U.S.-Hungary Biophysical Studies of the Enzyme Thiocapsa Roseopersicina Hydrogenases

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This U.S.-Hungarian research project involves Michael Maroney of the University of Massachusetts, Amherst, and Csaba Bagyinka of the Institute of Biophysics at the Hungarian Biological Research Center, Szeged. They intend to examine the biological processes in hydrogenase reaction mechanisms, which catalyze the reversible two-electron redox chemistry of dihydrogen. The project features work with the enzyme Thiocapsa roseopersicina.Theory suggests a number of possibilities for structures of T. roseopersicina catalytic intermediates which the international team will test by spectroscopic and other physical probes. To do so the researchers plan to use time-resolved FTIR studies for determining the species involved in catalysis. They will characterize interconversions and their rates, hoping to detect kinetic intermediates and follow evolving thermodynamic microstates. The US-Hungarian partners specifically seek answers to questions about what roles protons play in determining the charge on active sites, what redox states are involved in catalysis, or whether protonated cysteines are present. If successful, findings may provide clues applicable to conversion of chemical energy to electricity for fuel cells and to storage of solar energy in chemical form via photochemical hydrogen production. This international project in biophysics research fulfills the program objective of advancing scientific knowledge by enabling experts in the Untied States and Central Europe to combine complementary talents and share research resources in areas of strong mutual interest and competence.