Synthesis and Characterization of the cis- and trans-Trimethylsilylcyclohexanols¹

Abstract

CHARACTERIZATION OF TRIMETHPLSILYLCYCLOHEXANOLS2483 exo-7-Acetoxy 1,6-dimethylbicyclo [4.1 .O]heptane.'8--To a solution of 5.0 g (29.8 mmoles) of exo acid, mp 137-139', in 100mlof anhydrous ether, was added with stirring 160 ml of a solution of methyllithium in ether containing 59.6 mmoles of total base as l?termined by titration. After 5 min the reaction mixture was worked up, yielding 1.75 g of recovered starting material, mp 136-139", and 3.34 g of neutral product. The small amount of less volatile tertiary alcohol (2.87 p ) cont,aminating the product was removed by distillation through a spinning-band column at oil pump pressure which gavc 2.08 g of ketone (65% based on unrecovered acid): bp 29-30' (0.2 mm); 5.92 p ;210 mp ( E 6800); I (CC1.t) 7.89 (3 H) and 8.80 (6 H).To a slurry of 2.00 g (12.0 mmoles) of ketone and t 6 g of dibasic sodium phosphate in 80 ml of methylene chloride was added, with stirring, a solut,ion of peroxytrifluoroacetic acid prepared by adding, with stirring, 1.0 ml (37 mmoles) of 90% hydrogen peroxide and 6.2 ml (44 mmoles) of trifluoroacetic anhydride to 15 ml of ice-cooled methylene chloride. Work-up gave 1.50 g of crude product which was first subjected to shortpath dist,illation (oil bath 105-140") and then preparative gc. Material corresponding to the major peak (85%) at 6.7 rnin was collected: A tz 5.73 p ; I (CClr) 6.42 (1 H) 8.00 (3 H), 9.03 ( 6 H). A n d . Calcd for CI1HlnO2: C, 72.53; H, 9.89. Found: C, 72.76; H, 10.07.Conversion of the cyclopropyl acetate to cyclopropanol was effected by using freshly dist,illed solvents for each run (including work lip). Typically, a solution of 37 mg of acetate in a mixture of 2.5 ml of methanol and 1.5 ml of 0.3 N sodium hydroxide sohition was allowed to st and at room temperature for 50 miri under nitrogen. Water (10 ml) was then added and the mixture was extracted with three 3-ml portions of pentane. The combined extracts were washed with 2 ml of water and then dried over sodinm snlfate. Evaporation of solvent left a white solid showing hydroxylir (2.8 and 2.9 p ) but no carbonyl absorp tion; 7 (CDCI,) 6.93 (1 H), 8.07 ( 1 H), 8.95 (1 HI singlet superimposed on complex absorption).The white solid from one run was treated with excess acetic anhydride in pyridine. Work-up, nsing carbon tetrachloride as solvent, gave a solution showing the same nmr absorption as (18) General procsedures: G. Tegner, Acta Chem. S c a d . , 6, 782 (1952); K, D. Emmons and G. 13. Lneas, J. Am. Chem. Sac., 77, 2287 (1955); C. H. DePuy and L. R. Slahoney, {bid., 86, 2653 (1964).starting acetate. Capillary gc of the concentrated solution showed, apart from solvent, only one peak with a retention time corresponding to that of starting acet,ate. endo-7-Acetoxy-l,6-dimethylbicyclo[4.1 .O] heptane was similarly prepared18 from endo acid, mp 120-122"; 1.450 g of the acid yielding 0.800 g of crude ketone which showed only weak hydroxyl absorption in the infrared spectrum. A portion (580 mg) of this crude ketone was subjected to Baeyer-Villiger oxidation, giving 549 mg...

A thermodynamic analysis of the interaction between the mitochondrial coupling adenosine triphosphatase and its naturally occurring inhibitor protein

“…The mitochondrial ATPase was isolated by the method of Knowles & Penefsky (1972a). Submitochondrial particles (A particles) were prepared by sonication of mitochondria in the presence of EDTA and NH3 (Fessenden & Racker, 1966). Inhibitor-depleted particles (AS particles) were prepared by gel filtration of A particles at high ionic strength (Horstman & Racker, 1970); refiltration of these particles gave no further increase in ATPase activity.…”

Antibodies to the F1‐ATPase of Rhodospirillum rubrum and Its Purified Native β‐Subunit:

“…Antibodies were successfully prepared against the holo F1-ATPase of beef heart mitochondria [4,5], higher plant chloroplasts Escherichia coli [9,10], Rhodopseudoomonas c.upsu/um [ I l l , R. rubrum [12,13] and other bacteria [14,15]. In R. rubrum, Berzborn et al [I21 have shown that antisera prepared against the native RrFl agglutinated the chromatophore membrane, whereas antisera prepared against denatured RrFl had no effect.…”

“…Antibodies were successfully prepared against the holo F1-ATPase of beef heart mitochondria [4,5], higher plant chloroplasts Escherichia coli [9,10],Rhodopseudoomonas c.upsu/um [ I l l ,R. rubrum [12,13] and other bacteria [14,15].…”

Translocations Through Natural Membranes

“…When F1 was detached, the ATPase activity woul depend upon the replacement of X-I by HzO. The propose system will explain (77) the fact that oligomycin stimulates oxidativ phosphorylation and reversed electron transfer under certain cond tions (234)(235)(236).…”