Ritimukta Sarangi

Abstract Enzymes that catalyze long-range electron transfer (ET) reactions often function as higher order complexes that possess two structurally symmetrical halves. The functional advantages for such an architecture remain a mystery. Using cryoelectron microscopy we capture snapshots of the nitrogenase-like dark-operative protochlorophyllide oxidoreductase (DPOR) during substrate binding and turnover.

Introduction Click to copy section linkSection link copied! One of the major challenges in homogeneous catalysis is the use of first-row transition metals as catalysts. (1) The reactivity of these metals is fundamentally different from that of their heavier and rarer noble metal counterparts that are currently often employed in catalysis. First-row transition metals tend to form high-spin complexes, for example, and they are typically more prone to 1e– reactivity than noble metals.

Introduction Click to copy section linkSection link copied! One of the major challenges in homogeneous catalysis is the use of first-row transition metals as catalysts. (1) The reactivity of these metals is fundamentally different from that of their heavier and rarer noble metal counterparts that are currently often employed in catalysis. First-row transition metals tend to form high-spin complexes, for example, and they are typically more prone to 1e– reactivity than noble metals.