X-ray Absorption Spectroscopy

Fighting Antibiotic Resistance: The dapE-encoded N-succinyl-L,L-Diaminopimelic Acid Desuccinylase from Haemophilus influenzae is a Dinuclear Metallohydrolase

April 30, 2004

Antibiotics and the bacteria they attack are engaged in a constant race to out-evolve one another. An antibiotic is effective against specific bacteria only so long before the random mutations that all bacteria undergo make them resistant to that particular drug. Recently, scientists from the University of Georgia, Utah State University, and Guilford Pharmaceuticals carried out studies at SSRL that could enable drug designers to pull ahead, at least for a while, by developing a new class of antibiotics.

Remediation of Uranium-contaminated Ground Water at Fry Canyon, Utah

November 28, 2003

A new technology that acts like a giant underground filter is successfully beginning to clean up the uranium contaminating an aquifer in a remote Utah canyon. Uranium contamination in groundwater is a serious problem because the toxic metal can travel long distances in underground aquifers, which are vital sources of fresh water for people, animals and agriculture. Recent research at SSRL showed that the filters-called PRBs (permeable reactive barrier) do intercept uranium, but in an unexpected way that has important implications for monitoring, costs, and future technology selection.

Converting Methane to Methanol: Structural Insight into the Reaction Center of Particulate Methane Monooxygenase

October 31, 2003

A team headed by Timothy Stemmler of Wayne State University's School of Medicine and Amy Rosenzweig at Northwestern University, has isolated a new form of a bacterial enzyme that efficiently converts methane to methyl alcohol. This enzyme is isolated from methanotropic bacteria, which are found in soil, landfills, groundwater, seawater, hot springs and even the Antarctic. 

X-ray Absorption Spectroscopy Catches the Chemical Form of Mercury in Fish

August 29, 2003

The presence of "methyl mercury" in fish is well-known, but until now the detailed chemical identity of the mercury has remained a mystery. In an x-ray absorption spectroscopy study published in the August 29 issue of Science (Science 301, 2003: 1203;Science now: Murky Picture on Fish Mercury), SSRL scientists report that the chemical form of mercury involves a sulfur atom (most likely in a so-called aliphatic form). The study presents significant new knowledge - because the toxic properties of mercury (or any element) are critically dependent upon its chemical form - and represents an important milestone in developing an understanding of how harmful mercury in fish might actually be. The study was carried out by SSRL staff scientists Ingrid Pickering and Graham George and postdoctoral fellow Hugh Harris using SSRL's structural molecular biology beam line 9-3. The very high flux, excellent beam stability and state-of-the-art detector technology allowed the team to measure samples of fish containing micromolar levels of mercury, much lower than had previously been possible.

Fate and Stability of Cr Following Reduction by Microbially Generated Fe(II)

May 30, 2003

Industrial activities have led to widespread chromium (Cr) contamination in the environment. Although Cr is an essential element for humans, the hexavalent form is toxic, mutagenic and carcinogenic. Consequently, the presence of Cr in the environment poses a serious threat to human and animal welfare. However, the toxicity of Cr is a function of oxidation state. For example, hexavalent Cr has a high solubility in soils and groundwater and, as a consequence, tends to be mobile in the environment.

Solvent Tuning of Properties of Iron-Sulfur Clusters in Proteins

November 29, 2007

Proteins containing iron-sulfur clusters are ubiquitous in nature and catalyze one-electron transfer processes. These proteins have evolved into two classes that have large differences in their electrochemical potentials: high potential iron-sulfur proteins (HiPIPs) and bacterial ferredoxins (Fds). The role of the surrounding protein environment in tuning these redox potentials has been a persistent puzzle in the understanding of biological electron transfer. Although high potential iron-sulfur proteins and ferredoxins have the same iron-sulfur structural motif, there are large differences in their electrochemical potentials.

The Structure of a Reaction Intermediate in Enzymatic Halogenation

March 31, 2008

Halogenated natural products play important roles as antibiotics, antifungals, and antitumor agents. The process of halogenation involves the replacement of a hydrogen with a halide (such as chloride or bromide), and is a challenging task for a synthetic chemist. However, the iron-containing enzymes in the haloperoxidase and halogenase families readily catalyze these reactions. It is thought that when this reaction occurs, the iron in the enzyme is at a high-valent Fe(IV) state, and that this species is responsible for removing a hydrogen atom (called an abstraction) from the substrate, creating a substrate radical, and that a halogen radical is subsequently transferred to the substrate to complete the halogenation reaction.

In situ Observation of Sulfur in Living Mammalian Cells: Uptake of Taurine into MDCK Cells

May 30, 2008

Sulfur is essential for life, playing important roles in metabolism and protein structure and function. Although information on sulfur biochemistry is highly desirable, it is an element that is difficult to study as it is not easily accessible with most biophysical techniques. However, sulfur x-ray absorption spectroscopy (XAS) is one such method and has become increasingly used for the study of sulfur in biological systems. Recently, a group of researchers from Stanford University, the University of Saskatchewan, SSRL, and ExxonMobil used SSRL's Beam Line 6-2 for an in situ sulfur XAS study of living mammalian cell cultures.

Insights into the Role of the Tyr-Cys Cross-link in Galactose Oxidase from Sulfur K-edge Spectroscopy

May 29, 2012

The continuous advancement of X-ray spectroscopic techniques allows us to probe the structure of biological machineries for smaller samples in more dilute concentrations and thus to ask tough scientific questions about problems that have not been possible in the past. Careful biochemical preparation and systematic analytical characterization resulted in galactose oxidase samples that could be interrogated by X-rays. This metalloenzyme contains a copper at its active site that is coordinated to a cross-linked tyrosine and cysteine ligand, which both are essential to convert alcohols and sugars to their oxidized aldehyde forms by oxygen molecule. The remarkable feature of this reaction that it is selective and does not results in formation of carboxylates (a form of vinegar).

Beamline 4-3 and the Rescue of Ancient Warships

May 29, 2012

Nearly 400 years ago, the Swedish warship Vasa sank to its watery grave. In 287 BCE, a Roman warship with its bronze naval ram sank after battle to the bottom of the sea. And in 1545, the flagship of Henry VIII’s navy, the Mary Rose, sank outside of Portsmouth while maneuvering to engage the French fleet. Using SSRL Beam Line 4-3, a team of SSRL and University of Palermo researchers measured x-ray spectra of the sulfur inside wooden sections of the Roman ram, revealing the kinds of sulfur hidden within.

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