pulse data, we developed a kinetic model that includes a locally excited, acceptor-based S2 state, a charge separated S1 state, and their vibrationally excited counterparts, with either excited νCC (denoted as S1Atr, S1Btr, S2Atr, and S2Btr, where tr stands for the excited triplet bond, νCC) or excited daughter modes of the νCC relaxation (S1Ah, S1Bh, S2Ah, and S2Bh, where h stands for vibrationally hot species). The kinetic model was solved analytically, and the species-associated spectra (SAS) were determined numerically using a matrix approach, treating first the experiments with longer t1 delays and then using the already determined SAS for modeling the experiments with shorter t1 delays. Strong vibronic coupling of νCC and of vibrationally hot states makes the analysis complicated. Nevertheless, the SAS were identified and the ET rates of the vibrationally excited species, S2Atr, S2Btr and S2Bh, were determined. The results show that the ET rate for the S2A species is ca. 1.2-fold slower when the νCC mode is excited. The ET rate for species S2B is slower by ca. 1.3-fold if the compound is vibrationally hot and is essentially unchanged when the νCC mode is excited. The SAS determined for the tr and h species resemble the SAS for their respective precursor species in the 2-pulse transient absorption experiments, which validates the procedure used and the results.

Using Adiabatic Energy Splitting To Compute Dexter Energy Transfer Couplings.

Dexter energy transfer and transport (DET) are of broad interest in energy science, and DET rates depend on electronic couplings between donor and acceptor species. DET couplings are challenging to compute since they originate from both one- and two-particle interactions, and the strength of this interaction drops approximately exponentially with donor-acceptor distances. Using adiabatic energy splitting to compute DET couplings has advantages because adiabatic states can be calculated directly using conventional quantum chemical methods. We describe a minimum energy splitting method to compute the DET coupling by altering molecular geometries to drive the systems into a T1/T2 energy quasi-degenerate-activated DA complex. We explore the accuracy of various quantum chemical approaches to calculate the Dexter couplings.

Correlated particle transport enables biological free energy transduction.

Studies of biological transport frequently neglect the explicit statistical correlations among particle site occupancies (i.e., they use a mean-field approximation). Neglecting correlations sometimes captures biological function, even for out-of-equilibrium and interacting systems. We show that neglecting correlations fails to describe free energy transduction, mistakenly predicting an abundance of slippage and energy dissipation, even for networks that are near reversible and lack interactions among particle sites. Interestingly, linear charge transport chains are well described without including correlations, even for networks that are driven and include site-site interactions typical of biological electron transfer chains. We examine three specific bioenergetic networks: a linear electron transfer chain (as found in bacterial nanowires), a near-reversible electron bifurcation network (as in complex III of respiration and other recently discovered structures), and a redox-coupled proton pump (as in complex IV of respiration).

Oxalate decarboxylase uses electron hole hopping for catalysis.

The hexameric low-pH stress response enzyme oxalate decarboxylase catalyzes the decarboxylation of the oxalate mono-anion in the soil bacterium Bacillus subtilis. A single protein subunit contains two Mn-binding cupin domains, and catalysis depends on Mn(III) at the N-terminal site. The present study suggests a mechanistic function for the C-terminal Mn as an electron hole donor for the N-terminal Mn. The resulting spatial separation of the radical intermediates directs the chemistry toward decarboxylation of the substrate. A π-stacked tryptophan pair (W96/W274) links two neighboring protein subunits together, thus reducing the Mn-to-Mn distance from 25.9 Å (intrasubunit) to 21.5 Å (intersubunit). Here, we used theoretical analysis of electron hole-hopping paths through redox-active sites in the enzyme combined with site-directed mutagenesis and X-ray crystallography to demonstrate that this tryptophan pair supports effective electron hole hopping between the C-terminal Mn of one subunit and the N-terminal Mn of the other subunit through two short hops of ∼8.5 Å. Replacement of W96, W274, or both with phenylalanine led to a large reduction in catalytic efficiency, whereas replacement with tyrosine led to recovery of most of this activity. W96F and W96Y mutants share the wildtype tertiary structure. Two additional hole-hopping networks were identified leading from the Mn ions to the protein surface, potentially protecting the enzyme from high Mn oxidation states during turnover. Our findings strongly suggest that multistep hole-hopping transport between the two Mn ions is required for enzymatic function, adding to the growing examples of proteins that employ aromatic residues as hopping stations.

