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A Samuni

Publications and source records attributed to A Samuni.

49 records · Page 3Linked to original sources
PubMed1979

Dynamics of pH-induced spectral changes in bacteriorhodopsin.

The kinetics of the spectral shift induced in bacteriorhodopsin by low pH are investigated by using the rapid-mixing, stopped-flow technique. The generation of the acid form of the chromophore (A605) occurs in two distinct steps: a fast process (t1/2I = 21 +/- 4 ms) is followed by a much slower reaction (t1/2II = 6 +/- 2 s). The observations are interpreted in terms of neutralization of an acid group in the neighborhood of the retinyl chromophore, the double-staged kinetics being attributed to cooperative effects between chromophores. The method may serve as a tool for studying the kinetics of proton migration across the purple membrane.

Bacteriorhodopsins↗
PubMed1978

Quaternary states of methemoglobin and its valence-hybrid. A pulse radiolysis study.

Using the pulse radiolysis technique on solutions of stripped adult human methemoglobin, we found that the heme-iron within a single subunit in the tetramer was reduced to iron(II). The valence-hybrid thus formed was reacted with oxygen and with carbon monoxide. Kinetics of the reactions were studied. The effects of pH, inositol hexaphosphate, and temperature on these reactions were examined. The kinetics of the ligation of O2 and CO were used to characterize the affinity states of the valence-hybrid and its parent methemoglobin. Our results support the description of stripped methemoglobin A as residing in an R state. In the presence of inositol hexaphosphate methemoglobin is stabilized in a T state, but it switches into a high affinity state when the pH is raised a0ove 8.0. This structural transition was not found to coincide with the switch of spin state of the heme-iron that accompanies the ionization of water in aquomethemoglobin A.

Adult↗
PubMed1976

Acquisition of substrate-specific parameters during the catalytic reaction of penicillinase.

The progress of the catalytic reaction of penicillinase (EC 3.5.2.6; penicillin amido-beta-lactamhydrolase) depends on the structure of the side-chain in derivatives of 6-aminopenicillanic acid (the parent substrate). Side-chains of one class promote the rate of the reaction and cause no deviation from the linear kinetics observed with the parent compound. By contrast, side-chains of the other class induce a time-dependent, reversible change in the parameters of the catalytic reaction. The rate decelerates considerably and then becomes constant; the decrease in kcat is accompanied by a corresponding decrease in Km. The initial parameters of the biphasic reaction, determined by stopped-flow spectrophotometry, approach those of the unsubstituted 6-aminopenicillanic acid. The final parameters, which are specific for each derivative, are not acquired when the native conformation of the enzyme is stabilized by homologous antibodies.

Antibodies↗
PubMedDate not supplied

Inhibition of Plasmodium falciparum growth by a synthetic iron chelator.

The susceptibility of the chloroquine-resistant malaria parasite Plasmodium falciparum (FCR-3) to a pyridoxal-based iron chelator was tested. 10 microM of the chelator 1[N-ethoxycarbonylmethyl-pyridoxy-lidenium]-2-[2'-pyri dyl] hydrazine bromide (code name L2-9) effectively inhibited growth in vitro of the parasites. Presaturation of the chelator with either ferric or ferrous iron partially blocked the inhibitory effect. Two hours' exposure of parasites to 20 microM L2-9 was sufficient to inhibit their growth irreversibly. Desferrioxamine blocked the inhibitory effect of L2-9. It is suggested that the chelator may be acting by generating free radicals in complexing intracellular iron.

Animals↗