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Bastien Christ

Researcher at University of Zurich

Publications -  24
Citations -  930

Bastien Christ is an academic researcher from University of Zurich. The author has contributed to research in topics: Chlorophyll & Chloroplast. The author has an hindex of 15, co-authored 23 publications receiving 705 citations. Previous affiliations of Bastien Christ include Massachusetts Institute of Technology & University of São Paulo.

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Mechanism and Significance of Chlorophyll Breakdown

TL;DR: This review summarizes the current knowledge on the biochemical reactions involved in chlorophyll breakdown, with a special focus on the second-phase reactions and the fate of by-products that are released from chlorophylla during its breakdown.
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Cytochrome P450 CYP89A9 Is Involved in the Formation of Major Chlorophyll Catabolites during Leaf Senescence in Arabidopsis

TL;DR: A group of distinct dioxobilin-type chlorophyll catabolites (DCCs) are identified as the major breakdown products in wild-type Arabidopsis, representing more than 90% of the chlorophyh of green leaves.
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Repeated evolution of cytochrome P450-mediated spiroketal steroid biosynthesis in plants.

TL;DR: In this article, the diosgenin-biosynthetic pathway in plants was investigated in the presence of a pair of cytochromes P450 that catalyzes oxidative 5,6-spiroketalization of cholesterol to produce diogenin.
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MES16, a Member of the Methylesterase Protein Family, Specifically Demethylates Fluorescent Chlorophyll Catabolites during Chlorophyll Breakdown in Arabidopsis

TL;DR: It is demonstrated that MES16 is an integral component of Chl breakdown in Arabidopsis and specifically demethylates Chl catabolites at the level of FCCs in the cytosol.
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Different mechanisms are responsible for chlorophyll dephytylation during fruit ripening and leaf senescence in tomato

TL;DR: It is concluded that PPH is the core phytol-hydrolytic enzyme during leaf senescence in different plant species; however, fruit ripening involves other hydrolases, which are active in parallel to PPH or are the core hydrolase in fruits.