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Models For Molybdenum Coordination During The Catalytic Cycle Of Periplasmic Nitrate Reductase From Paracoccus Denitrificans Derived From Epr And Exafs Spectroscopy, Clive S. Butler, John M. Charnock, Brian Bennett, Heather J. Sears, Ann J. Reilly, Stuart J. Ferguson, C. David Garner, David J. Lowe, Andrew J. Thomson, Ben C. Berks, David J. Richardson
Models For Molybdenum Coordination During The Catalytic Cycle Of Periplasmic Nitrate Reductase From Paracoccus Denitrificans Derived From Epr And Exafs Spectroscopy, Clive S. Butler, John M. Charnock, Brian Bennett, Heather J. Sears, Ann J. Reilly, Stuart J. Ferguson, C. David Garner, David J. Lowe, Andrew J. Thomson, Ben C. Berks, David J. Richardson
Physics Faculty Research and Publications
The periplasmic nitrate reductase from Paracoccus denitrificans is a soluble two-subunit enzyme which binds two hemes (c-type), a [4Fe-4S] center, and a bis molybdopterin guanine dinucleotide cofactor (bis-MGD). A catalytic cycle for this enzyme is presented based on a study of these redox centers using electron paramagnetic resonance (EPR) and extended X-ray absorption fine structure (EXAFS) spectroscopies. The Mo(V) EPR signal of resting NAP (High g [resting]) has gav = 1.9898 is rhombic, exhibits low anisotropy, and is split by two weakly interacting protons which are not solvent-exchangeable. Addition of exogenous ligands to this resting …