Andreas Hansson

TL;DR: The fate of the modified components, the energetic costs to the cell of replacing such components, as well as strategies to minimize transfer of oxidatively damaged components to the next generation are considered.

TL;DR: In chlorophyll biosynthesis, insertion of Mg(2+) into protoporphyrin IX is catalysed in an ATP-dependent reaction by a three-subunit (BchI, BchD and BchH) enzyme magnesium chelatase, and the three-dimensional structure of the ATP-binding subunit BchI is presented to provide insight into the subunit organisation of magnesiumChelatase and the homologous colbalt chelatases.

TL;DR: The X-ray structure revealed the active site of the enzyme, to which only one of the isomers was bound, and for the first time allowed characterization of the mode of porphyrin macrocycle distortion by ferrochelatase.

TL;DR: It is shown that the Arabidopsis ntrc mutant is perturbed in chlorophyll biosynthesis and accumulate intermediates preceding protochlorophyllide formation, supporting the hypothesis that this NADPH‐dependent hydrogen peroxide scavenging system is particularly important during periods with limited reducing power from photosynthesis, e.g. under chloroplast biogenesis.

TL;DR: It is hypothesized that the association of the 42-k Da subunit with the 70-kDa subunit allows them to form a specific complex with the 140-k da subunit and that this complex inserts Mg2+ into protoporphyrin IX.