Context. Hydrogenation reactions of CO in inter-and circumstellar ices are regarded as an important starting point in the formation of more complex species. Previous laboratory measurements by two groups of the hydrogenation of CO ices provided controversial results about the formation rate of methanol. Aims. Our aim is to resolve this controversy by an independent investigation of the reaction scheme for a range of H-atom fluxes and different ice temperatures and thicknesses. To fully understand the laboratory data, the results are interpreted theoretically by means of continuous-time, random-walk Monte Carlo simulations. Methods. Reaction rates are determined by using a state-of-the-art ultra high vacuum experimental setup to bombard an interstellar CO ice analog with H atoms at room temperature. The reaction of CO + H into H 2 CO and subsequently CH 3 OH is monitored by a Fourier transform infrared spectrometer in a reflection absorption mode. In addition, after each completed measurement, a temperature programmed desorption experiment is performed to identify the produced species according to their mass spectra and to determine their abundance. Different H-atom fluxes, morphologies, and ice thicknesses are tested. The experimental results are interpreted using Monte Carlo simulations. This technique takes into account the layered structure of CO ice. Results. The formation of both formaldehyde and methanol via CO hydrogenation is confirmed at low temperature (T = 12−20 K). We confirm that the discrepancy between the two Japanese studies is caused mainly by a difference in the applied hydrogen atom flux, as proposed by Hidaka and coworkers. The production rate of formaldehyde is found to decrease and the penetration column to increase with temperature. Temperature-dependent reaction barriers and diffusion rates are inferred using a Monte Carlo physical chemical model. The model is extended to interstellar conditions to compare with observational H 2 CO/CH 3 OH data.

Defects in the conversion of androstenedione to testosterone in the fetal testes by the enzyme 17 beta-hydroxysteroid dehydrogenase (17 beta-HSD) give rise to genetic males with female external genitalia. We have used expression cloning to isolate cDNAs encoding a microsomal 17 beta-HSD type 3 isozyme that shares 23% sequence identity with other 17 beta-HSD enzymes, uses NADPh as a cofactor, and is expressed predominantly in the testes. The 17 beta HSD3 gene on chromosome 9q22 contains 11 exons. Four substitution and two splice junction mutations were identified in the 17 beta HSD3 genes of five unrelated male pseudohermaphrodites. The substitution mutations severely compromised the activity of the 17 beta-HSD type 3 isozyme.

The conversion of testosterone into dihydrotestosterone by steroid 5 alpha-reductase is a key reaction in androgen action, and is essential both for the formation of the male phenotype during embryogenesis and for androgen-mediated growth of tissues such as the prostate. Single gene defects that impair this conversion lead to pseudohermaphroditism in which 46X,Y males have male internal urogenital tracts, but female external genitalia. We have described the isolation of a human 5 alpha-reductase complementary DNA from prostate. Subsequent cloning and genetic studies showed that this gene (designated 5 alpha-reductase 1) was normal in patients with 5 alpha-reductase deficiency. We report here the isolation of a second 5 alpha-reductase cDNA by expression cloning and the polymerase chain reaction. The biochemical and pharmacological properties of this cDNA-encoded enzyme (designated 5 alpha-reductase 2) are consistent with it being the major isozyme in genital tissue. A deletion in this gene is present in two related individuals with male pseudohermaphroditism caused by 5 alpha-reductase deficiency. These results verify the existence of at least two 5 alpha-reductases in man and provide insight into a fundamental hormone-mediated event in male sexual differentiation.

A detailed kinetic analysis of the complex reaction systems arising from the ozonolysis of C2H4 and (CH3)2CC(CH3)2 (TME), respectively, is carried out, using master equations and statistical rate theory. The thermochemical as well as the molecular data required are obtained from CCSD(T)/TZ2P and B3LYP/DZP calculations. It is shown that the primary ozonides are not collisionally stabilized under atmospheric conditions. In the reaction sequence for O3 + TME, the same is true for CH2C(CH3)OOH formed from (CH3)2COO, which completely dissociates to give OH radicals. However, in this system, a pressure dependence is predicted for the relative branching fractions of the reactions of the Criegee intermediate. Under atmospheric conditions, for both examples, the product yields obtained are in reasonable agreement with experimental results.

␤-Carotene 15,15-monooxygenase (BCO), formerly known as ␤-carotene 15,15-dioxygenase, catalyzes the first step in the synthesis of vitamin A from dietary carotenoids. We have biochemically and enzymologically characterized the purified recombinant human BCO enzyme. A highly active BCO enzyme was expressed and purified to homogeneity from baculovirusinfected Spodoptera frugiperda 9 insect cells. The K m and V max of the enzyme for ␤-carotene were 7 M and 10 nmol retinal/mg ؋ min, respectively, values that corresponded to a turnover number (k cat ) of 0.66 min ؊1 and a catalytic efficiency (k cat /K m ) of ϳ10 M ؊1 ⅐min؊1 . The enzyme existed as a tetramer in solution, and substrate specificity analyses suggested that at least one unsubstituted ␤-ionone ring half-site was imperative for efficient cleavage of the carbon 15,15-double bond in carotenoid substrates. High levels of BCO mRNA were observed along the whole intestinal tract, in the liver, and in the kidney, whereas lower levels were present in the prostate, testis, ovary, and skeletal muscle. The current data suggest that the human BCO enzyme may, in addition to its well established role in the digestive system, also play a role in peripheral vitamin A synthesis from plasma-borne provitamin A carotenoids.