Rapid Quench in an Electrostatic Levitator

Abstract METGLAS Alloy 2826 (Fe40Ni40P14B6) is a ferromagnetic, high permeability, nickel-iron metallic glass which, when appropriately annealed, yields a material similar to the higher nickel containing permalloys in magnetic properties. Alloy 2826 is a single phase, opaque metallic material with a glass-like structure obtained by a very rapid quench from the liquid state. This datasheet provides information on composition, physical properties, hardness, elasticity, and tensile properties as well as creep. It also includes information on forming and heat treating. Filing Code: Ni-235. Producer or source: Allied Chemical Corporation.

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Precise Density Measurement of Liquid Titanium by Electrostatic Levitator

MATERIALS TRANSACTIONS ◽

10.2320/matertrans.l-m2017835 ◽

2017 ◽

Vol 58 (12) ◽

pp. 1664-1669 ◽

Cited By ~ 5

Author(s):

Shumpei Ozawa ◽

Yu Kudo ◽

Kazuhiko Kuribayashi ◽

Yuki Watanabe ◽

Takehiko Ishikawa

Keyword(s):

Density Measurement ◽

Liquid Titanium ◽

Electrostatic Levitator

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Solution electrostatic levitator for measuring surface properties and bulk structures of an extremely supersaturated solution drop above metastable zone width limit

Review of Scientific Instruments ◽

10.1063/1.4982363 ◽

2017 ◽

Vol 88 (5) ◽

pp. 055101 ◽

Cited By ~ 3

Author(s):

Sooheyong Lee ◽

Wonhyuk Jo ◽

Yong chan Cho ◽

Hyun Hwi Lee ◽

Geun Woo Lee

Keyword(s):

Surface Properties ◽

Supersaturated Solution ◽

Metastable Zone Width ◽

Zone Width ◽

Measuring Surface ◽

Metastable Zone ◽

Electrostatic Levitator ◽

Bulk Structures

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Electron transfer and half-reactivity in nitrogenase

Biochemical Society Transactions ◽

10.1042/bst0390201 ◽

2011 ◽

Vol 39 (1) ◽

pp. 201-206 ◽

Cited By ~ 2

Author(s):

Thomas A. Clarke ◽

Shirley Fairhurst ◽

David J. Lowe ◽

Nicholas J. Watmough ◽

Robert R. Eady

Keyword(s):

Electron Transfer ◽

Protein Molecule ◽

Stopped Flow ◽

Protein Binding Sites ◽

Molybdenum Iron Protein ◽

Iron Protein ◽

Mofe Protein ◽

Fe Protein ◽

Rapid Quench ◽

Important Enzyme

Nitrogenase is a globally important enzyme that catalyses the reduction of atmospheric dinitrogen into ammonia and is thus an important part of the nitrogen cycle. The nitrogenase enzyme is composed of a catalytic molybdenum–iron protein (MoFe protein) and a protein containing an [Fe4–S4] cluster (Fe protein) that functions as a dedicated ATP-dependent reductase. The current understanding of electron transfer between these two proteins is based on stopped-flow spectrophotometry, which has allowed the rates of complex formation and electron transfer to be accurately determined. Surprisingly, a total of four Fe protein molecules are required to saturate one MoFe protein molecule, despite there being only two well-characterized Fe-protein-binding sites. This has led to the conclusion that the purified Fe protein is only half-active with respect to electron transfer to the MoFe protein. Studies on the electron transfer between both proteins using rapid-quench EPR confirmed that, during pre-steady-state electron transfer, the Fe protein only becomes half-oxidized. However, stopped-flow spectrophotometry on MoFe protein that had only one active site occupied was saturated by approximately three Fe protein equivalents. These results imply that the Fe protein has a second interaction during the initial stages of mixing that is not involved in electron transfer.

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