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A New Way of Looking at Photosystem II

By Guest PostJune 14, 2012Sciencealgae, angstroms, bacteria, berkeley lab, carbon dioxide, catalytic cycle, critical formation, cryogenic freezing, electrochemical energy, electrons, femtosecond timescale, femtosecond x ray pulses, green, green plants, hydrogen atom, hydrogen ions, jan kern, junko yano, knowledge, lcls, microcrystals, nicholas sauter, oxidation states, oxygen molecules, paul adams, photooxidation, photosynthesis, photosystem ii, protein crystallography, proteins, protons, renewable energy, resolution, slac, solar energy, synchrotron radiation, terabytes of data, uwe bergmann, vittal yachandra, water, xray diffraction, xrays

Berkeley Lab and SLAC Researchers Study Key Protein Complex Crucial to Photosynthesis

Future prospects for clean, green, renewable energy may hinge upon our ability to mimic and improve upon photosynthesis – the process by which green plants, algae and some bacteria convert solar energy into electrochemical energy. An artificial version of photosynthesis, for example, could use sunlight to produce liquid fuels from nothing more than carbon dioxide and water. First, however, scientists need a better understanding of how a large complex of proteins, called photosystem II, is able to split water molecules into oxygen, electrons and hydrogen ions (protons). A new road to reaching this understanding has now been opened by an international team of researchers, led by scientists at the U.S. Department of Energy (DOE)’s Lawrence Berkeley National Laboratory (Berkeley Lab) and SLAC National Accelerator Laboratory.

Using ultrafast, intensely bright pulses of X-rays from SLAC’s Linac Coherent Light Source (LCLS), the research team produced the first ever images at room temperature of microcrystals of the photosystem II complex. Previous imaging studies, using X-rays generated via synchrotron radiation sources, required cryogenic freezing, which alters the samples. Also, to catalyze its reactions, photosystem II relies upon an enzyme that contains a manganese-calcium cluster that is highly sensitive to radiation. With the high-intensity femtosecond X-ray pulses of the LCLS, the research team was able to record intact images of these clusters before the radiation destroyed them. (more…)

Correct Protein Folding:

By Guest PostFebruary 26, 2012Sciencealzheimers, amino acids, atp hydrolysis, atp molecules, biomolecular nanomachines, cancer, chain, chaperonin, corie ralston, crystal structure, diseases, eukaryotes, gold standard, jose pereira, light sources, macromolecules, Nanotechnology, nicholai douglas, nucleotide, parkinson's, paul adams, prokaryotes, protein, ramya kumar, xray beams

*Berkeley Lab Researchers Identify Structure of Key Control Element Behind Protein Misfolding That Can Lead to Disease*

The gold standard for nanotechnology is nature’s own proteins. These biomolecular nanomachines – macromolecules forged from peptide chains of amino acids – are able to fold themselves into a dazzling multitude of shapes and forms that enable them to carry out an equally dazzling multitude of functions fundamental to life. As important as protein folding is to virtually all biological systems, the mechanisms behind this process have remained a mystery. The fog, however, is being lifted.

A team of researchers with the U.S. Department of Energy (DOE)’s Lawrence Berkeley National Laboratory (Berkeley Lab), using the exceptionally bright and powerful x-ray beams of the Advanced Light Source, have determined the crystal structure of a critical control element within chaperonin, the protein complex responsible for the correct folding of other proteins. The incorrect or “misfolding” of proteins has been linked to many diseases, including Alzheimer’s, Parkinson’s and some forms of cancer. (more…)

Clearing a Potential Road Block to Bisabolane

By Guest PostJanuary 14, 2012Scienceabies grandis, abies grandis α bisabolene synthase, advanced biofuels, agbis, andy degiovanni, berkeley lab, biofuel, biosynthetic alternative, bisabolane, ca, chemical compounds, cofactors, d2 diesel fuel, emeryville, enzyme, evolutionary heritage, flavorings, fragrances, grand fir, green energy, inhibitors, jay keasling, jose pereira, masood hadi, microbes, microbial based production, pamela peralta yahya, paul adams, precursor, protein, protein crystal structure, renewable alternative, resolution, ryan mcandrew, synthases in plants, terpene class, terpenoid synthases, three dimensional crystal structure, trucking industry, united states, x ray crystallography

*Joint BioEnergy Institute Researchers Identify Key Enzyme Structure*

The recent discovery that bisabolane, a member of the terpene class of chemical compounds used in fragrances and flavorings, holds high promise as a biosynthetic alternative to D2 diesel fuel has generated keen interest in the green energy community and the trucking industry. Now a second team of researchers with the U.S Department of Energy (DOE)’s Joint BioEnergy Institute (JBEI) has determined the three-dimensional crystal structure of a protein that is key to boosting the microbial-based production of bisabolane as an advanced biofuel.

The JBEI research team, led by bioengineers Paul Adams and Jay Keasling, solved the protein crystal structure of an enzyme in the Grand fir (Abies grandis) that synthesizes bisabolene, the immediate terpene precursor to bisabolane. The performance of this enzyme – the Abies grandis α-bisabolene synthase (AgBIS) – when engineered into microbes, has resulted in a bottleneck that hampers the conversion by the microbes of simple sugars into bisabolene. (more…)

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A New Way of Looking at Photosystem II

Correct Protein Folding:

Clearing a Potential Road Block to Bisabolane