Binding of Fe3+ ions to halobacterial purple membranes as studied by Mössbauer spectroscopy.

Purple membranes (PM) from Halobacterium were reconstituted with 57Fe ions and investigated by Mössbauer spectroscopy within the temperature range from 5 to 300 K at the Fe/bacteriorhodopsin (BR) ratio 0.6-300. When the Fe/Br ratio was below 2, Fe3+ bonded to PM mostly as hydroxymonomeric particle [FeOH]2+.

An investigation of the electrochemical cycle of bacteriorhodopsin analogs with the modified ring.

5,6-Epoxy-, 4-methoxy-, 4-hydroxy-, and 3,4-dehydrobacteriorhodopsins can generate delta psi coupled to a photochemical cycle with intermediate M. The kinetics of delta psi comprises three main electrogenic phases: the fast small negative, the microsecond, and the millisecond positive phases. The photocycle efficiency is lower in all the analogs.

[Cloning of the gene for ribosomal protein HS4 in the archaebacterium Halobacterium halobium].

Using a synthetic oligonucleotide probe, a gene of the ribosomal protein HS4 from an archaebacterium Halobacterium halobium has been cloned and partly sequenced. The translation initiation region contains a sequence complementary to the 3' end of the 16S rRNA.

Purification and properties of serine protease from Halobacterium halobium.

Pure extracellular serine protease was isolated from the culture filtrate of Halobacterium halobium by bacitracin-Sepharose affinity chromatography. The enzyme activity was completely and irreversibly lost if the NaCl concentration fell below 2 M. The protease consists of one polypeptide chain with a molecular weight of 41,000.