Measurement of the velocity distribution of sputtered Na atoms from NaCl by Doppler shift laser fluorescence

The velocity distribution of sputtered Na atoms from NaCI during 15 keV, Ar+ bombardment was measured by a Doppler shift laser fluorescence technique. Contrary to other measurements, the sputtered Na atoms were found to have a velocity distribution identical to that of a three-dimensional Maxwell-Boltzmann gas.Peer reviewedElectrical and Computer Engineerin

A thermostable hybrid cluster protein from Pyrococcus furiosus: Effects of the loss of a three helix bundle subdomain

Pyrococcus furiosus hybrid cluster protein (HCP) was expressed in Escherichia coli, purified, and characterized. This is the first archaeal and thermostable HCP to be isolated. Compared with the protein sequences of previously characterized HCPs from mesophiles, the protein sequence of P. furiosus HCP exhibits a deletion of approximately 13 kDa as a single amino acid stretch just after the N-terminal cysteine motif, characteristic for class-III HCPs from (hyper)thermophilic archaea and bacteria. The protein was expressed as a thermostable, soluble homodimeric protein. Hydroxylamine reductase activity of P. furiosus HCP showed a K m value of 0.40 mM and a k cat value of 3.8 s?1 at 70 °C and pH 9.0. Electron paramagnetic resonance spectroscopy showed evidence for the presence of a spin-admixed, S = 3/2 [4Fe–4S]+ cubane cluster and of the hybrid cluster. The cubane cluster of P. furiosus HCP is presumably coordinated by a CXXC–X7–C–X5–C motif close to the N-terminus, which is similar to the CXXC–X8–C–X5–C motif of the Desulfovibrio desulfuricans and Desulfovibrio vulgaris HCPs. Amino acid sequence alignment and homology modeling of P. furiosus HCP reveal that the deletion results in a loss of one of the two three-helix bundles of domain 1. Clearly the loss of one of the three-helix bundles of domain 1 does not diminish the hydroxylamine reduction activity and the incorporation of the iron–sulfur clusters.BiotechnologyApplied Science