photosynthesis – Lightsources.org

Elusive missing step in the final act of photosynthesis

2023/05/032023/05/04

After decades of effort and help from SLAC’s X-ray laser, scientists have finally seen the process by which nature creates the oxygen we breathe.

Photosynthesis plays a crucial role in shaping and sustaining life on Earth, yet many aspects of the process remain a mystery. One such mystery is how Photosystem II, a protein complex in plants, algae and cyanobacteria, harvests energy from sunlight and uses it to split water, producing the oxygen we breathe. Now researchers from the Department of Energy’s SLAC National Accelerator Laboratory and Lawrence Berkeley National Laboratory, together with collaborators from Uppsala University, Humboldt University, and other institutions have succeeded in cracking a key secret of Photosystem II.

Using SLAC’s Linac Coherent Light Source (LCLS) and the SPring-8 Angstrom Compact free electron LAser (SACLA) in Japan, they captured for the first time in atomic detail what happens in the final moments leading up to the release of breathable oxygen. The data reveal an intermediate reaction step that had not been observed before.

Find out more on the SLAC website

How a soil microbe could rev up artificial photosynthesis

2022/04/292022/05/05

Researchers discover that a spot of molecular glue and a timely twist help a bacterial enzyme convert carbon dioxide into carbon compounds 20 times faster than plant enzymes do during photosynthesis. The results stand to accelerate progress toward converting carbon dioxide into a variety of products.

Plants rely on a process called carbon fixation – turning carbon dioxide from the air into carbon-rich biomolecules – for their very existence. That’s the whole point of photosynthesis, and a cornerstone of the vast interlocking system that cycles carbon through plants, animals, microbes and the atmosphere to sustain life on Earth.

But the carbon fixing champs are not plants, but soil bacteria. Some bacterial enzymes carry out a key step in carbon fixation 20 times faster than plant enzymes do, and figuring out how they do this could help scientists develop forms of artificial photosynthesis to convert the greenhouse gas into fuels, fertilizers, antibiotics and other products.

Now a team of researchers from the Department of Energy’s SLAC National Accelerator Laboratory, Stanford University, Max Planck Institute for Terrestrial Microbiology in Germany, DOE’s Joint Genome Institute (JGI) and the University of Concepción in Chile has discovered how a bacterial enzyme – a molecular machine that facilitates chemical reactions – revs up to perform this feat.

Rather than grabbing carbon dioxide molecules and attaching them to biomolecules one at a time, they found, this enzyme consists of pairs of molecules that work in sync, like the hands of a juggler who simultaneously tosses and catches balls, to get the job done faster. One member of each enzyme pair opens wide to catch a set of reaction ingredients while the other closes over its captured ingredients and carries out the carbon-fixing reaction; then, they switch roles in a continual cycle.

Read more on the SLAC website

First detailed look at how charge transfer distorts a molecule’s structure

2021/05/042021/05/27

Charge transfer is highly important in most areas of chemistry, including photosynthesis and other processes in living things. A SLAC X-ray laser study reveals how it works in a molecule whose lopsided response to light has puzzled scientists for nearly a decade.

When light hits certain molecules, it dislodges electrons that then move from one location to another, creating areas of positive and negative charge. This “charge transfer” is highly important in many areas of chemistry, in biological processes like photosynthesis and in technologies like semiconductor devices and solar cells.

Even though theories have been developed to explain and predict how charge transfer works, they have been validated only indirectly because of the difficulty of observing how a molecule’s structure responds to charge movements with the required atomic resolution and on the required ultrafast time scales.

In a new study, a research team led by scientists from Brown University, the Department of Energy’s SLAC National Accelerator Laboratory and the University of Edinburgh used SLAC’s X-ray free-electron laser to make the first direct observations of molecular structures associated with charge transfer in gas molecules hit with light.

Molecules of this gas, called N,N′-dimethylpiperazine or DMP, are normally symmetric, with a nitrogen atom at each end. Light can knock an electron out of a nitrogen atom, leaving a positively charged ion known as a “charge center.”

Read more on the SLAC website

Image: In experiments with SLAC’s X-ray free-electron laser, scientists knocked electrons out of a molecule known as DMP to make the first detailed observations of how a process called charge transfer affects its molecular structure. Left: DMP is normally symmetric. Center: When a pulse of light knocks an electron out of one of its nitrogen atoms (blue spheres), it leaves a positively charged ion known as a charge center, shown in pink. This creates a charge imbalance that shifts the positions of atoms. Right: But within three trillionths of a second, the charge redistributes itself between the two nitrogen atoms until it evens out and the molecule becomes symmetric again.

