Water Determination by Near Infrared Spectrophotometry.

Meeker, R. L.; Critchfield, F. E.; Bishop, E.

doi:10.1021/ac60191a048

Cited by 30 publications

(9 citation statements)

References 2 publications

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“…The yield of N 2 was determined to be 86±5 % by GCMS analysis, and formation of 15 N 2 was observed when using 15 N 2 O. Thus, the yield of 2 is representative of the production of N 2 from N 2 O. Owing to the incompatibility of various reaction components with reagents employed in Karl Fischer titration and other chemical H 2 O assays, the formation of H 2 O was verified qualitatively using an established near‐IR assay, although H 2 O quantification proved to be challenging by this method (Supporting Information, pages S23–S25).…”

Section: Figurementioning

confidence: 77%

N₂O Reductase Activity of a [Cu₄S] Cluster in the 4Cu^I Redox State Modulated by Hydrogen Bond Donors and Proton Relays in the Secondary Coordination Sphere

et al. 2019

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The model complex [Cu4(μ4‐S)(dppa)4]2+ (1, dppa=μ2‐(Ph2P)2NH) has N2O reductase activity in methanol solvent, mediating 2 H+/2 e− reduction of N2O to N2+H2O in the presence of an exogenous electron donor (CoCp2). A stoichiometric product with two deprotonated dppa ligands was characterized, indicating a key role of second‐sphere N−H residues as proton donors during N2O reduction. The activity of 1 towards N2O was suppressed in solvents that are unable to provide hydrogen bonding to the second‐sphere N−H groups. Structural and computational data indicate that second‐sphere hydrogen bonding induces structural distortion of the [Cu4S] active site, accessing a strained geometry with enhanced reactivity due to localization of electron density along a dicopper edge site. The behavior of 1 mimics aspects of the CuZ catalytic site of nitrous oxide reductase: activity in the 4CuI:1S redox state, use of a second‐sphere proton donor, and reactivity dependence on both primary and secondary sphere effects.

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Section: Figurementioning

confidence: 77%

N₂O Reductase Activity of a [Cu₄S] Cluster in the 4Cu^I Redox State Modulated by Hydrogen Bond Donors and Proton Relays in the Secondary Coordination Sphere

et al. 2019

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“…The water content was determined (Meeker et al, 1962) as about 0.15%. Trifluoroacetic anhydride (Eastman) was carefully added until the water content was 0.01%.…”

Section: Arg-lys-ile-cys-leu-asp-pro-asp-ala-pro-arg-ile-lys-lys-ile-mentioning

confidence: 99%

“…Heptafluorobutyric acid was prepared as previously described (Edman & Begg, 1967). The water content was determined (Meeker et al, 1962) as about 0.15%. Trifluoroacetic anhydride (Eastman) was carefully added until the water content was 0.01%.…”

mentioning

confidence: 99%

Complete covalent structure of human .beta.-thromboglobulin

Begg¹,

Pepper²,

Chesterman³

et al. 1978

Biochemistry

210

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The complete primary structure of the platelet-specific protein human beta-thromboglobulin has been determined. beta-Thromboglobulin consists of identical subunits of 81 amino acids, each with a molecular weight of 8851. The amino acid sequence of the beta-thromboglobulin subunit is: Gly-Lys-Glu-Glu-Ser-Leu-Asp-Ser-Asp-Leu-Tyr-Ala-Glu-Leu-Arg-Cys-Met-Cys-Ile-Lys-Thr-Thr-Ser-Gly-Ile-His-Pro-Lys-Asn-Ile-Gln-Ser-Leu-Glu-Val-Ile-Gly-Lys-Gly-Thr-His-Cys-Asn-Gln-Val-Glu-Val-Ile-Ala-Thr-Leu-Lys-Asp-Gly-Arg-Lys-Ile-Cys-Leu-Asp-Pro-Asp-Ala-Pro-Arg-Ile-Lys-Lys-Ile-Val-Gln-Lys-Lys-Leu-Ala-Gly-Asp-Glu-Ser-Ala-Asp. Disulfide bridge-18 to half-cystine-58. The amino acid sequence of beta-thromboglobulin shows a marked homology with that of platelet factor 4. When the sequences are aligned for maximum homology, 42 of the 81 residues of beta-thromboglobulin are identical with those of platelet factor 4, including the position of the four half-cystines.

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“…Several different regions of the near-infrared spectrum are individually predictive of water concentration in DMSO. The water first combination band near 5150 cm À1 is often used to determine water in organic solvents, [8][9][10][11][12] but it is not considered here due to its excessive absorption for water concentrations above approximately 4 wt % in TrakMate tubes. Similarly, the DMSO first combination band region near 4330 cm À1 is not useful for samples in TrakMate tubes due to excessive absorption.…”

Section: Resultsmentioning

confidence: 99%

Rapid, Nondestructive Near-Infrared Assay for Water in Sealed Dimethyl Sulfoxide Compound Repository Containers

Pelletier

Fabiilli

2007

Appl Spectrosc

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Water contamination in dimethyl sulfoxide (DMSO) compound libraries is a recognized problem in the pharmaceutical industry. We describe a nondestructive, near-infrared (NIR) assay for water contamination inside the sealed containers used for compound libraries. This assay does not require opening the containers. We also report our observation of the permeation of water from laboratory air through the sealed container and into the DMSO solution over a period of months, as well as the rate of water absorption by DMSO directly exposed to laboratory air.

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Water Determination by Near Infrared Spectrophotometry.

Cited by 30 publications

References 2 publications

N₂O Reductase Activity of a [Cu₄S] Cluster in the 4Cu^I Redox State Modulated by Hydrogen Bond Donors and Proton Relays in the Secondary Coordination Sphere

N₂O Reductase Activity of a [Cu₄S] Cluster in the 4Cu^I Redox State Modulated by Hydrogen Bond Donors and Proton Relays in the Secondary Coordination Sphere

Complete covalent structure of human .beta.-thromboglobulin

Rapid, Nondestructive Near-Infrared Assay for Water in Sealed Dimethyl Sulfoxide Compound Repository Containers

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Water Determination by Near Infrared Spectrophotometry.

Cited by 30 publications

References 2 publications

N2O Reductase Activity of a [Cu4S] Cluster in the 4CuI Redox State Modulated by Hydrogen Bond Donors and Proton Relays in the Secondary Coordination Sphere

N2O Reductase Activity of a [Cu4S] Cluster in the 4CuI Redox State Modulated by Hydrogen Bond Donors and Proton Relays in the Secondary Coordination Sphere

Complete covalent structure of human .beta.-thromboglobulin

Rapid, Nondestructive Near-Infrared Assay for Water in Sealed Dimethyl Sulfoxide Compound Repository Containers

Contact Info

Product

Resources

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N₂O Reductase Activity of a [Cu₄S] Cluster in the 4Cu^I Redox State Modulated by Hydrogen Bond Donors and Proton Relays in the Secondary Coordination Sphere

N₂O Reductase Activity of a [Cu₄S] Cluster in the 4Cu^I Redox State Modulated by Hydrogen Bond Donors and Proton Relays in the Secondary Coordination Sphere