Regulating Singlet-Triplet Energy Gaps through Substituent-Driven Modulation of the Exchange and Coulomb Interactions.

Control of the singlet-triplet energy gap (ΔEST) is central to realizing productive energy conversion reactions, photochemical reaction trajectories, and emergent applications that exploit molecular spin physics. Despite this, no systematic methods have been defined to tune ΔEST in simple molecular frameworks, let alone by an approach that also holds chromophore size and electronic structural parameters (such as the HOMO-LUMO gap) constant. Using a combination of molecular design, photophysical and potentiometric experiments, and quantum chemical analyses, we show that the degree of electron-electron repulsion in excited singlet and triplet states may be finely controlled through the substitution pattern of a simple porphyrin absorber, enabling regulation of relative electronically excited singlet and triplet state energies by the designed restriction of the electron-electron Coulomb (J) and exchange (K) interaction magnitudes. This approach modulates the ΔEST magnitude by controlling the densities of state in the occupied and virtual molecular orbital manifolds, natural transition orbital polarization, and the relative contributions of one electron transitions involving select natural transition orbital pairs. This road map, which regulates electron density overlaps in the occupied and virtual states that define the singlet and triplet wave functions of these chromophores, enables new approaches to preserve excitation energy despite intersystem crossing.

Discovery of the Xenon-Protein Interactome Using Large-Scale Measurements of Protein Folding and Stability.

The intermolecular interactions of noble gases in biological systems are associated with numerous biochemical responses, including apoptosis, inflammation, anesthesia, analgesia, and neuroprotection. The molecular modes of action underlying these responses are largely unknown. This is in large part due to the limited experimental techniques to study protein-gas interactions. The few techniques that are amenable to such studies are relatively low-throughput and require large amounts of purified proteins. Thus, they do not enable the large-scale analyses that are useful for protein target discovery. Here, we report the application of stability of proteins from rates of oxidation (SPROX) and limited proteolysis (LiP) methodologies to detect protein-xenon interactions on the proteomic scale using protein folding stability measurements. Over 5000 methionine-containing peptides and over 5000 semi-tryptic peptides, mapping to ∼1500 and ∼950 proteins, respectively, in the yeast proteome, were assayed for Xe-interacting activity using the SPROX and LiP techniques. The SPROX and LiP analyses identified 31 and 60 Xe-interacting proteins, respectively, none of which were previously known to bind Xe. A bioinformatics analysis of the proteomic results revealed that these Xe-interacting proteins were enriched in those involved in ATP-driven processes. A fraction of the protein targets that were identified are tied to previously established modes of action related to xenon's anesthetic and organoprotective properties. These results enrich our knowledge and understanding of biologically relevant xenon interactions. The sample preparation protocols and analytical methodologies developed here for xenon are also generally applicable to the discovery of a wide range of other protein-gas interactions in complex biological mixtures, such as cell lysates.

Synthetic Control of Exciton Dynamics in Bioinspired Cofacial Porphyrin Dimers.