Credit: Greg Stewart/ SLAC National Accelerator Laboratory

Newly discovered photosynthesis enzyme yields evolutionary clues

2020/12/072020/12/10

Rubisco is one of the oldest carbon-fixing enzymes on the planet, taking CO₂ from the atmosphere and fixing it into sugar for plants and other photosynthetic organisms. Form I (“form one”) rubisco goes back nearly 2.4 billion years and is a key focus of scientists studying the evolution of life as well as those seeking to develop bio-based fuels and renewable-energy technologies. A newly discovered form of rubisco—dubbed form I′ (“one prime”)—is thought to represent a missing link in the evolution of photosynthetic organisms, potentially providing clues as to how this enzyme changed the planet.

To learn how form I′ rubisco compares to other rubisco enzymes, researchers performed x-ray crystallography at Advanced Light Source (ALS) Beamline 8.2.2. Then, to capture how the enzyme’s structure changes during different states of activity, they applied small-angle x-ray scattering (SAXS) using Beamline 12.3.1 (SIBYLS). This combination of approaches enables scientists to construct unprecedented models of complex molecules as they appear in nature.

Using European XFEL to shed light on photosynthesis

2019/11/082019/11/14

First membrane protein studied at European XFEL

In a paper now published in Nature Communications an international group of scientists show that the fast X-ray pulse rate produced by the European XFEL can be used to study the structure of membrane proteins such as those involved in the process of photosynthesis. These results open up eagerly awaited experimental opportunities for scientists studying these types of proteins.

Large proteins and protein complexes are difficult to study with traditional structural biology approaches. Large protein complexes, such as those that sit across cell membranes and regulate traffic in and out of cells, are difficult to crystalize and generally only produce small crystals that are hard to analyse. The extremely fast X-ray pulses generated by European XFEL now enable scientists to collect large amounts of data from a stream of small crystals to develop detailed models of the 3D structure of these proteins.

>Read more on the European XFEL website

Image (extract, full illustration in the article): Graphic shows the basic design of a serial femtosecond crystallography experiment at European XFEL. X-ray bursts strike crystallized samples resulting in diffraction patterns that can be reassembled into detailed images.
Credit: Shireen Dooling for the Biodesign Institute at ASU

Research on how light-harvesting bacteria toggle off and on

2019/07/232019/07/31

The results could have long-range implications for artificial photosynthesis and optogenetics—the use of light to selectively activate biological processes.

Cyanobacteria are water-dwelling microbes capable of absorbing sunlight and converting it into chemical energy through photosynthesis. Long ago, ancient versions of these bacteria were incorporated into plant cells, where they eventually evolved into chloroplasts, the organelles responsible for carrying out photosynthesis in green plants. Today, in seeking to develop artificial photosynthesis to harness the sun’s abundant energy, scientists look to cyanobacteria to better understand the nuts and bolts of how natural photosynthesis works.

Cyanobacterial “off switch”

One topic of interest is how cyanobacteria respond to too much light. If a sunlight-harvesting system becomes overloaded with absorbed solar energy, it most likely will suffer some form of damage. Nature has solved the problem in cyanobacteria through a protective mechanism—an energy-quenching “off switch” in which excess solar energy is safely dissipated as heat.

Illustration: X-ray footprinting provides time-resolved information about where key conformational changes occur. On the left is the overall OCP structure. The two structures on the right highlight local areas with increasing protein packing over time (blue shading) and areas with decreasing protein packing over time (red shading). The changes in accessibility are initiated by the movement of the carotenoid molecule (magenta chain).

A timely solution for the photosynthetic oxygen evolving clock

2019/01/252019/01/31

XFEL Hub collaboration reveals the intermediates of the photosynthetic water oxidation clock

A large international collaborative effort aided by the XFEL Hub at Diamond Light Source has generated the most detailed time-resolved studies to date of a key protein involved in photosynthesis. The pioneering work, recently published in Nature, shows how photosystem II harnesses light energy to produce oxygen – insights that could direct a next generation of photovoltaic cells.
>Read more on the Diamond Light Source website

Image: this figure is issued from a video you can watch here.

Researchers create most complete high-res atomic movie of photosynthesis to date

2018/11/082018/11/08

In a major step forward, SLAC’s X-ray laser captures all four stable states of the process that produces the oxygen we breathe, as well as fleeting steps in between. The work opens doors to understanding the past and creating a greener future.

