Publication Abstract from PubMed
We determine the number of authentic reaction intermediates in the later stages of the photocycle of photoactive yellow protein at room temperature, their atomic structures, and a consistent set of chemical kinetic mechanisms, by analysis of a set of time-dependent difference electron density maps spanning the time range from 5 micros to 100 ms. The successful fit of exponentials to right singular vectors derived from a singular value decomposition of the difference maps demonstrates that a chemical kinetic mechanism holds and that structurally distinct intermediates exist. We identify two time-independent difference maps, from which we refine the structures of the corresponding intermediates. We thus demonstrate how structures associated with intermediate states can be extracted from the experimental, time-dependent crystallographic data. Stoichiometric and structural constraints allow the exclusion of one kinetic mechanism proposed for the photocycle but retain other plausible candidate kinetic mechanisms.
Protein kinetics: structures of intermediates and reaction mechanism from time-resolved x-ray data.,Schmidt M, Pahl R, Srajer V, Anderson S, Ren Z, Ihee H, Rajagopal S, Moffat K Proc Natl Acad Sci U S A. 2004 Apr 6;101(14):4799-804. Epub 2004 Mar 23. PMID:15041745[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