Understanding how the complex interplay among excitonic interactions, vibronic couplings, and reorganization energy determines coherence-enabled transport mechanisms is a grand challenge with both foundational implications and potential payoffs for energy science. We use a combined experimental and theoretical approach to show how a modest change in structure may be used to modify the exciton delocalization, tune electronic and vibrational coherences, and alter the mechanism of exciton transfer in covalently linked cofacial Zn-porphyrin dimers (meso-beta linked ABm-ß and meso-meso linked AAm-m). While both ABm-ß and AAm-m feature zinc porphyrins linked by a 1,2-phenylene bridge, differences in the interporphyrin connectivity set the lateral shift between macrocycles, reducing electronic coupling in ABm-ß and resulting in a localized exciton. Pump-probe experiments show that the exciton dynamics is faster by almost an order of magnitude in the strongly coupled AAm-m dimer, and two-dimensional electronic spectroscopy (2DES) identifies a vibronic coherence that is absent in ABm-ß. Theoretical studies indicate how the interchromophore interactions in these structures, and their system-bath couplings, influence excitonic delocalization and vibronic coherence-enabled rapid exciton transport dynamics. Real-time path integral calculations reproduce the exciton transfer kinetics observed experimentally and find that the linking-modulated exciton delocalization strongly enhances the contribution of vibronic coherences to the exciton transfer mechanism, and that this coherence accelerates the exciton transfer dynamics. These benchmark molecular design, 2DES, and theoretical studies provide a foundation for directed explorations of nonclassical effects on exciton dynamics in multiporphyrin assemblies.

Voltage-induced long-range coherent electron transfer through organic molecules.

Biological structures rely on kinetically tuned charge transfer reactions for energy conversion, biocatalysis, and signaling as well as for oxidative damage repair. Unlike man-made electrical circuitry, which uses metals and semiconductors to direct current flow, charge transfer in living systems proceeds via biomolecules that are nominally insulating. Long-distance charge transport, which is observed routinely in nucleic acids, peptides, and proteins, is believed to arise from a sequence of thermally activated hopping steps. However, a growing number of experiments find limited temperature dependence for electron transfer over tens of nanometers. To account for these observations, we propose a temperature-independent mechanism based on the electric potential difference that builds up along the molecule as a precursor of electron transfer. Specifically, the voltage changes the nature of the electronic states away from being sharply localized so that efficient resonant tunneling across long distances becomes possible without thermal assistance. This mechanism is general and is expected to be operative in molecules where the electronic states densely fill a wide energy window (on the scale of electronvolts) above or below the gap between the highest-occupied molecular orbital (HOMO) and the lowest unoccupied molecular orbital (LUMO). We show that this effect can explain the temperature-independent charge transport through DNA and the strongly voltage-dependent currents that are measured through organic semiconductors and peptides.

Engineering opposite electronic polarization of singlet and triplet states increases the yield of high-energy photoproducts.

Efficient photosynthetic energy conversion requires quantitative, light-driven formation of high-energy, charge-separated states. However, energies of high-lying excited states are rarely extracted, in part because the congested density of states in the excited-state manifold leads to rapid deactivation. Conventional photosystem designs promote electron transfer (ET) by polarizing excited donor electron density toward the acceptor ("one-way" ET), a form of positive design. Curiously, negative design strategies that explicitly avoid unwanted side reactions have been underexplored. We report here that electronic polarization of a molecular chromophore can be used as both a positive and negative design element in a light-driven reaction. Intriguingly, prudent engineering of polarized excited states can steer a "U-turn" ET-where the excited electron density of the donor is initially pushed away from the acceptor-to outcompete a conventional one-way ET scheme. We directly compare one-way vs. U-turn ET strategies via a linked donor-acceptor (DA) assembly in which selective optical excitation produces donor excited states polarized either toward or away from the acceptor. Ultrafast spectroscopy of DA pinpoints the importance of realizing donor singlet and triplet excited states that have opposite electronic polarizations to shut down intersystem crossing. These results demonstrate that oppositely polarized electronically excited states can be employed to steer photoexcited states toward useful, high-energy products by routing these excited states away from states that are photosynthetic dead ends.

Mapping hole hopping escape routes in proteins.

