title: Ultrafast catalytic processes and conformational changes in the light-driven enzyme protochlorophyllide oxidoreductase (POR).
abstract: 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.affiliation: Department of Physics and Astronomy, Faculty of Sciences, Vrije Universiteit, Amsterdam, The Netherlands.
authors.forename: Olga A
authors.initials: OA
authors.lastname: Sytina
authors.forename: Derren J
authors.initials: DJ
authors.lastname: Heyes
authors.forename: C Neil
authors.initials: CN
authors.lastname: Hunter
authors.forename: Marie Louise
authors.initials: ML
authors.lastname: Groot
mesh_terms: D002384:Catalysis / Q000528:radiation effects; D008027:Light; D008958:Models, Molecular; D044925:Oxidoreductases Acting on CH-CH Group Donors / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation / Q000528:radiation effects; D013997:Time Factors
chemical_list: D044925:Oxidoreductases Acting on CH-CH Group Donors; C023886:protochlorophyllide reductase