The magnetic moment of the 10+ isomer in140Ce andE1 transitions inN=82 isotones caused by outer subshell configurations

Using the reaction¹³⁸Ba(α,2n)¹⁴⁰Ce the magnetic moment of the 10 ₁ ⁺ isomer atE _x =3714.7 keV in theN=82 nucleus¹⁴⁰Ce has been determined by means of the TDPAD method toμ=+10.3(4)μ _N . Measuredg-factors in¹⁴⁰Ce are compared to calculations within the shell model with configuration mixing. For the 10 ₁ ⁺ isomer in¹⁴⁰Ce the four proton configuration π(1g ₇ ^2/2 ,2d ₅ ^2/2 ) has been found to be dominant. From theg-factor measurement strong contributions of multiparticle excitations to thegp2d _3/2,π3s ₁ ² or π1h ₁₁ ² shells and admixtures of neutron excitations to the wave function of the 10 ₁ ⁺ state could be excluded. The strongE1γ-branch of the deexcitation of the 10 ₁ ⁺ isomer in¹⁴⁰Ce can be explained by means of small admixtures of configurations which contain the outer subshell excitationsπ2f _7/2 andπ1h _9/2. On this basisE1 transitions experimentally observed in theN=82 nuclei¹⁴⁰Ce,¹⁴¹Pr and¹⁴⁵Eu may be understood.     

Meromorphic extensions of regular holonomic distributions

In this paper we consider distributions of the form 1/P and dy/P(x,y), whereP is a polynomial. Using results by Kashiwara and Kawai we give fairly accessible proofs that these expressions can be defined as regular holonomic distributions by utilising a meromorphic parameter. We also discuss distributions of the form /P and their direct image , when one knows that is a regular holonomic distribution. All these distributions are relevant to the study of renormalised Feynman integrals.     

Binding of single nucleotides to H+-ATP synthases observed by fluorescence resonance energy transfer

F(0)F(1)-ATP synthases couple proton translocation with the synthesis of ATP from ADP and phosphate. The enzyme has three catalytic nucleotide binding sites, one on each beta-subunit; three non-catalytic binding sites are located mainly on each alpha-subunit. In order to observe substrate binding to the enzyme, the H(+)-ATP synthase from Escherichia coli was labelled selectively with the fluorescence donor tetramethylrhodamine (TMR) at position T106C of the gamma-subunit. The labelled enzymes were incorporated into liposomes and catalysed proton-driven ATP synthesis. The substrate ATP-Alexa Fluor 647 was used as the fluorescence acceptor to perform intermolecular fluorescence resonance energy transfer (FRET). Single molecules are detected with a confocal set-up. When one ATP-Alexa Fluor 647 binds to the enzyme, FRET can be observed. Five stable states with different intermolecular FRET efficiencies were distinguished for enzyme-bound ATP-Alexa Fluor 647 indicating binding to different binding sites. Consecutive hydrolysis of excess ATP resulted in stepwise changes of the FRET efficiency. Thereby, gamma-subunit movement during catalysis was directly monitored with respect to the binding site with bound ATP-Alexa Fluor 647.