A recently proposed oxidative damage protection mechanism in proteins relies on hole hopping escape routes formed by redox-active amino acids. We present a computational tool to identify the dominant charge hopping pathways through these residues based on the mean residence times of the transferring charge along these hopping pathways. The residence times are estimated by combining a kinetic model with well-known rate expressions for the charge-transfer steps in the pathways. We identify the most rapid hole hopping escape routes in cytochrome P450 monooxygenase, cytochrome c peroxidase, and benzylsuccinate synthase (BSS). This theoretical analysis supports the existence of hole hopping chains as a mechanism capable of providing hole escape from protein catalytic sites on biologically relevant timescales. Furthermore, we find that pathways involving the [4Fe4S] cluster as the terminal hole acceptor in BSS are accessible on the millisecond timescale, suggesting a potential protective role of redox-active cofactors for preventing protein oxidative damage.

Delocalization-Assisted Transport through Nucleic Acids in Molecular Junctions.

The flow of charge through molecules is central to the function of supramolecular machines, and charge transport in nucleic acids is implicated in molecular signaling and DNA repair. We examine the transport of electrons through nucleic acids to understand the interplay of resonant and nonresonant charge carrier transport mechanisms. This study reports STM break junction measurements of peptide nucleic acids (PNAs) with a G-block structure and contrasts the findings with previous results for DNA duplexes. The conductance of G-block PNA duplexes is much higher than that of the corresponding DNA duplexes of the same sequence; however, they do not display the strong even-odd dependence conductance oscillations found in G-block DNA. Theoretical analysis finds that the conductance oscillation magnitude in PNA is suppressed because of the increased level of electronic coupling interaction between G-blocks in PNA and the stronger PNA-electrode interaction compared to that in DNA duplexes. The strong interactions in the G-block PNA duplexes produce molecular conductances as high as 3% G0, where G0 is the quantum of conductance, for 5 nm duplexes.

Excited-State Dynamics and Nonlinear Optical Properties of Hyperpolarizable Chromophores Based on Conjugated Bis(terpyridyl)Ru(II) and Palladium and Platinum Porphyrinic Components: Impact of Heavy Metals upon Supermolecular Electro-Optic Properties.

A new series of strongly coupled oscillators based upon (porphinato)Pd, (porphinato)Pt, and bis(terpyridyl)ruthenium(II) building blocks is described. These RuPPd, RuPPt, RuPPdRu, and RuPPtRu chromophores feature bis(terpyridyl)Ru(II) moieties connected to the (porphinato)metal unit via an ethyne linker that bridges the 4'-terpyridyl and porphyrin macrocycle meso-carbon positions. Pump-probe transient optical data demonstrate sub-picosecond excited singlet-to-triplet-state relaxation. The relaxed lowest-energy triplet (T1) excited states of these chromophores feature absorption manifolds that span the 800-1200 nm spectral region, microsecond triplet-state lifetimes, and large absorptive extinction coefficients [ε(T1 → Tn) > 4 × 104 M-1 cm-1]. Dynamic hyperpolarizability (ßλ) values were determined from hyper-Rayleigh light scattering (HRS) measurements carried out at several incident irradiation wavelengths over the 800-1500 nm spectral region. Relative to benchmark RuPZn and RuPZnRu chromophores which showed large ßHRS values over the 1200-1600 nm range, RuPPd, RuPPt, RuPPdRu, and RuPPtRu displayed large ßHRS values over the 850-1200 nm region. Generalized Thomas-Kuhn sum (TKS) rules and experimental hyperpolarizability values were utilized to determine excited state-to-excited state transition dipole terms from experimental electronic absorption data and thus assessed frequency-dependent ßλ values, including two- and three-level contributions for both ßzzz and ßxzx tensor components to the RuPPd, RuPPt, RuPPdRu, and RuPPtRu hyperpolarizability spectra. These analyses qualitatively rationalize how the ßzzz and ßxzx tensor elements influence the observed irradiation wavelength-dependent hyperpolarizability magnitudes. The TKS analysis suggests that supermolecules related to RuPPd, RuPPt, RuPPdRu, and RuPPtRu will likely feature intricate dependences of experimentally determined ßHRS values as a function of irradiation wavelength that derive from substantial singlet-triplet mixing, and complex interactions among multiple different ß tensor components that modulate the long wavelength regime of the nonlinear optical response.

