AADH Induces Substrate Conformation Crucial For Promoting Vibration That Reduces The Effective Potential Energy Barrier To Proton Transfer
In this study,we have employed combined quantum mechanical/molecular mechanical methods with molecular dynamics and potential energy surface calculations to investigate how enzyme and substratemotion affects the energy barrier to proton transfer for the rate-limiting H-transfer step in aromatic amine dehydrogenase (AADH) with tryptamine as substrate.
In particular, the conformation of the iminoquinone adduct induced by AADH was found to be essential for a promoting vibration identified previously-this lowers significantly the 'effective' potential energy barrier, that is the barrier which remains to be surmounted following collective, thermally equilibrated motion attaining a quantum degenerate state of reactants and products.
When the substrate adopts a conformation similar to that in the free iminoquinone, this barrier was found to increase markedly. This is consistent with AADH facilitating the H-transfer event by holding the substrate in a conformation that induces a promoting vibration.
Journal of the Royal Society Interface
Journal of the Royal Society Interface is the Society's cross-disciplinary publication promoting research at the interface between the physical and life sciences. It offers rapidity, visibility and high-quality peer review and is ranked fourth in JCR'S multidisciplinary category.
Journal of the Royal Society Interface
AADH induce Substrat conformaþie crucial pentru Promovarea vibratii care reduce Potential de energie eficientã barierã în calea Proton Transfer - AADH Induces Substrate Conformation Crucial For Promoting Vibration That Reduces The Effective Potential Energy Barrier To Proton Transfer - articole medicale engleza - startsanatate