Ultrafast enzymatic reaction dynamics in protochlorophyllide oxidoreductase.
The reaction catalyzed by the light-driven enzyme protochlorophyllide oxidoreductase (POR) has been initiated with a 50-fs laser pulse. We show that the catalytic mechanism, involving proton and hydride transfers, proceeds with time constants of 3 ps and 400 ps. It is known that catalysis by POR involves thermally excited protein dynamics; our results show that these molecular motions occur on an ultrafast timescale.
Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield S10 2TN, UK.
Derren J
DJ
Heyes
C Neil
CN
Hunter
Ivo H M
IH
van Stokkum
Rienk
R
van Grondelle
Marie Louise
ML
Groot
D002384:Catalysis / Q000528:radiation effects; D000458:Cyanobacteria / Q000201:enzymology; D007700:Kinetics; D007834:Lasers; D009249:NADP / Q000378:metabolism; D010088:Oxidoreductases / Q000737:chemistry* / Q000378:metabolism*; D044925:Oxidoreductases Acting on CH-CH Group Donors; D011521:Protochlorophyllide / Q000737:chemistry / Q000378:metabolism; D013057:Spectrum Analysis / Q000379:methods; D013997:Time Factors
D011521:Protochlorophyllide; D009249:NADP; D010088:Oxidoreductases; D044925:Oxidoreductases Acting on CH-CH Group Donors; C023886:protochlorophyllide reductase