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• W2169659823 abstract "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." @default.
• W2169659823 created "2016-06-24" @default.
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• W2169659823 date "2004-03-23" @default.
• W2169659823 modified "2023-09-30" @default.
• W2169659823 title "Protein kinetics: Structures of intermediates and reaction mechanism from time-resolved x-ray data" @default.
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• W2169659823 doi "https://doi.org/10.1073/pnas.0305983101" @default.
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