Benz

Bochner

Bredin

Galleni

H. Nikaido

Hajjar

Hall

Harder

James

Jaurin

Nikaido

Novick

Okusu

Pages

S. Kojima

Schnaitman

Simonet

Smit

Sulavik

Takatsuka

Vidal

Yoshimura

Zimmermann

English

Significance
          Porin channels in the outer membrane of Gram-negative bacteria were originally thought to be nonspecific channels that discriminate among solutes only by their gross physicochemical properties, such as size, hydrophobicity, and charge. Since the discovery of the ampicillin-binding site inside one porin channel, however, such “specific” interactions are hypothesized to play significant roles especially for the permeation of drugs. We show, by the careful examination of influx and efflux of ampicillin and benzylpenicillin, that the original nonspecific model is still valid and that it is misleading to overemphasize the role of specific binding sites.</jats:p

Seiji Kojima

Hiroshi Nikaido

Crossref

Proceedings of the National Academy of Sciences

Permeation rates of penicillins indicate that
            <i>Escherichia coli</i>
            porins function principally as nonspecific channels

http://www.pnas.org/content/110/28/E2629.full.pdf

Permeation rates of penicillins indicate that Escherichia coli porins function principally as nonspecific channels

Permeation rates of penicillins indicate that Escherichia coli porins function principally as nonspecific channels

Abstract

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