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Science 8 October 1999:
Vol. 286. no. 5438, pp. 252 - 253
DOI: 10.1126/science.286.5438.252

Perspectives

STRUCTURAL BIOCHEMISTRY:
Proton Pump Caught in the Act

Robert B. Gennis and Thomas G. Ebrey

How does a protein pump protons in only one direction? In his Perspective, Gennis explains how this occurs in bacteriorhodopsin, a membrane protein that pumps protons in response to light stimulation. A new structure by Luecke et al. on p. 255 shows that small changes in the conformation within bacteriorhodopson induced as a result of light absorption by retinal, are sufficient to change the pKa's of several key residues enough to promote the release of protons on one side of the membrane.


R. B. Gennis is in the Department of Biochemistry, University of Illinois, Urbana, IL 61801, USA. E-mail: r-gennis{at}uiuc.edu. T. G. Ebrey is in the Departments of Cell and Structural Biology, and Biochemistry, University of Illinois, Urbana, IL 61801, USA. E-mail: t-ebrey{at}uiuc.edu

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Crystallographic Study of Hydration of an Internal Cavity in Engineered Proteins with Buried Polar or Ionizable Groups.
J. L. Schlessman, C. Abe, A. Gittis, D. A. Karp, M. A. Dolan, and B. Garcia-Moreno E. (2008)
Biophys. J. 94, 3208-3216
   Abstract »    Full Text »    PDF »
The Iron-Sulfur Cluster of the Rieske Iron-Sulfur Protein Functions as a Proton-exiting Gate in the Cytochrome bc1 Complex.
B. Gurung, L. Yu, D. Xia, and C.-A. Yu (2005)
J. Biol. Chem. 280, 24895-24902
   Abstract »    Full Text »    PDF »



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Science. ISSN 0036-8075 (print), 1095-9203 (online)