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Orange is the new red

7/6/2015

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Berkeley Lab Study Shows Orange Carotenoid Protein Shifts More Than Just Color for Cyanobacterial Photoprotection
Overexposure to sunlight, which is damaging to natural photosynthetic systems of green plants and cyanobacteria, is also expected to be damaging to artificial photosynthetic systems. Nature has solved the problem through a photoprotection mechanism called “nonphotochemical-quenching,” in which excess solar energy is safely dissipated as heat from one molecular system to another. With an eye on learning from nature’s success, a team of Berkeley Lab researchers has discovered a surprising key event in this energy-quenching process.
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Translocation of the carotenoid pigment within a critical light-sensitive protein called the Orange Carotenoid Protein triggers a shifting of the protein from the light-absorbing orange state to the energy- quenching red state, providing cyanobacteria with protection from too much sunlight.
In a study led by Cheryl Kerfeld, a structural biologist who holds joint appointments with Berkeley Lab’s Physical Biosciences Division and Michigan State University, the research team found that in cyanobacteria the energy-quenching mechanism is triggered by an unprecedented, large-scale movement (relatively speaking) from one location to another of the carotenoid pigment within a critical light-sensitive protein called the Orange Carotenoid Protein (OCP). As a result of this translocation, the carotenoid changes its shape slightly and interacts with a different set of amino acid neighbors causing the protein to shift from an “orange” light-absorbing state to a “red” photoprotective state. This turns out to be an unanticipated molecular priming event in photoprotection.
“Prior to our work, the assumption was that carotenoids are static, held in place by the protein scaffold,” Kerfeld says. “Having shown that the translocation of carotenoid within the protein is a functional trigger for photoprotection, scientists will need to revisit other carotenoid-binding protein complexes to see if translocation could play a role in those as well. Understanding the dynamic function of carotenoids should be useful for the design of future artificial photosynthetic systems.”
Read the full article here
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UGA researchers identify, name toxic cyanobacteria

2/19/2015

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Source: uga.edu
Athens, Ga. - University of Georgia researchers have formally identified and named toxic cyanobacteria that have been killing American bald eagles across the Southeast.

After years of studying the cyanobacteria coating the leaves of water plants in lakes, researchers in UGA's Warnell School of Forestry and Natural Resources have determined that it is a previously undiscovered species in a new genus. In a paper published recently in the journal Phytotaxa, they named it Aetokthonos hydrillicola and lay out evidence that it is responsible for the eagle deaths.

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Warnell researchers spotted an eagle afflicted with avian vacuolar myelinopathy near Lake Thurmond in Georgia just days before finding it dead. (Credit: Rebecca Haynie)
"This new species has a growth form and gene sequence so unusual that it does not fit into any of the existing families," said Susan Wilde, the Warnell professor who has been leading the research. "The naming convention for cyanobacteria is to use Greek for the genus—Aetokthonos translates to ‘eagle-killer.' The species name is always Latin, and hydrillicola means ‘lives on hydrilla.'"

Beginning in the mid-1990s, American bald eagles started to die off in noticeable numbers from a neurological disease called avian vacuolar myelinopathy. AVM was first found in Arkansas in 1994, but over the past two decades, 160 eagles are known to have died across the Southeast from the disease, including 80 from one Georgia impoundment on the Savannah River, the J. Strom Thurmond Reservoir.

read the full article here!
The study is online here
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Scientists Capture live bacteria Portraits for the first time

2/19/2015

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Source: chinatopix.com
For the first time in history, researchers were able to observe a chemical bond being born.


Using an X-ray laser at the Department of Energy's SLAC National Accelerator Laboratory, scientists caught their first glimpse of the transition state in which two atoms begin to form a weak bond in the first steps of transforming into a molecule.

Picture
(Photo : SLAC National Accelerator Laboratory) X-ray portraits of living cyanobacteria using SLAC's Linac Coherent Light Source.

Read the full article here!
The findings could lead to X-ray exploration of the molecular machinery at work in viral infections, cell division, photosynthesis and other processes.


"This is the very core of all chemistry. It's what we consider a Holy Grail, because it controls chemical reactivity. But because so few molecules inhabit this transition state at any given moment, no one thought we'd ever be able to see it," said Professor Anders Nilsson at the SLAC/Stanford SUNCAT Center for Interface Science and Catalysis and study lead author.

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  • About Us
    • Who We Are >
      • About CLERC
      • BOARD OF DIRECTORS
      • STAFF
      • Collaborators
    • What We Do >
      • Fire & Forestry >
        • Community Projects >
          • Hazardous Fuel Reduction Project - Phase 1
          • Wildfire Resilience Project - Phase 1
          • Northshore Fuels Team
          • South Lake Chipping Program
          • Fox Drive Fire Prevention Project
          • Middletown and Cobb Evacuation Route Clearing
          • Bottle Rock Rd Project
        • Cost-Share Programs >
          • North Bay Forest Improvement Program (NBFIP)
          • Building Fire Resiliency in California's Coast Range Forests and Grasslands
      • Hitch Observation Program
  • The CLERC Lab
  • Resources
    • Current Conditions
    • Lab Forms
    • Report Hitch Sighting
    • Lake County TREX
    • Wildfire Resiliency Resources
    • The CLERC Library
  • Connect
    • CLERC News
    • Work With Us
    • Contact Us >
      • Landowner Contact Form
    • Donate