When it comes to visual entertainment, three-dimensional viewing can be quite eye-opening. So, too, in science where a recent finding involving University of Iowa researchers used three-dimensional imaging to understand how a bacterial enzyme can take oxygen from air and use it to convert certain molecules into useful chemicals.
Specifically, the scientists saw that naphthalene dioxygenase, a bacterial enzyme, can bind oxygen (to iron) in a side-on fashion and add it on to naphthalene, a hydrocarbon molecule. The discovery is a result of the first three-dimensional imaging of naphthalene dioxygenase, a member of the family of enzymes called Rieske dioxygenases. The findings could help lead to the development of microorganisms that can clean up toxic and cancer-causing waste in the environment and to the development of novel drugs. The research results appear in the Feb. 14 issue of Science.
"The more we know about how enzymes catalyze reactions, the better able we are to modify them -- to improve or stop reactions, as desired" said S. Ramaswamy, Ph.D., UI professor of biochemistry and one of the studys authors.
Becky Soglin | EurekAlert!
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A study led by scientists of the Max Planck Institute for the Structure and Dynamics of Matter (MPSD) at the Center for Free-Electron Laser Science in Hamburg presents evidence of the coexistence of superconductivity and “charge-density-waves” in compounds of the poorly-studied family of bismuthates. This observation opens up new perspectives for a deeper understanding of the phenomenon of high-temperature superconductivity, a topic which is at the core of condensed matter research since more than 30 years. The paper by Nicoletti et al has been published in the PNAS.
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