Conformational changes in an ultrafast light-driven enzyme determine catalytic activity

• Published in: Nature (London) Vol. 456; no. 7224; pp. 1001 - 1004
• Main Authors: Sytina, Olga A, van Stokkum, Ivo H. M, Alexandre, Maxime T, Groot, Marie Louise, Hunter, C. Neil, Heyes, Derren J, van Grondelle, Rienk
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 18.12.2008; Nature Publishing Group
• Subjects: Analytical, structural and metabolic biochemistry; Biocatalysis - radiation effects; Biological and medical sciences; Catalysis; Catalytic Domain - radiation effects; Changes; Enzymes; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; Humanities and Social Sciences; letter; Light; Models, Molecular; multidisciplinary; Oxidoreductases; Oxidoreductases Acting on CH-CH Group Donors - chemistry; Oxidoreductases Acting on CH-CH Group Donors - metabolism; Oxidoreductases Acting on CH-CH Group Donors - radiation effects; Protein Conformation - radiation effects; Protons; Science; Science (multidisciplinary); Structure-Activity Relationship; Synechocystis - enzymology; Time Factors; United States; Chlorophyll; Protochlorophyllide reductase; Enzyme; Light; Biosynthesis; Oxidoreductases; Catalyst activity; Conformation

The role of conformational changes in explaining the huge catalytic power of enzymes is currently one of the most challenging questions in biology. Although it is now widely regarded that enzymes modulate reaction rates by means of short- and long-range protein motions, it is almost impossible to di...