Breakdown of the isobaric multiplet mass equation for the A = 20 and 21 multiplets.

Using the Penning trap mass spectrometer TITAN, we performed the first direct mass measurements of (20,21)Mg, isotopes that are the most proton-rich members of the A = 20 and A = 21 isospin multiplets. These measurements were possible through the use of a unique ion-guide laser ion source, a development that suppressed isobaric contamination by 6 orders of magnitude. Compared to the latest atomic mass evaluation, we find that the mass of (21)Mg is in good agreement but that the mass of (20)Mg deviates by 3 σ. These measurements reduce the uncertainties in the masses of (20,21)Mg by 15 and 22 times, respectively, resulting in a significant departure from the expected behavior of the isobaric multiplet mass equation in both the A = 20 and A = 21 multiplets. This presents a challenge to shell model calculations using either the isospin nonconserving universal sd USDA and USDB Hamiltonians or isospin nonconserving interactions based on chiral two- and three-nucleon forces.

In-trap spectroscopy of charge-bred radioactive ions.

In this Letter, we introduce the concept of in-trap nuclear decay spectroscopy of highly charged radioactive ions and describe its successful application as a novel spectroscopic tool. This is demonstrated by a measurement of the decay properties of radioactive mass A=124 ions (here, ^{124}In and ^{124}Cs) in the electron-beam ion trap of the TITAN facility at TRIUMF. By subjecting the trapped ions to an intense electron beam, the ions are charge bred to high charge states (i.e., equivalent to the removal of N-shell electrons), and an increase of storage times to the level of minutes without significant ion losses is achieved. The present technique opens the venue for precision spectroscopy of low branching ratios and is being developed in the context of measuring electron-capture branching ratios needed for determining the nuclear ground-state properties of the intermediate odd-odd nuclei in double-beta (ßß) decay.

New precision mass measurements of neutron-rich calcium and potassium isotopes and three-nucleon forces.

We present precision Penning trap mass measurements of neutron-rich calcium and potassium isotopes in the vicinity of neutron number N=32. Using the TITAN system, the mass of 51K was measured for the first time, and the precision of the (51,52)Ca mass values were improved significantly. The new mass values show a dramatic increase of the binding energy compared to those reported in the atomic mass evaluation. In particular, 52Ca is more bound by 1.74 MeV, and the behavior with neutron number deviates substantially from the tabulated values. An increased binding was predicted recently based on calculations that include three-nucleon (3N) forces. We present a comparison to improved calculations, which agree remarkably with the evolution of masses with neutron number, making neutron-rich calcium isotopes an exciting region to probe 3N forces.

The on-line charge breeding program at TRIUMF's Ion Trap For Atomic and Nuclear Science for precision mass measurements.

TRIUMF's Ion Trap for Atomic and Nuclear science (TITAN) constitutes the only high precision mass measurement setup coupled to a rare isotope facility capable of increasing the charge state of short-lived nuclides prior to the actual mass determination in a Penning trap. Recent developments around TITAN's charge breeder, the electron beam ion trap, form the basis for several successful experiments on radioactive isotopes with half-lives as low as 65 ms and in charge states as high as 22+.

Local structure of isolated positively charged muonium as an analog for the hydrogen ion in p-type GaAs.

We determine the local structure of isolated positively charged muonium (Mu+) in heavily doped p-type GaAs based on muon level crossing resonance and zero applied field muon spin depolarization data. These measurements provide the first direct experimental confirmation that Mu+, and by analogy H+, is located within a stretched Ga-As bond. The distances between Mu+ and the nearest neighbor Ga and As atoms are estimated to be 1.83 +/- 0.10 A; and 1.76 +/- 0.10 A, respectively. These results are compared to existing theoretical calculations on the structure of hydrogen in GaAs and additionally provide data on the induced electric field gradients.

Structures and proton-pumping strategies of mitochondrial respiratory enzymes.

Enzymes of the mitochondrial respiratory chain serve as proton pumps, using the energy made available from electron transfer reactions to transport protons across the inner mitochondrial membrane and create an electrochemical gradient used for the production of ATP. The ATP synthase enzyme is reversible and can also serve as a proton pump by coupling ATP hydrolysis to proton translocation. Each of the respiratory enzymes uses a different strategy for performing proton pumping. In this work, the strategies are described and the structural bases for the action of these proteins are discussed in light of recent crystal structures of several respiratory enzymes. The mechanisms and efficiency of proton translocation are also analyzed in terms of the thermodynamics of the substrate transformations catalyzed by these enzymes.

