2016 Rudi Lemberg Travelling Fellowship Lecture - Detection of Nitric Oxide: Combining EPR and NMR

About the talk

This is a talk about harnessing two magnetic resonance methods, EPR and NMR to observe interesting natural metabolites in-vivo. Nitric oxide is involved in muscle relaxation and maintenance of blood pressure and is a product of the enzyme catalyzed conversion of arginine by nitric oxide synthase. NO is produced in the brain as a synaptic neuronal messenger. The paramagnetic gas NO is effectively EPR silent. However, it was shown that one can ‘trap’ NO as the ferrous iron complex in a coordination complex involving dithiocarbamates. The basal levels of NO, however, are sub micromolar, hence too small to observe in-vivo. even after long-term accumulation. However, there are pathological states where NO levels are exceptionally high, approaching sub-millimolar concentrations.

Spin-trapped NO complex is an excellent MRI contrast agent, allowing much higher resolution imaging by virtue of the efficient paramagnetic relaxation of water protons in the tissue near the NO. Hence a temporal measurement of NO generation can be imaged ‘indirectly’ (but locally) in the MRI image, including the effects of nitric oxide synthase inhibitors where the MRI contrast was diminished with the reduced levels of generated NO.

About the speaker

Professor Lawrence J. Berliner, University of Denver, and Emeritus Professor of The Ohio State University, is a pioneer in protein structural and free radical research. His team developed thiol specific spin labels, which facilitated site directed spin labelling for studying protein structure in solution by electron paramagnetic resonance (EPR). His research has involved protein-protein interactions, free radicals and in-vivo EPR. He is a fellow of the prestigious American Academy of Arts and Sciences, the American Chemical Society, Past-President of the International EPR Society. He and has received the 2000 Silver Medal of the International EPR Society and the 2005 Lifetime Achievement Award in Biological EPR Spectroscopy. He is Editor-in-Chief of Cell Biochemistry and Biophysics and has edited over 30 books on magnetic resonance applications in biology and medicine. He has spoken at many conferences the world on proteins, magnetic resonance the history of the Nobel Prize.

About the Fellowship

The Rudi Lemberg Travelling Fellowship commemorates the contributions of Professor M.R. Lemberg, FAA, FRS to science in Australia. The Fellowship is financed through the generous bequest of Mrs Hanna Lemberg and the Society for Biochemistry and Molecular Biology.

The purpose of the Fellowship is to enable either Australian or overseas scientists of standing to visit Australian scientific centers and to deliver lectures.

Room 302, Level 3 LIMS2 building Molecular Science, La Trobe University,Kingsbury Drive Victoria

Contact Information

Professor Brian Smith
Email: brian.smith@latrobe.edu.au

3:00 PM - 4:00 PM September 07, 2016
FOR Scientist
Add to reminder to
Add to Calendar 07/09/2016 3:00 PM 07/09/2016 4:00 PM Australia/Sydney 2016 Rudi Lemberg Travelling Fellowship Lecture - Detection of Nitric Oxide: Combining EPR and NMR

About the talk

This is a talk about harnessing two magnetic resonance methods, EPR and NMR to observe interesting natural metabolites in-vivo. Nitric oxide is involved in muscle relaxation and maintenance of blood pressure and is a product of the enzyme catalyzed conversion of arginine by nitric oxide synthase. NO is produced in the brain as a synaptic neuronal messenger. The paramagnetic gas NO is effectively EPR silent. However, it was shown that one can ‘trap’ NO as the ferrous iron complex in a coordination complex involving dithiocarbamates. The basal levels of NO, however, are sub micromolar, hence too small to observe in-vivo. even after long-term accumulation. However, there are pathological states where NO levels are exceptionally high, approaching sub-millimolar concentrations.

Spin-trapped NO complex is an excellent MRI contrast agent, allowing much higher resolution imaging by virtue of the efficient paramagnetic relaxation of water protons in the tissue near the NO. Hence a temporal measurement of NO generation can be imaged ‘indirectly’ (but locally) in the MRI image, including the effects of nitric oxide synthase inhibitors where the MRI contrast was diminished with the reduced levels of generated NO.

About the speaker

Professor Lawrence J. Berliner, University of Denver, and Emeritus Professor of The Ohio State University, is a pioneer in protein structural and free radical research. His team developed thiol specific spin labels, which facilitated site directed spin labelling for studying protein structure in solution by electron paramagnetic resonance (EPR). His research has involved protein-protein interactions, free radicals and in-vivo EPR. He is a fellow of the prestigious American Academy of Arts and Sciences, the American Chemical Society, Past-President of the International EPR Society. He and has received the 2000 Silver Medal of the International EPR Society and the 2005 Lifetime Achievement Award in Biological EPR Spectroscopy. He is Editor-in-Chief of Cell Biochemistry and Biophysics and has edited over 30 books on magnetic resonance applications in biology and medicine. He has spoken at many conferences the world on proteins, magnetic resonance the history of the Nobel Prize.

About the Fellowship

The commemorates the contributions of Professor M.R. Lemberg, FAA, FRS to science in Australia. The Fellowship is financed through the generous bequest of Mrs Hanna Lemberg and the Society for Biochemistry and Molecular Biology.

The purpose of the Fellowship is to enable either Australian or overseas scientists of standing to visit Australian scientific centers and to deliver lectures.

Room 302, Level 3 LIMS2 building Molecular Science, La Trobe University,Kingsbury Drive Victoria false DD/MM/YYYY

Contact Information

Professor Brian Smith
Email: brian.smith@latrobe.edu.au

3:00 PM - 4:00 PM September 07, 2016

© 2024 Australian Academy of Science

Top