Experiment to evaluate feasibility of utilizing Skylab-EREP remote sensing data for tectonic analysis of the Bighorn Mountains region, Wyoming-Montana

There are no author-identified significant results in this report

Mixing with the radiofrequency single-electron transistor

By configuring a radio-frequency single-electron transistor as a mixer, we demonstrate a unique implementation of this device, that achieves good charge sensitivity with large bandwidth about a tunable center frequency. In our implementation we achieve a measurement bandwidth of 16 MHz, with a tunable center frequency from 0 to 1.2 GHz, demonstrated with the transistor operating at 300 mK. Ultimately this device is limited in center frequency by the RC time of the transistor's center island, which for our device is ~ 1.6 GHz, close to the measured value. The measurement bandwidth is determined by the quality factor of the readout tank circuit.Comment: Submitted to APL september 200

In-situ measurement of the permittivity of helium using microwave NbN resonators

By measuring the electrical transport properties of superconducting NbN quarter-wave resonators in direct contact with a helium bath, we have demonstrated a high-speed and spatially sensitive sensor for the permittivity of helium. In our implementation a $\sim10^{-3}$ mm$^3$ sensing volume is measured with a bandwidth of 300 kHz in the temperature range 1.8 to 8.8 K. The minimum detectable change of the permittivity of helium is calculated to be $\sim6\times$$10^{-11}$ $\epsilon_0$/Hz$^{1/2}$ with a sensitivity of order $10^{-13}$ $\epsilon_0$/Hz$^{1/2}$ easily achievable. Potential applications include operation as a fast, localized helium thermometer and as a transducer in superfluid hydrodynamic experiments.Comment: 4 pages, 3 figure

Analysis of the 23 June 2001 M w = 8.4 Peru underthrusting earthquake and its aftershocks

Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/95298/1/grl16079.pd

Interaction of intermediate energy protons with light nuclei

Interaction of intermediate energy protons with light nucle

A versatile and compact capacitive dilatometer

We describe the design, construction, calibration, and operation of a relatively simple differential capacitive dilatometer suitable for measurements of thermal expansion and magnetostriction from 300 K to below 1 K with a low-temperature resolution of about 0.05 angstroms. The design is characterized by an open architecture permitting measurements on small samples with a variety of shapes. Dilatometers of this design have operated successfully with a commercial physical property measurement system, with several types of cryogenic refrigeration systems, in vacuum, in helium exchange gas, and while immersed in liquid helium (magnetostriction only) to temperatures of 30 mK and in magnetic fields to 45 T.Comment: 8 pages, incorporating 6 figures, submitted to Rev. Sci. Instru

Analysis of Oligomerization Properties of Heme a Synthase Provides Insights into Its Function in Eukaryotes

Heme a is an essential cofactor for function of cytochrome c oxidase in the mitochondrial electron transport chain. Several evolutionarily conserved enzymes have been implicated in the biosynthesis of heme a, including the heme a synthase Cox15. However, the structure of Cox15 is unknown, its enzymatic mechanism and the role of active site residues remain debated, and recent discoveries suggest additional chaperone-like roles for this enzyme. Here, we investigated Cox15 in the model eukaryote Saccharomyces cerevisiae via several approaches to examine its oligomeric states and determine the effects of active site and human pathogenic mutations. Our results indicate that Cox15 exhibits homotypic interactions, forming highly stable complexes dependent upon hydrophobic interactions. This multimerization is evolutionarily conserved and independent of heme levels and heme a synthase catalytic activity. Four conserved histidine residues are demonstrated to be critical for eukaryotic heme a synthase activity and cannot be substituted with other heme-ligating amino acids. The 20-residue linker region connecting the two conserved domains of Cox15 is also important; removal of this linker impairs both Cox15 multimerization and enzymatic activity. Mutations of COX15 causing single amino acid conversions associated with fatal infantile hypertrophic cardiomyopathy and the neurological disorder Leigh syndrome result in impaired stability (S344P) or catalytic function (R217W), and the latter mutation affects oligomeric properties of the enzyme. Structural modeling of Cox15 suggests these two mutations affect protein folding and heme binding, respectively. We conclude that Cox15 multimerization is important for heme a biosynthesis and/or transfer to maturing cytochrome c oxidase

Analysis of Oligomerization Properties of Heme a Synthase Provides Insights into Its Function in Eukaryotes

Heme a is an essential cofactor for function of cytochrome c oxidase in the mitochondrial electron transport chain. Several evolutionarily conserved enzymes have been implicated in the biosynthesis of heme a, including the heme a synthase Cox15. However, the structure of Cox15 is unknown, its enzymatic mechanism and the role of active site residues remain debated, and recent discoveries suggest additional chaperone-like roles for this enzyme. Here, we investigated Cox15 in the model eukaryote Saccharomyces cerevisiae via several approaches to examine its oligomeric states and determine the effects of active site and human pathogenic mutations. Our results indicate that Cox15 exhibits homotypic interactions, forming highly stable complexes dependent upon hydrophobic interactions. This multimerization is evolutionarily conserved and independent of heme levels and heme a synthase catalytic activity. Four conserved histidine residues are demonstrated to be critical for eukaryotic heme a synthase activity and cannot be substituted with other heme-ligating amino acids. The 20-residue linker region connecting the two conserved domains of Cox15 is also important; removal of this linker impairs both Cox15 multimerization and enzymatic activity. Mutations of COX15 causing single amino acid conversions associated with fatal infantile hypertrophic cardiomyopathy and the neurological disorder Leigh syndrome result in impaired stability (S344P) or catalytic function (R217W), and the latter mutation affects oligomeric properties of the enzyme. Structural modeling of Cox15 suggests these two mutations affect protein folding and heme binding, respectively. We conclude that Cox15 multimerization is important for heme a biosynthesis and/or transfer to maturing cytochrome c oxidase

Physical Electronics

Contains reports on three research projects

The Assembly Factor Pet117 Couples Heme a Synthase Activity to Cytochrome Oxidase Assembly

Heme a is an essential metalloporphyrin cofactor of the mitochondrial respiratory enzyme cytochrome c oxidase (CcO). Its synthesis from heme b requires several enzymes, including the evolutionarily conserved heme a synthase (Cox15). Oligomerization of Cox15 appears to be important for the process of heme a biosynthesis and transfer to maturing CcO. However, the details of this process remain elusive, and the roles of any additional CcO assembly factors that may be involved remain unclear. Here we report the systematic analysis of one such uncharacterized assembly factor, Pet117, and demonstrate in Saccharomyces cerevisiae that this evolutionarily conserved protein is necessary for Cox15 oligomerization and function. Pet117 is shown to reside in the mitochondrial matrix, where it is associated with the inner membrane. Pet117 functions at the later maturation stages of the core CcO subunit Cox1 that precede Cox1 hemylation. Pet117 also physically interacts with Cox15 and specifically mediates the stability of Cox15 oligomeric complexes. This Cox15-Pet117 interaction observed by co-immunoprecipitation persists in the absence of heme a synthase activity, is dependent upon Cox1 synthesis and early maturation steps, and is further dependent upon the presence of the matrix-exposed, unstructured linker region of Cox15 needed for Cox15 oligomerization, suggesting that this region mediates the interaction or that the interaction is lost when Cox15 is unable to oligomerize. Based on these findings, it was concluded that Pet117 mediates coupling of heme a synthesis to the CcO assembly process in eukaryotes