Reaction of Escherichia coli cytochrome bo(3) and mitochondrial cytochrome bc(1) with a photoreleasable decylubiquinol.

In order to probe the reaction chemistry of respiratory quinol-oxidizing enzymes on a rapid time scale, a photoreleasable quinol substrate was synthesized by coupling decylubiquinol with the water-soluble protecting group 3',5'-bis(carboxymethoxy)benzoin (BCMB) through a carbonate linkage. The resulting compound, DQ-BCMB, was highly soluble in aqueous detergent solution, and showed no reactivity with quinol-oxidizing enzymes prior to photolysis. Upon photolysis in acetonitrile, 5, 7-bis(carboxymethoxy)-2-phenylbenzofuran, carbon dioxide, and decylubiquinol were formed. In aqueous media, free 3', 5'-bis(carboxymethoxy)benzoin was also produced. Photolysis of DQ-BCMB with a 308 nm excimer laser led to the release of the BCMB group in less than 10(-6) s. Decylubiquinol was released in the form of a carbonate monoester, which decarboxylated with an observed first-order rate constant of 195-990 s(-1), depending on the reaction medium. Yields of decylubiquinol as high as 35 microM per laser pulse were attained readily. In the presence of Escherichia coli cytochrome bo(3), photolysis of DQ-BCMB led to the oxidation of quinol by the enzyme with a rate that was limited by the rate of the decylubiquinol release. Mitochondrial cytochrome bc(1) reacted with photoreleased decylubiquinol with distinct kinetic phases corresponding to rapid b heme reduction and somewhat slower c heme reduction. Oxidation of photoreleased ubiquinol by this enzyme showed saturation kinetics with a K(m) of 3.6 microM and a k(cat) of 210 s(-1). The saturation behavior was a result of decylubiquinol being released as a carbonate monoester during the photolysis of DQ-BCMB and interacting with cytochrome bc(1) before decarboxylation of this intermediate yielded free decylubiquinol. The reaction of cytochrome bc(1) and photoreleased decylubiquinol in the presence of antimycin A led to monophasic b heme reduction, but also yielded slower quinol oxidation kinetics. The discrimination of kinetic phases in the reaction of cytochrome bc(1) with ubiquinol substrates has provided a means of exploring the bifurcation of electron transfer that is central to the operation of the Q-cycle in this enzyme.

Thermodynamics of electron transfer in Escherichia coli cytochrome bo3.

The proton translocation mechanism of the Escherichia coli cytochrome bo3 complex is intimately tied to the electron transfers within the enzyme. Herein we evaluate two models of proton translocation in this enzyme, a cytochrome c oxidase-type ion-pump and a Q-cycle mechanism, on the basis of the thermodynamics of electron transfer. We conclude that from a thermodynamic standpoint, a Q-cycle is the more favorable mechanism for proton translocation and is likely occurring in the enzyme.

Reaction of Escherichia coli cytochrome bo3 with substoichiometric ubiquinol-2: a freeze-quench electron paramagnetic resonance investigation.

The reaction of the quinol oxidase cytochrome bo3 from Escherichia coli with ubiquinol-2 (UQ2H2) was carried out using substoichiometric (0.5 equiv) amounts of substrate. Reactions were monitored through the use of freeze-quench EPR spectroscopy. Under 1 atm of argon, semiquinone was formed at the QB site of the enzyme with a formation rate constant of 140 s-1; the QB semiquinone EPR signal decayed with a rate constant of about 5 s-1. Heme b and CuB were reduced within the 10-ms dead time of the freeze-quench experiment and remained at a constant level of reduction over the 1-s time course of the experiment. Quantitation of the reduction levels of QB and heme b during this reaction yielded a reduction potential of 30-60 mV for heme b. Under a dioxygen atmosphere, the rates of semiquinone formation and its subsequent decay were not altered significantly. However, accurate quantitation of the EPR signals for heme b and heme o3 could not be made, due to interference from dioxygen. In the reaction between the QB-depleted enzyme and UQ2H2 under substoichiometric conditions, there was no observable change in the EPR spectra of the enzyme over the time course of the reaction, suggesting an electron transfer from heme b to the binuclear site in the absence of QB which occurs within the dead time of the freeze-quench apparatus. Analysis of the thermodynamics and kinetics of electron transfers in this enzyme suggests that a Q-cycle mechanism for proton translocation is more likely than a cytochrome c oxidase-type ion-pump mechanism.