Charge Transfer and Spin Dynamics in a Zinc Porphyrin Donor Covalently Linked to One or Two Naphthalenediimide Acceptors.

Quantum coherence effects on charge transfer and spin dynamics in a system having two degenerate electron acceptors are studied using a zinc 5,10,15-tri(n-pentyl)-20-phenylporphyrin (ZnP) electron donor covalently linked to either one or two naphthalene-1,8:4,5-bis(dicarboximide) (NDI) electron acceptors using an anthracene (An) spacer, ZnP-An-NDI (1) and ZnP-An-NDI2 (2), respectively. Following photoexcitation of 1 and 2 in toluene at 295 K, femtosecond transient absorption spectroscopy shows that the electron transfer (ET) rate constant for 2 is about three times larger than that of 1, which can be accounted for by the statistical nature of incoherent ET as well as the electron couplings for the charge separation reactions. In contrast, the rate constant for charge recombination (CR) of 1 is about 25% faster than that of 2. Using femtosecond transient infrared spectroscopy and theoretical analysis, we find that the electron on NDI2•- in 2 localizes onto one of the two NDIs prior to CR, thus precluding electronically coherent CR from NDI2•-. Conversely, CR in both 1 and 2 is spin coherent as indicated by the observation of a resonance in the 3*ZnP yield following CR as a function of applied magnetic field, giving spin-spin exchange interaction energies of 2J = 210 and 236 mT, respectively, where the line width of the resonance for 2 is greater than 1. These data show that while CR is a spin-coherent process, incoherent hopping of the electron between the two NDIs in 2, consistent with the lack of delocalization noted above, results in greater spin decoherence in 2 relative to 1.

Electron ratcheting in self-assembled soft matter.

Ratcheted multi-step hopping electron transfer systems can plausibly produce directional charge transport over very large distances without requiring a source-drain voltage bias. We examine molecular strategies to realize ratcheted charge transport based on multi-step charge hopping, and we illustrate two ratcheting mechanisms with examples based on DNA structures. The charge transport times and currents that may be generated in these assemblies are also estimated using kinetic simulations. The first ratcheting mechanism described for nanoscale systems requires local electric fields on the 109 V/m scale to realize nearly 100% population transport. The second ratcheting mechanism for even larger systems, based on electrochemical gating, is estimated to generate currents as large as 0.1 pA for DNA structures that are a few µm in length with a gate voltage of about 5 V, a magnitude comparable to currents measured in DNA wires at the nanoscale when a source-drain voltage bias of similar magnitude is applied, suggesting an approach to considerably extend the distance range over which DNA charge transport devices may operate.

Why Are DNA and Protein Electron Transfer So Different?

The corpus of electron transfer (ET) theory provides considerable power to describe the kinetics and dynamics of electron flow at the nanoscale. How is it, then, that nucleic acid (NA) ET continues to surprise, while protein-mediated ET is relatively free of mechanistic bombshells? I suggest that this difference originates in the distinct electronic energy landscapes for the two classes of reactions. In proteins, the donor/acceptor-to-bridge energy gap is typically several-fold larger than in NAs. NA ET can access tunneling, hopping, and resonant transport among the bases, and fluctuations can enable switching among mechanisms; protein ET is restricted to tunneling among redox active cofactors and, under strongly oxidizing conditions, a few privileged amino acid side chains. This review aims to provide conceptual unity to DNA and protein ET reaction mechanisms. The establishment of a unified mechanistic framework enabled the successful design of NA experiments that switch electronic coherence effects on and off for ET processes on a length scale of multiple nanometers and promises to provide inroads to directing and detecting charge flow in soft-wet matter.

Symmetry controlled photo-selection and charge separation in butadiyne-bridged donor-bridge-acceptor compounds.

