Noncontact dipole effects on channel permeation. III. Anomalous proton conductance effects in gramicidin

Proton transport on water wires, of interest for many problems in membrane biology, is analyzed in side-chain analogs of gramicidin A channels. In symmetrical 0.1 N HCl solutions, fluorination of channel Trp(11), Trp-(13), or Trp(15) side chains is found to inhibit proton transport, and replacement of one or more Trps with Phe enhances proton transport, the opposite of the effects on K(+) transport in lecithin bilayers. The current-voltage relations are superlinear, indicating that some membrane field-dependent process is rate limiting. The interfacial dipole effects are usually assumed to affect the rate of cation translocation across the channel. For proton conductance, however, water reorientation after proton translocation is anticipated to be rate limiting. We propose that the findings reported here are most readily interpreted as the result of dipole-dipole interactions between channel waters and polar side chains or lipid headgroups. In particular, if reorientation of the water column begins with the water nearest the channel exit, this hypothesis explains the negative impact of fluorination and the positive impact of headgroup dipole on proton conductance.     

Purification and characterization of macromomycin-I,a protein antibiotic containing a non-protein chromophore

One-step chromatography of crude macromomycin on DEAE-Sephacel yielded two forms of the antibiotic. The more active form of the drug contained a non-protein chromophore. Apoprotein and chromophore components of this drug form were separated. The apoprotein was found to be inactive and the chromophore only slightly active against $\text{Sarcina}\text{lutea}$, while recombination of both components resulted in a partial recovery of the activity. In contrast, recombination of chromophore and apoprotein did not restore the ability of intact macromomycin to nick isolated DNA.