Search NASA⌕ Search

Engineering topics

Vinyard, David J.

Publications and source records attributed to Vinyard, David J..

8 records
All sourcesNASA NTRSDOE OSTI
DOE OSTI2024

Cryo-EM structure of a photosystem I variant containing an unusual plastoquinone derivative in its electron transfer chain

Photosystem I (PS I) is a light-driven oxidoreductase responsible for converting photons into chemical bond energy. Its application for renewable energy was revolutionized by the creation of the MenB deletion (ΔmenB) variant in the cyanobacterium Synechocystis sp. PCC 6803, in which phylloquinone is replaced by plastoquinone-9 with a low binding affinity. This permits its exchange with exogenous quinones covalently coupled to dihydrogen catalysts that bind with high affinity, thereby converting PS I into a stable solar fuel catalyst. Here, we reveal the 2.03-Å-resolution cryo-EM structure of a recent MenB variant of PS I. The quinones and their binding environment are analyzed in the context of previous biophysical data, thereby enabling a protocol to solve future PS I hybrids and constructs from this genetically tractable cyanobacterium.

37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CH↗
DOE OSTI2024

Bicarbonate is a key regulator but not a substrate for O2 evolution in Photosystem II

Abstract Photosystem II (PSII) uses light energy to oxidize water and to reduce plastoquinone in the photosynthetic electron transport chain. O 2 is produced as a byproduct. While most members of the PSII research community agree that O 2 originates from water molecules, alternative hypotheses involving bicarbonate persist in the literature. In this perspective, we provide an overview of the important roles of bicarbonate in regulating PSII activity and assembly. Further, we emphasize that biochemistry, spectroscopy, and structural biology experiments have all failed to detect bicarbonate near the active site of O 2 evolution. While thermodynamic arguments for oxygen-centered bicarbonate oxidation are valid, the claim that bicarbonate is a substrate for photosynthetic O 2 evolution is challenged.

Vinyard, David J.↗
DOE OSTI2024

Assembly and Repair of Photosystem II in Chlamydomonas reinhardtii

Oxygenic photosynthetic organisms use Photosystem II (PSII) to oxidize water and reduce plastoquinone. Here, we review the mechanisms by which PSII is assembled and turned over in the model green alga Chlamydomonas reinhardtii. This species has been used to make key discoveries in PSII research due to its metabolic flexibility and amenability to genetic approaches. PSII subunits originate from both nuclear and chloroplastic gene products in Chlamydomonas. Nuclear-encoded PSII subunits are transported into the chloroplast and chloroplast-encoded PSII subunits are translated by a coordinated mechanism. Active PSII dimers are built from discrete reaction center complexes in a process facilitated by assembly factors. The phosphorylation of core subunits affects supercomplex formation and localization within the thylakoid network. Proteolysis primarily targets the D1 subunit, which when replaced, allows PSII to be reactivated and completes a repair cycle. While PSII has been extensively studied using Chlamydomonas as a model species, important questions remain about its assembly and repair which are presented here.

59 BASIC BIOLOGICAL SCIENCES↗
DOE OSTI2023

Cationic Cobalt(II) Bisphosphine Hydroformylation Catalysis: In Situ Spectroscopic and Reaction Studies

[HCo(CO) x (bisphosphine)](BF 4 ), x = 1–3, is a highly active hydroformylation catalyst system, especially for internal branched alkenes. In situ infrared spectroscopy (IR), electron paramagnetic resonance (EPR), and nuclear magnetic resonance studies support the proposed catalyst formulation. IR studies reveal the formation of a dicationic Co(I) paramagnetic CO-bridged dimer, [Co 2 (μ-CO) 2 (CO)(bisphosphine) 2 ] 2+ , at lower temperatures formed from the reaction of two catalyst complexes via the elimination of H 2 . Here, DFT studies indicate a dimer structure with square-pyramidal and tetrahedral cobalt centers. This monomer–dimer equilibrium is analogous to that seen for HCo(CO) 4 , reacting to eliminate H 2 and form Co 2 (CO) 8 . EPR studies on the catalyst show a high-spin (S = 3/2) Co(II) complex. Reaction studies are presented that support the cationic Co(II) bisphosphine catalyst as the catalyst species present in this system and minimize the possible role of neutral Co(I) species, HCo(CO) 4 or HCo(CO) 3 (phosphine), as catalysts.

37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CH↗
DOE OSTI2023

A low-cost and realistic noisy light system for studying photosynthesis

Unlike the light conditions commonly used to grow photosynthetic organisms in the research laboratory, the light intensity in real environments is dynamic. A simple and low-cost system is described in which a commercial dimmable LED panel is controlled to simulate a sinusoidal function representing daylight hours and overlaid with stochastic shading events. The output closely resembles light intensity measurements on Earth’s surface on partly cloudy days or in lower levels of plant canopies. Here, this tool may be useful to researchers studying photosynthetic acclimation responses.

59 BASIC BIOLOGICAL SCIENCES↗
DOE OSTI2021

Chloride facilitates Mn(III) formation during photoassembly of the Photosystem II oxygen-evolving complex

The Mn 4 Ca oxygen-evolving complex (OEC) in Photosystem II (PSII) is assembled in situ from free Mn 2+ , Ca 2+ , and water. In an early light-driven step, Mn 2+ in a protein high-affinity site is oxidized to Mn 3+ . Using dual-mode electron paramagnetic resonance spectroscopy, we observed that Mn 3+ accumulation increases as chloride concentration increases in spinach PSII membranes depleted of all extrinsic subunits. At physiologically relevant pH values, this effect requires the presence of calcium. Here, when combined with pH studies, we conclude that the first Mn 2+ oxidation event in OEC assembly requires a deprotonation that is facilitated by chloride.

59 BASIC BIOLOGICAL SCIENCES↗
DOE OSTI2021

Structure of a monomeric photosystem II core complex from a cyanobacterium acclimated to far-red light reveals the functions of chlorophylls $d$ and $f$

Far-red light (FRL) photoacclimation (FaRLiP) in cyanobacteria provides a selective growth advantage for some terrestrial cyanobacteria by expanding the range of photosynthetically active radiation to include far-red/near-infrared light (700 to 800 nm). During this photoacclimation process, photosystem II (PSII), the water:plastoquinone photooxidoreductase involved in oxygenic photosynthesis, is modified. The resulting FRL-PSII is comprised of FRL-specific core subunits and binds chlorophyll (Chl) d and Chl f molecules in place of several of the Chl a molecules found when cells are grown in visible light. These new Chls effectively lower the energy canonically thought to define the “red limit” for light required to drive photochemical catalysis of water oxidation. Changes to the architecture of FRL-PSII were previously unknown, and the positions of Chl d and Chl f molecules had only been proposed from indirect evidence. Here, we describe the 2.25-Å resolution cryo-EM structure of a monomeric FRL-PSII core complex from Synechococcus sp. PCC 7335 cells that were acclimated to FRL. We identify one Chl d molecule in the Chl D1 position of the electron transfer chain, and four Chl f molecules in the core antenna. We also make observations that enhance our understanding of PSII biogenesis, especially on the acceptor side of the complex where a bicarbonate molecule is replaced by a glutamate sidechain in the absence of the assembly factor Psb28. In conclusion, these results provide a structural basis for the lower energy limit required to drive water oxidation, which is the gateway for most solar energy utilization on Earth.

37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CH↗