Electron transfer (ET) in donor-bridge-acceptor (DBA) compounds depends strongly on the structural and electronic properties of the bridge. Among the bridges that support donor-acceptor conjugation, alkyne bridges have attractive and unique properties: they are compact, possess linear structure permitting access to high symmetry DBA molecules, and allow torsional motion of D and A, especially for longer bridges. We report conformation dependent electron transfer dynamics in a set of novel DBA compounds featuring butadiyne (C4) bridge, N-isopropyl-1,8-napthalimide (NAP) acceptors, and donors that span a range of reduction potentials (trimethyl silane (Si-C4-NAP), phenyl (Ph-C4-NAP), and dimethyl aniline (D-C4-NAP)). Transient mid-IR absorption spectra of the C[triple bond, length as m-dash]C bridge stretching modes, transient spectra in the visible range, and TD-DFT calculations were used to decipher the ET mechanisms. We found that the electronic excited state energies and, especially, the transition dipoles (S0 → Sn) depend strongly on the dihedral angle (θ) between D and A and the frontier orbital symmetry, offering an opportunity to photo-select particular excited states with specific ranges of dihedral angles by exciting at chosen wavelengths. For example, excitation of D-C4-NAP at 400 nm predominantly prepares an S1 excited state in the planar conformations (θ ∼ 0) but selects an S2 state with θ ∼ 90°, indicating the dominant role of the molecular symmetry in the photophysics. Moreover, the symmetry of the frontier orbitals of such DBA compounds not only defines the photo-selection outcome, but also determines the rate of the S2 → S1 charge separation reaction. Unprecedented variation of the S2-S1 electronic coupling with θ by over four orders of magnitude results in slow ET at θ ca. 0° and 90° but extremely fast ET at θ of 20-60°. The unique features of high-symmetry alkyne bridged DBA structures enable frequency dependent ET rate selection and make this family of compounds promising targets for the vibrational excitation control of ET kinetics.

A Robust Bioderived Wavelength-Specific Photosensor Based on BLUF Proteins.

Photosensitive proteins are naturally evolved photosensors that often respond to light signals of specific wavelengths. However, their poor stability under ambient conditions hinders their applications in non-biological settings. In this proof-of-principle study, we grafted the blue light using flavin (BLUF) protein reconstructed with flavin adenine dinucleotide (FAD) or roseoflavin (RoF) onto pristine graphene, and achieved selective sensitivity at 450 nm or 500 nm, respectively. We improved the thermal and operational stability substantially via structure-guided cross-linking, achieving 6-month stability under ambient condition and normal operation at temperatures up to 200 °C. Furthermore, the device exhibited rare negative photoconductivity behavior. The origins of this negative photoconductivity behavior were elucidated via a combination of experimental and theoretical analysis. In the photoelectric conversion studies, holes from photoexcited flavin migrated to graphene and recombined with electrons. The device allows facile modulation and detection of charge transfer, and provides a versatile platform for future studies of photoinduced charge transfer in biosensors as well as the development of stable wavelength-selective biophotosensors.

Directing Charge Transfer in Quantum Dot Assemblies.

