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Title: Photocurrent Generation by Photosynthetic Purple Bacterial Reaction Centers Interfaced with a Porous Antimony-Doped Tin Oxide (ATO) Electrode

Authors:
 [1];  [2];  [2];  [2];  [3];  [3];  [4];  [2];  [5];  [5]
  1. Biodesign Center for Innovation in Medicine at Biodesign Institute, Arizona State University, Tempe, Arizona 85287, United States
  2. School of Molecular Sciences, Arizona State University, Tempe, Arizona 85287-1604, United States
  3. Institute of Molecular Cell and Systems Biology, University of Glasgow, Glasgow, Scotland G12 8QQ, United Kingdom
  4. School of Molecular Sciences, Arizona State University, Tempe, Arizona 85287-1604, United States; Biodesign Center for Molecular Design and Biomimetics at Biodesign Institute, Arizona State University, Tempe, Arizona 85287, United States
  5. Biodesign Center for Innovation in Medicine at Biodesign Institute, Arizona State University, Tempe, Arizona 85287, United States; School of Molecular Sciences, Arizona State University, Tempe, Arizona 85287-1604, United States
Publication Date:
Research Org.:
Energy Frontier Research Centers (EFRC) (United States). Photosynthetic Antenna Research Center (PARC)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
OSTI Identifier:
1388792
DOE Contract Number:
SC0001035
Resource Type:
Journal Article
Resource Relation:
Journal Name: ACS Applied Materials and Interfaces; Journal Volume: 8; Journal Issue: 38; Related Information: PARC partners with Washington University in St. Louis (lead); University of California, Riverside; University of Glasgow, UK; Los Alamos National Laboratory; University of New Mexico; New Mexico Corsortium; North Carolina State University; Northwestern University; Oak Ridge National Laboratory; University of Pennsylvania; Sandia National Laboratories; University of Sheffield, UK
Country of Publication:
United States
Language:
English
Subject:
solar (fuels), photosynthesis (natural and artificial), biofuels (including algae and biomass), bio-inspired, charge transport, membrane, synthesis (novel materials), synthesis (self-assembly)

