A novel penicillin-binding protein, PBP-2' (Mr about 75,000), is known to be induced in excessively large amount by most beta-lactam compounds in cells of a clinically isolated strain of Staphylococcus aureus, TK784, that is highly resistant to beta-lactams and also most other antibiotics. This protein has very low affinities to most beta-lactam compounds and has been supposed to be the cause of the resistance of the cells to beta-lactams. A 14-kilobase DNA fragment was isolated from the cells that carried the gene encoding this penicillin-binding protein and also a genetically linked marker that is responsible for the resistance to tobramycin. This DNA was cloned on plasmid pACYC184 and was shown to cause both production of PBP-2' and resistance to tobramycin in Escherichia coli cells. However, the formation of PBP-2' in E. coli was only moderate and was independent of normal inducer beta-lactams. The PBP-2' formed in the E. coli cells showed slow kinetics of binding to beta-lactams similar to that of PBP-2' formed in the original S. aureus cells and gave a similar pattern of peptides to the latter when digested with the proteolytic V8 enzyme of S. aureus.

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The acidification of aqueous solutions containing Na2MoO4·2H2O in the presence of a chiral lysine ligand (d- and l-form) gives octamolybdates coordinating two lysine ligands, Na2[Mo8O26(d-lysH2)2]·8H2O (Mo8-d) and Na2[Mo8O26(l-lysH2)2]·8H2O (Mo8-l) (where lysH2 is 2,6-diammoniohexanoato), respectively. These two compounds crystallize with triclinic symmetry in the space group P1, the cell parameters being a = 10.782(2), b = 11.241(5), c = 10.027(2) Å, α = 93.21(2), β = 102.86(2), γ = 112.98(2)°, V = 1077(1) Å3, and Z = 1 for the Mo8-d, and a = 10.783(4), b = 11.246(3), c = 10.019(4) Å, α = 93.21(3), β = 102.75(3), γ = 112.98(2)°, V = 1077(2) Å3, and Z = 1 for Mo8-l. The X-ray crystal structures of these two species have been solved by the MITHRIL direct method and refined to R = 0.0337 and 0.0312 for Mo8-d and -l, respectively. The chiral lysine ligands are coordinated via their carboxylate-oxygen atoms at the vacant sites on the two five-coordinate molybdenum for the centrosymmetric γ-[Mo8O26]4− anion to retain their configuration with a resultant formation of optically-active octamolybdate species.

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