The optical and electronic properties of semiconductor quantum dots (QDs) make them attractive candidates for applications in photovoltaics, spintronics, photocatalysis, and optoelectronics. Understanding how to control the flow of charge in QD assemblies is essential for realizing novel applications. This Account explores some unique characteristics of charge transport in QD dyads, triads, and their assemblies. The emerging features of these assemblies that provide new opportunities to manipulate charge flow at the nanoscale are (1) cascading energy landscapes and band offsets to inhibit charge recombination, (2) electrostatic fields that direct charge flow through QD-QD and QD-conjugated polymer junctions, and (3) QD chirality and chiral imprinting that promotes vectorial electron and spin selective transport. Charge flow kinetics is determined by a combination of familiar electron transfer parameters (reaction free energy, reorganization energy, and electronic coupling), donor and acceptor electronic densities of states, and internal electric fields. Electron transfer and electronic structure theory, combined with kinetic modeling, place the measured kinetics of QD electron transfer donor-acceptor assemblies into a unified conceptual context. The experimental transfer rates measured in these systems depend upon structure and the internal electric fields that are present in the assemblies. A negatively charged donor and positively charged acceptor, for example, facilitates (inhibits) electron (hole) transfer, while an electric field of opposite orientation (reversal of charges) inhibits (promotes) electron (hole) transfer. These and other emerging rules that govern charge flow in NP assemblies provide a strategy to design the directionality and yield of interfacial charge transport. Chirality at the nanoscale can induce spin selective charge transport, providing new ways to direct charge (and spin) flow in QD assemblies. Magnetoresistance and magnetic conductive probe atomic force microscopy experiments show spin selective electron transport for chirally imprinted QD assemblies. Photoinduced electron transfer from achiral donor-QDs to chiral acceptor-QDs depends on the electron spin and chiroptical properties of the acceptor-QDs. These assemblies show transport characteristics that correlate with features of the QDs' circular dichroism spectra, presenting intriguing challenges to theory, and indicating that spectroscopic signatures may assist in the design and diagnosis of functional molecular assemblies. Theoretical and experimental studies of charge transport in well-defined QD assemblies are establishing design principles for vectorial charge transport and are also refining questions surrounding the mechanism and control of these processes. These intensified efforts are forging links between fundamental discoveries regarding mechanism and practical applications for these novel assembled nanostructures.

Energy Transduction in Nitrogenase.

Nitrogenase is a complicated two-component enzyme system that uses ATP binding and hydrolysis energy to achieve one of the most difficult chemical reactions in nature, the reduction of N2 to NH3. One component of the Mo-based nitrogenase system, Fe protein, delivers electrons one at a time to the second component, the catalytic MoFe protein. This process occurs through a series of synchronized events collectively called the "Fe protein cycle". Elucidating details of the events associated with this cycle has constituted an important challenge in understanding the nitrogenase mechanism. Electron delivery is a multistep process involving three metal clusters with intra- and interprotein events. It is proposed that the first electron transfer event is a gated intraprotein transfer of one electron from the MoFe protein P-cluster to the FeMo cofactor. Measurement of the effect of osmotic pressure on the rate of this electron transfer process revealed that it is gated by protein conformational changes. This first electron transfer is activated by binding of the Fe protein containing two bound ATP molecules. The mechanism of how this protein-protein association triggers electron transfer remains unknown. The second electron transfer event is proposed to be a rapid interprotein "backfill" with transfer of one electron from the reduced Fe protein 4Fe-4S cluster to the oxidized P-cluster. In this way, electron delivery can be viewed as a case of "deficit spending". Such a deficit-spending electron transfer process can be envisioned as a way to achieve one-direction electron flow, limiting the potential for back electron flow. Hydrolysis of two ATP molecules associated with the Fe protein occurs after the electron transfer and therefore is not used to directly drive the electron transfer. Rather, ATP hydrolysis is proposed to contribute to relaxation of the "activated" conformational state associated with the ATP form of the complex, with the free energy from ATP hydrolysis being used to pay back energy associated with component protein association and electron transfer. Release of inorganic phosphate (Pi) and protein-protein dissociation follow electron transfer and ATP hydrolysis. The rate-limiting step for the Fe protein cycle is not dissociation of the two proteins, as previously believed, but rather is release of Pi after ATP hydrolysis, which is then followed by rapid protein-protein complex dissociation. Nitrogenase is composed of two catalytic halves that do not function independently but rather exhibit anticooperative nuclear motion in which electron transfer in one-half of the complex partially inhibits electron transfer and ATP hydrolysis in the other half. Calculations indicated the existence of anticooperative interactions across the entire nitrogenase complex, suggesting a mechanism for the control of events on opposite ends of this large complex. The mechanistic necessity for this anticooperative process remains unknown. This Account presents a working model for how all of these processes work together in the nitrogenase "machine" to transduce the energy from ATP binding and hydrolysis to drive N2 reduction.