Citation Formats

Carey, Anne-Marie, Zhang, HaoJie, Mieritz, Daniel, Volosin, Alex, Gardiner, Alastair T., Cogdell, Richard J., Yan, Hao, Seo, Dong-Kyun, Lin, Su, and Woodbury, Neal W.. Photocurrent Generation by Photosynthetic Purple Bacterial Reaction Centers Interfaced with a Porous Antimony-Doped Tin Oxide (ATO) Electrode. United States: N. p., 2016. Web. doi:10.1021/acsami.6b07940.
Carey, Anne-Marie, Zhang, HaoJie, Mieritz, Daniel, Volosin, Alex, Gardiner, Alastair T., Cogdell, Richard J., Yan, Hao, Seo, Dong-Kyun, Lin, Su, & Woodbury, Neal W.. Photocurrent Generation by Photosynthetic Purple Bacterial Reaction Centers Interfaced with a Porous Antimony-Doped Tin Oxide (ATO) Electrode. United States. doi:10.1021/acsami.6b07940.
Carey, Anne-Marie, Zhang, HaoJie, Mieritz, Daniel, Volosin, Alex, Gardiner, Alastair T., Cogdell, Richard J., Yan, Hao, Seo, Dong-Kyun, Lin, Su, and Woodbury, Neal W.. 2016. "Photocurrent Generation by Photosynthetic Purple Bacterial Reaction Centers Interfaced with a Porous Antimony-Doped Tin Oxide (ATO) Electrode". United States. doi:10.1021/acsami.6b07940.
@article{osti_1388792,
title = {Photocurrent Generation by Photosynthetic Purple Bacterial Reaction Centers Interfaced with a Porous Antimony-Doped Tin Oxide (ATO) Electrode},
author = {Carey, Anne-Marie and Zhang, HaoJie and Mieritz, Daniel and Volosin, Alex and Gardiner, Alastair T. and Cogdell, Richard J. and Yan, Hao and Seo, Dong-Kyun and Lin, Su and Woodbury, Neal W.},
abstractNote = {},
doi = {10.1021/acsami.6b07940},
journal = {ACS Applied Materials and Interfaces},
number = 38,
volume = 8,
place = {United States},
year = 2016,
month = 9
}
  • The initial step of charge separation at 10 K has been monitored with 100-fs time resolution in reaction centers from Rhodopseudomonas viridis and Rhodobacter sphaeroides as well as in reaction centers from the latter species in which one of the two monomeric bacteriochlorophyll (B) molecules has been removed by treatment with borohydride. Upon excitation at 870 nm, the absorbance changes measured at several wavelengths in the near-infrared absorption bands of the pigments, and notably at the absorption maximum of the B molecule(s), give no indication of a detectable concentration of B{sup {minus}}. Instead, the appearance of the cation radical ofmore » the dimeric primary electron donor (P) and of the bacteriopheophytin anion develops in concert with the decay of P{sup *}. An initial bleaching of the 850-nm band in reaction centers from Rhodopseudomonas viridis is consistent with an assignment of at least a large fraction of this band to the high-energy exciton component of P. Upon excitation of the B molecule(s) around 600 nm in the three types of reaction centers investigated, ultrafast energy transfer leads to the formation of P{sup *} in less than 100 fs. Under these conditions, a fast transient bleaching decaying with a 400-fs time constant is observed within the absorption band of B. This transient is also present upon preferential excitation of the bacteriopheophytins in the reaction center of Rhodopseudomonas viridis.« less
  • Fast time-resolved EPR spectroscopy is used to study electron spin polarization (ESP) in perdeuterated native, Fe{sup 2+}-containing reaction centers (RCs) of photosynthetic purple bacteria. The spin-correlated radical pair-(SCRP) model previously used to simulate ESP observed in Fe-depleted RCs is extended to include the large anisotropy arising from the magnetic interactions between Fe{sup 2+} and the reduced primary electron-acceptor quinone (Q{sub A}{sup .-}), which results in different quantization axes from the P{sup .+} and the (Q{sub A}{sup .-}Fe{sup 2+}) spins. Using spectral simulations, it is shown that the ESP spectrum is solely due to the P{sup .+} part of the spin-correlatedmore » radical pair [P{sup .+}(Q{sub A}{sup .-}Fe{sup 2+})], whereas the rapid decay of the spin-polarized signal is due to spin-lattice relaxation of the (Q{sub A}{sup .-}Fe{sup 2+}) complex. The simulations are very sensitive to the relative orientation of the g matrices of P{sup .+} and (Q{sub A}{sup .-}Fe{sup 2+}). Using orientation II of the g matrix of the oxidized primary donor P{sup .+}, the orientation of the g matrix of (Q{sub A}{sup .-}Fe{sup 2+}) is assessed. Finally, it is shown that the ESP spectrum of perdeuterated native, Fe{sup 2+}-containing RCs of Rhodopseudomonas (Rps) viridis is virtually identical to the spectrum obtained for perdeuterated native Rhodobacter (Rb.) sphaeroides. 55 refs., 5 figs., 4 tabs.« less
  • The spin-polarized radical pairs P{sub 865}{sup {center_dot}+}Q{sub A}{sup {center_dot}-} in protonated and deuterated Zn-substituted reaction centers from two different mutants of the photosynthetic bacteria Rhodobacter sphaeroides and P{sub 700}{sup {center_dot}+}A{sub 1}{sup {center_dot}-} in plant photosystem I from Synechococcus elongatus are investigated by pulsed EPR spectroscopy. Spin-polarized radical pairs give rise to a characteristic out-of-phase electron spin echo. This echo shows a deep envelope modulation with a frequency governed by the spin-spin interaction. The known distance dependence of the magnetic dipolar interaction allows the determination of the distance between the cofactors carrying the unpaired electron spins. For the bacterial reaction centersmore » this distance is known for the electronic ground state from crystal structures and is compared here with the distance of the radical pair spins, i.e. the charge-separated state. In photosystem I the location of the acceptor A{sub 1} is not known yet. A distance of 25.4 {+-} 0.3 angstrom between P{sub 700}{sup {center_dot}+} and A{sub 1}{sup {center_dot}-} is obtained here and gives new structural information on photosystem I. 42 refs., 6 figs.« less
  • The three-dimensional structure of a photosynthetic reaction center has recently been obtained at atomic resolution using x-ray crystallography by Deisenhofer, Epp, Miki, Huber, and Michel (J. Mol. Biol. 1984, 180, 385-398; Nature 1985, 318, 618-624). This breakthrough provides the fundamental structural information needed to understand the mechanisms of the initial energy- and electron-transfer steps in photosynthesis. The structure reveals the distances among the reactive bacteriochlorophylls and quinones as well as the location of all nearby solvent molecules, the amino acids of the reaction center protein. Thus, the reaction center provides a complex but well-defined solid-state reactive system for the studymore » of fundamental physical and chemical processes with implications and applications well beyond this specific system. We review recent studies of the reaction intermediates and mechanism of electron transfer in which the energetics and reaction dynamics have been perturbed with external electric and magnetic fields. Electron-transfer mechanisms which have been proposed are reviewed critically in light of the available data, and electron transfer in the reaction center is compared with electron transfer in other biological and nonbiological systems.« less
  • Electron spin polarization develops on P{sup +} [Fe{sup 2+}]{sup -} n iron-containing photosynthetic bacterial reaction centers (RC) of Rhodobacter sphaeroides. The spin-polarized electron paramagnetic resonance (EPR) spectra of the oxidized primary donor (P{sup +}) depend on {tau}{sub H}, the lifetime of the radical pair P{sup +}H{sup -} formed prior to P{sup +}[Fe{sup 2+}]{sup -}. The polarized EPR signal can be described by the sequential electron transfer polarization (SETP) model in which the chemically induced dynamic electron polarization (CIDEP) developed in P{sup +}H{sup -} is projected onto the correlated radical pair polarization (CRPP) developed in P{sup +}[Fe{sup 2+}]{sup -}. Replacing themore » native ubiquinone-10 with various anthraquinones and naphthoquinones alters both the free energy and rate of electron transfer from H{sup -} to QFe{sup 2+}, which in turn modifies {tau}{sub H}{minus}. At long {tau}{sub H}{minus}, the polarized P{sup +} EPR signal is dominated by the CIDEP component of SETP. At short {tau}{sub H}{minus}, the signal is dominated by the CRPP component, while at intermediate {tau}{sub H}{minus}`s the signal can only be described using the full SETP model. The ranges of {tau}{sub H}, where polarization is dominated by interactions on the prior or observed radical pair are influenced by the EPR microwave frequency and RC isotopic composition. 71 refs., 8 figs., 2 tabs.« less