Despite its role in shaping life as we know it, many aspects of photosynthesis remain a mystery. An international collaboration between scientists at SLAC National Accelerator Laboratory, Lawrence Berkeley National Laboratory and several other institutions is working to change that. The researchers used SLAC’s Linac Coherent Light Source (LCLS) X-ray laser to capture the most complete and highest-resolution picture to date of Photosystem II, a key protein complex in plants, algae and cyanobacteria responsible for splitting water and producing the oxygen we breathe. The results were published in Nature today.

Explosion of life

When Earth formed about 4.5 billion years ago, the planet’s landscape was almost nothing like what it is today. Junko Yano, one of the authors of the study and a senior scientist at Berkeley Lab, describes it as “hellish.” Meteors sizzled through a carbon dioxide-rich atmosphere and volcanoes flooded the surface with magmatic seas.
Over the next 2.5 billion years, water vapor accumulating in the air started to rain down and form oceans where the very first life appeared in the form of single-celled organisms. But it wasn’t until one of those specks of life mutated and developed the ability to harness light from the sun and turn it into energy, releasing oxygen molecules from water in the process, that Earth started to evolve into the planet it is today. This process, oxygenic photosynthesis, is considered one of nature’s crown jewels and has remained relatively unchanged in the more than 2 billion years since it emerged.

Image: Using SLAC’s X-ray laser, researchers have captured the most complete high-res atomic movie to date of Photosystem II, a key protein complex in plants, algae and cyanobacteria responsible for splitting water and producing the oxygen we breathe.
Credit: Gregory Stewart, SLAC National Accelerator Laboratory)

Insight into catalysis through novel study of X-ray absorption spectroscopy

2018/07/312018/08/07

An international team has made a breakthrough at BESSY II.

For the first time, they succeeded in investigating electronic states of a transition metal in detail and drawing reliable conclusions on their catalytic effect from the data. These results are helpful for the development of future applications of catalytic transition-metal systems. The work has now been published in Chemical Science, the Open Access journal of the Royal Society of Chemistry.

Many important processes in nature depend on catalysts, which are atoms or molecules that facilitate a reaction, but emerge from it themselves unchanged. One example is photosynthesis in plants, which is only possible with the help of a protein complex comprising four manganese atom sites at its centre. Redox reactions, as they are referred to, often play a pivotal role in these types of processes. The reactants are reduced through uptake of electrons, or oxidized through their release. Catalytic redox processes in nature and industry often only succeed thanks to suitable catalysts, where transition metals supply an important function.

Image: Manganese compounds also play a role as catalysts in photosynthesis.
Credit: HZB

Magnetic trick triples the power of SLAC’s X-ray laser

2018/01/312018/02/01

The new technique will allow researchers to observe ultrafast chemical processes previously undetectable at the atomic scale.

Scientists at the Department of Energy’s SLAC National Accelerator Laboratory have discovered a way to triple the amount of power generated by the world’s most powerful X-ray laser. The new technique, developed at SLAC’s Linac Coherent Light Source (LCLS), will enable researchers to observe the atomic structure of molecules and ultrafast chemical processes that were previously undetectable at the atomic scale.

The results, published in a Jan. 3 study in Physical Review Letters (PRL), will help address long-standing mysteries about photosynthesis and other fundamental chemical processes in biology, medicine and materials science, according to the researchers.

“LCLS produces the world’s most powerful X-ray pulses, which scientists use to create movies of atoms and molecules in action,” said Marc Guetg, a research associate at SLAC and lead author of the PRL study. “Our new technique triples the power of these short pulses, enabling higher contrast.”

>Read more on the LCSL website

Picture: The research team, from left: back row, Yuantao Ding, Matt Gibbs, Nora Norvell, Alex Saad, Uwe Bergmann, Zhirong Huang; front row, Marc Guetg and Timothy Maxwell.
Credit: Dawn Harmer/SLAC

Fuel from the sun: insight into electrode performance

2018/01/232018/02/02

Soft x-ray studies of hematite electrodes—potentially key components in producing fuel from sunlight—revealed the material’s electronic band positions under realistic operating conditions.

In photosynthesis, plants use sunlight to split water into oxygen and hydrogen. The oxygen is released into the atmosphere, and the hydrogen is used to produce molecules—such as carbohydrates and sugars—that store energy in chemical bonds. Such compounds constitute the original feedstocks for subsequent forms of fuel consumed by society.

Photoelectrochemical (PEC) water splitting is a form of “artificial” photosynthesis that uses semiconductor material, rather than organic plant material, to facilitate water splitting. Electrodes made of semiconductor material are immersed in an electrolyte, with sunlight driving the water-splitting process. The performance of such PEC devices is largely determined at the interface between the photoanode (the electrode at which light gets absorbed) and the electrolyte.

>Read more on the ALS webpage

Photo: Roy Kaltschmidt