Journal
BIOCHEMICAL SOCIETY TRANSACTIONS
Volume 37, Issue -, Pages 387-391Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BST0370387
Keywords
chlorophyllide; conformational change; Fourier-transform infrared (FTIR); hydride; protochlorophyllide oxidoreductase (POR)
Categories
Funding
- Netherlands Organisation for Scientific Research through the Dutch Foundation for Earth and Life Sciences [834.01.002, 831.00.004]
- Biotechnology and Biological Sciences Research Council [BB/D015413/1]
- Biotechnology and Biological Sciences Research Council [BB/D015413/1] Funding Source: researchfish
- BBSRC [BB/D015413/1] Funding Source: UKRI
Ask authors/readers for more resources
The enzyme POR (protochlorophyllide oxidoreductase), from the family of alcohol dehydrogenases, reduces protochlorophyllide into chlorophyllide on the absorption of light. The reduction involves the transfer of two protons and two electrons and is an important regulatory step in the biosynthesis of chlorophyll. in recent years, due to the availability of large quantities of the pure enzyme, much of the catalytic reaction has been unravelled by using a variety of spectroscopic methods, including ultrafast initial events in catalysis. in addition, it has been demonstrated that a light-activated conformational change of the protein is necessary to activate catalysis. This makes POR a very important model system to study the relationship between structural changes of enzymes and functionality.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available