Organomercurial-volatilizing bacteria in the mercury-polluted sediment of Minamata Bay, Japan.

A total of 4,604 bacterial strains isolated from the sediments of Minamata Bay and nearby low-level-mercury stations (control stations) were screened for the ability to volatilize mercury from inorganic and organic mercurial compounds. The strains that volatilize mercury from several kinds of organomercurials were found only in the sediments of Minamata Bay.     

Ribosomal resistance of an istamycin producer, Streptomycestenjimariensis, to aminoglycoside antibiotics

$\text{Streptomyces}\text{tenjimariensis}$ SS-939 was resistant to its own aminoglycoside antibiotics, istamycins, as well as kanamycin A, neamine, ribostamycin and butirosin A, but was susceptible to neomycin B, lividomycin A and streptomycin. This resistance to these antibiotics was found to be due to ribosomes of the strain.     

Spectroscopic demonstration of an initial stage of the complex of D-amino acid oxidase and its substrate D-alpha-aminobutyric acid

D-Amino acid oxidase [D-amino acid: O₂ oxidoreductase (deaminating), EC 1.4.3.3] was anaerobically mixed with its substrate D-α-aminobutyric acid at ?10°C and pa_H¹ 7 which were apart from their maxima for the enzymatic reaction. By an ordinary self-recording spectrophotometer, the absorption spectrum of an initial stage of the complex could be observed. The spectrum was in principle similar to that of the complex of this enzyme with benzoate, the enzyme-substrate complex model. The spectroscopic observation revealed that this species is in an equilibrium with the purple intermediate, a strong charge transfer complex between the enzyme and its substrate neutral D-amino acid.     

Interaction of steroids with D-amino acid oxidase.

1. Progesterone inhibited D-amino acid oxidase (D-amino acid : O2 oxidoreductase (deaminating), EC 1.4.3.3) in competition with its substrate, D-alanine. Binding of progesterone brought about the increase in both fluorescence intensity and fluorescence polarization of FAD, which indicates that the environment surrounding FAD chromophore is modified due to a conformational change in the apoenzyme. 2. Ethinyl estradiol, testosterone, testosterone propionate, corticosterone and aldosterone also inhibited the enzyme slightly in the same manner. Their binding also produced a slight increase in FAD fluorescence without decreasing the fluorescence polarization. 3. Cholesterol did not inhibit the enzyme, though it increased the fluorescence polarization of FAD. This indicates the binding of cholesterol with the enzyme at a site other than the substrate binding site.     

Adenylate regulation of photosynthetic electron transport and the coupling sites of phosphorylation in spinach chloroplasts

The regulation by adenylates of activities of various partial electron transport systems in spinach chloroplasts was studied using systems from H₂O to 2,5-dimethyl-p-benzoquinone, H₂O to 2,6-dichlorophenolindophenol, reduced 2,6-dichlorophenolindophenol to methyl viologen, and H₂O to methyl viologen or ferricyanide. Adenylates regulated all of them. The ratio of the amount of esterified Pi (P) to that of electrons transported (e) in coupling with phosphorylation manifested that there are two phosphorylation sites: one between H₂O and 2,5-dimethyl-p-benzoquinone or 2,6-dichlorophenolindophenol and another between reduced 2,6-dichlorophenolindophenol and methyl viologen, under the proposed stoichiometries,i.e., P/H⁺=0.5 and H⁺/e=1, where H⁺ is the amount of protons pumped by electron transport (= those translocated during phosphorylation), when the basal electron transport (the part not regulated by adenylates) was excluded. The effects of pH, phlorizin, and methylamine on the adenylate regulation of electron transport, and the stimulation profile of electron transport coupled with quasiarsenylation suggested no distinction between the two phosphorylation sites.     

High mutagenicity and toxicity of a diol epoxide derived from benzo[a]pyrene

(±)-7β,8α-Dihydroxy-9β,10β-epoxy-7,8,9,10-tetrahydrobenzo[a]pyrene (BP 7,8-diol-9,10-epoxide) is a suspected metabolite of benzo[a]pyrene that is highly mutagenic and toxic in several strains of $\text{Salmonella}\text{typhimurium}$ and in cultured Chinese hamster V79 cells. BP 7,8-diol-9,10-epoxide was approximately 5, 10 and 40 times more mutagenic than benzo[a]pyrene 4,5-oxide (BP 4,5-oxide) in strains TA 98 and TA 100 of $\text{S.}\text{typhimurium}$ and in V79 cells, respectively. Both compounds were equally mutagenic to strain TA 1538 and non-mutagenic to strain TA 1535 of $\text{S.}\text{typhimurium}$. The diol epoxide was toxic to the four bacterial strains at 0.5–2.0 nmole/plate, whereas BP 4,5-oxide was nontoxic at these concentrations. In V79 cells, the diol epoxide was about 60-fold more cytotoxic than BP 4,5-oxide.     

Enhancement factor for oxygen absorption into fermentation broth

Values of the enhancement factor for oxygen absorption into fermentation broth, i.e., the ratio of the liquid phase mass transfer coefficients for oxygen absorption for both cases with and without respiration of microorganisms were predicted theoretically on the assumption of various cell concentration distributions. Calculations indicate that in the usual case the enhancement factor is only slightly or negligibly larger than unity, even when accumulation of microorganisms at or near the gas-liquid interface is assumed. Results of experiments with sparged-stirred fermentors on oxygen absorption into fermentation broths containing resting and growing cells of Candida tropicalis confirmed the theoretical prediction. Except for extreme cases, the effect of respiration of microorganisms on k_La, values can practically be ignored.     

Properties of purified hydrogenase from the particulate fraction of Desulfovibrio vulgaris, Miyazaki.

The properties of purified hydrogenase [EC 1.12.2.1] solubilized from particulate fraction of sonicated Desulfovibrio vulgaris cells are described. The enzyme was a brownish iron-sulfur protein of molecular weight 89,000, composed of two different subunits (mol. wt.: 28,000 and 59,000), and it contained 7-9 iron atoms and 7-8 labile sulfide ions. Molybdenum was not detected in the preparation. The absorption spectrum of the enzyme was characteristic of iron-sulfur proteins. The millimolar absorbance coefficients of the enzyme were about 164 at 280nm, and 47 at 400nm. The absorption spectrum of the enzyme in the visible region changed upon incubating the enzyme under H2 in the presence of cytochrome c3, but not in its absence. This spectral change was due to the reduction of the enzyme. The absorbance ratio at 400nm of the reduced and the oxidized forms of the enzyme was 0.66. The activity of the enzyme was hardly affected by metal-complexing agents such as cyanide, azide, 1,10-phenanthroline, etc., except for CO, which was a strong inhibitor of the enzyme. The activity was inhibited by SH-reagents such as p-chloromercuribenzenesulfonate. The enzyme was significantly resistant to urea, but susceptible to sodium dodecyl sulfate. These properties were very similar to those of clostridial hydrogenase [EC 1.12.7.1], in spite of differences in the acceptor specificity and subunit structure.