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Wiley, Angewandte Chemie, 32(127), p. 9435-9439

DOI: 10.1002/ange.201503672

Wiley, Angewandte Chemie International Edition, 32(54), p. 9303-9307

DOI: 10.1002/anie.201503672

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Complete Proton Transfer Cycle in GFP and Its T203V and S205V Mutants**

Journal article published in 2015 by Sergey P. Laptenok ORCID, Laptenok Sp, Andras Lukacs, Agnieszka Gil, Richard Brust, Sazanovich Iv, Igor V. Sazanovich, Greetham Gm, Gregory M. Greetham, Peter J. Tonge ORCID, Tonge Pj, Stephen R. Meech, Meech Sr
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

Proton transfer is critical in many important biochemical reactions. The unique three-step excited-state proton transfer in avGFP allows observations of protein proton transport in real-time. In this work we exploit femtosecond to microsecond transient IR spectroscopy to record, in D2O, the complete proton transfer photocycle of avGFP, and two mutants (T203V and S205V) which modify the structure of the proton wire. Striking differences and similarities are observed among the three mutants yielding novel information on proton transfer mechanism, rates, isotope effects, H-bond strength and proton wire stability. These data provide a detailed picture of the dynamics of long-range proton transfer in a protein against which calculations may be compared.