In vitro-mutagenesis of NADPH:protochlorophyllide oxidoreductase B: two distinctive protochlorophyllide binding sites participate in enzyme catalysis and assembly

Molecular Genetics and Genomics : MGG
C ReinbotheSteffen Reinbothe

Abstract

NADPH:protochlorophyllide oxidoreductase (POR) B is a key enzyme for the light-induced greening of etiolated angiosperm plants. It is nucleus-encoded, imported into the plastids posttranslationally, and assembled into larger light-harvesting POR:protochlorophyllide complexes termed LHPP (Reinbothe et al., Nature 397:80-84, 1999). An in vitro-mutagenesis approach was taken to study the role of the evolutionarily conserved Cys residues in pigment binding. Four Cys residues are present in the PORB of which two, Cys276 and Cys303, established distinct pigment binding sites, as shown by biochemical tests, protein import studies, and in vitro-reconstitution experiments. While Cys276 constituted the Pchlide binding site in the active site of the enzyme, Cys303 established a second, low affinity pigment binding site that was involved in the assembly and stabilization of imported PORB enzyme inside etioplasts.

References

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Citations

Aug 30, 2008·Proceedings of the National Academy of Sciences of the United States of America·Frank BuhrChristiane Reinbothe
May 18, 2007·Annual Review of Microbiology·Aline Gomez Maqueo Chew, Donald A Bryant
Aug 31, 2010·Trends in Plant Science·Christiane ReinbotheSteffen Reinbothe
Feb 17, 2015·Photochemical & Photobiological Sciences : Official Journal of the European Photochemistry Association and the European Society for Photobiology·Aoife A Ryan, Mathias O Senge
Oct 18, 2020·Biological Chemistry·Daniel WittmannBernhard Grimm
May 18, 2021·Frontiers in Plant Science·Katalin Solymosi, Beata Mysliwa-Kurdziel

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