Cypress Avenue Pumping Station : hydraulic model investigation /

"July 1994."

Selecting large pumping units /

Includes bibliographical references.

Care and operation of pumping engines and units.

Mode of access: Internet.

Operator's, organizational, direct support, and general support maintenance manual : pumping assembly, diesel engine driven, wheel mtd, 350 gpm, 275 ft. head, model 13220E1070 (97403) (fuel use only), NSN 4320-01-092-3551 ....

"15 August 1984."

Operator and organizational maintenance manual : pumping assembly, flammable liquid, bulk transfer, lightweight, centrifugal, 100 gpm minimum, gasoline-engine-driven (Barnes model US6ACG), FSN 4320-150-6116.

Includes index.

Operation and organizational maintenance manual : pumping assembly, flammable liquid, bulk transfer, gasoline engine driven, 350 gpm capacity, 275 feet total dynamic head, wheel mounted (Peabody Barnes, Inc. model US37ACG), FSN 4320-195-4914.

Includes index.

Organizational, direct support, and general support maintenance repair parts and special tools list (including depot maintenance repair parts and special tools) : pumping assembly, flammable liquid, bulk transfer : gasoline engine driven; 350 GPM capacity at 190 feethead; wheel mounted (Gorman-Rupp model 84C15-4A084) NSN 4320-00-916-9172 and (Barnes model US36ACG) NSN 4320-00-407-2583.

Includes index.

Organizational, direct support, and general support maintenance repair parts and special tools list for pumping assembly, diesel engine driven, wheel mtd, 350 gpm, 275 ft. head, model 350PAF (fuel use only), NSN 4320-01-092-3551 ....

"23 July 1990."

Operator, organizational, direct and general support : pumping assembly, flammable liquid, bulk transfer, 50 GPM, (Barnes model 9117CA) Army model SPE 16 FSN 4320-728-0265, (Barnes model 15671CA)[ Army model SPE 16A FSN 4320-658-2888, (Barnes model 4074CA) FSN 4320-271-1858.

"May 1968."

Operation and organizational maintenance manual : pumping assembly, flammable liquid, bulk transfer, gasoline engine driven, 350 gpm capacity, 275 feet total dynamic head, wheel mounted (Peabody Barnes, Inc. model US37ACG), FSN 4320-195-4914.

"January 1974."

The redox-Bohr group associated with iron-sulfur cluster N2 of complex I

Proton pumping respiratory complex I (NADH: ubiquinone oxidoreductase) is a major component of the oxidative phosphorylation system in mitochondria and many bacteria. In mammalian cells it provides 40% of the proton motive force needed to make ATP. Defects in this giant and most complicated membrane-bound enzyme cause numerous human disorders. Yet the mechanism of complex I is still elusive. A group exhibiting redox-linked protonation that is associated with iron-sulfur cluster N2 of complex I has been proposed to act as a central component of the proton pumping machinery. Here we show that a histidine in the 49-kDa subunit that resides near iron-sulfur cluster N2 confers this redox-Bohr effect. Mutating this residue to methionine in complex I from Yarrowia lipolytica resulted in a marked shift of the redox midpoint potential of iron-sulfur cluster N2 to the negative and abolished the redox-Bohr effect. However, the mutation did not significantly affect the catalytic activity of complex I and protons were pumped with an unchanged stoichiometry of 4 H+/2e(-). This finding has significant implications on the discussion about possible proton pumping mechanism for complex I.

Projecte d’una instal•lació solar fotovoltaica per a un sistema de bombes de reg

Instal.lació d’una explotació agrícola amb funcionament per energia solar fotovoltaica a Torregrossa (Tarragona). Disseny i definició de les parts necessàries que conformaran la instal•lació solar fotovoltaica que subministrarà energia elèctrica a les bombes de reg

Wear in centrifugal slurry pumps

The project improves understanding of wear in slurry pumps. By measuring actual pump wear and microscopically examining worn surfaces, a clearer picture emerged of wear modes and mechanisms for different materials. This enables improved guidelines for material selection and modifications to hydraulic shape that increased pump wear life.

On the role of the K-proton transfer pathway in cytochrome c oxidase

Cytochrome c oxidase is a membrane-bound enzyme that catalyzes the four-electron reduction of oxygen to water. This highly exergonic reaction drives proton pumping across the membrane. One of the key questions associated with the function of cytochrome c oxidase is how the transfer of electrons and protons is coupled and how proton transfer is controlled by the enzyme. In this study we focus on the function of one of the proton transfer pathways of the R. sphaeroides enzyme, the so-called K-proton transfer pathway (containing a highly conserved Lys(I-362) residue), leading from the protein surface to the catalytic site. We have investigated the kinetics of the reaction of the reduced enzyme with oxygen in mutants of the enzyme in which a residue [Ser(I-299)] near the entry point of the pathway was modified with the use of site-directed mutagenesis. The results show that during the initial steps of oxygen reduction, electron transfer to the catalytic site (to form the “peroxy” state, Pr) requires charge compensation through the proton pathway, but no proton uptake from the bulk solution. The charge compensation is proposed to involve a movement of the K(I-362) side chain toward the binuclear center. Thus, in contrast to what has been assumed previously, the results indicate that the K-pathway is used during oxygen reduction and that K(I-362) is charged at pH ≈ 7.5. The movement of the Lys is proposed to regulate proton transfer by “shutting off” the protonic connectivity through the K-pathway after initiation of the O2 reduction chemistry. This “shutoff” prevents a short-circuit of the proton-pumping machinery of the enzyme during the subsequent reaction steps.