Zobrazeno 1 - 10 of 114 pro vyhledávání: '"B A, Averill"'
1
Nitric Oxide Binding to the Ferri- and Ferroheme States of Nitrophorin 1, a Reversible NO-Binding Heme Protein from the Saliva of the Blood-Sucking Insect, Rhodnius prolixus
Autor: X. D. Ding, William R. Montfort, B. A. Averill, John F. Andersen, Antonio J. Pierik, F.A. Walker, Andrzej Weichsel, Celia A. Balfour, Tatjana Kh. Shokhireva
Publikováno v: Journal of the American Chemical Society, 121, 128-138. American Chemical Society
The recombinant NO-binding heme protein, nitrophorin 1 (NP1) from the saliva of the blood-sucking insect, Rhodnius prolixus, has been studied by spectroelectrochemistry, EPR, NMR, and FTIR spectros...
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::73f2f742684b0fba95a020dffaaed8cc
https://doi.org/10.1021/ja982979i
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2
Internal friction of amine-intercalated TaS2
Autor: Jiadeng Zhu, E. D. Brandner, A Munier, Bellave Shivaram, B. A. Averill
Publikováno v: Journal of Materials Science. 33:1949-1954
Internal friction measurements on TaS2 and a representative number of its amine intercalates are reported. The intercalants are observed to magnify the features seen in the internal friction curve of pure TaS2 and to introduce new features such as ab
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::40ee8ac6664b6bc8f76ba8f34e60efef
https://doi.org/10.1023/a:1004382111266
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4
Composition- and Annealing-Dependent Properties of Ba(Bi,Tl)O3-δ
Autor: B. A. Averill, Thomas E. Sutto
Publikováno v: Journal of Solid State Chemistry. 105:263-270
Solid solutions of BaBiO 3 doped with thallium to give BaBi 1- x Tl x O 3-δ were prepared at 800°C and annealed at 425°C under either argon, air, or oxygen. All samples with x ≤ 0.4 showed an increase in the semiconducting band gap that was acco
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::70f574c6df5104c8cc2e892335834a92
https://doi.org/10.1006/jssc.1993.1214
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5
Resonance Raman excitation profiles indicate multiple Cys .fwdarw. Cu charge transfer transitions in type 1 copper proteins
Autor: Thomas M. Loehr, Joann Sanders-Loehr, Joan Selverstone Valentine, Jane Han, B. A. Averill, Yi Lu
Publikováno v: Journal of the American Chemical Society. 115:4256-4263
Nitrite reductase (NiR) from Achromobacrer cycloclastes and mutant yeast Cu-Zn superoxide dismutase (with Cys substituted for His80 and Cu for Zn) have both been shown to contain type 1 Cu sites. However, they differ from other type 1 (blue) Cu prote
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::f5b3285f20a28e7a84ed16a0a6ba3cf7
https://doi.org/10.1021/ja00063a048
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6
Characterization of the structural gene encoding a copper-containing nitrite reductase and homology of this gene to DNA of other denitrifiers
Autor: Marcos R. Fries, S G Bezborodnikov, Rick W. Ye, B A Averill, James M. Tiedje
Publikováno v: Applied and Environmental Microbiology. 59:250-254
A copper-containing nitrite reductase gene (nirU) from Pseudomonas sp. strain G-179 was found in a 1.9-kb EcoRI-BamHI DNA fragment. The coding region contained information for a polypeptide of 379 amino acids. The encoded protein had 78% identity in
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c95419b91486ed695fb1ddba21ef70cb
https://doi.org/10.1128/aem.59.1.250-254.1993
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8
H218O isotope exchange studies on the mechanism of reduction of nitric oxide and nitrite to nitrous oxide by denitrifying bacteria. Evidence for an electrophilic nitrosyl during reduction of nitric oxide
Autor: I Toro-Suarez, B A Averill, James M. Tiedje, Rick W. Ye
Publikováno v: Journal of Biological Chemistry. 266:12848-12851
Reduction of NO and NO2-by whole cells of eight strains of denitrifying bacteria known to contain either heme cd1 or copper-containing nitrite reductases (NiRs) has been examined in the presence of H218O. All organisms containing heme cd1 NiRs exhibi
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::8442890a63598deb2a9892fbff8bec81
https://doi.org/10.1016/s0021-9258(18)98771-5
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9
Fe-S and Mo-Fe-S clusters as models for the active site of nitrogenase
Autor: B A Averill
Publikováno v: Copper, Molybdenum, and Vanadium in Biological Systems ISBN: 9783540120421
Studies on the enzyme nitrogenase have shown that it contains two novel metal-sulfur clusters: the iron-molybdenum cofactor (FeMo-co), which contains one Mo, 6–7 Fe, and ∼ 4 S atoms in a spincoupled paramagnetic (S=3/2) cluster; and the P cluster
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::593f33e4da97345659ca56391361a712
https://doi.org/10.1007/bfb0111303
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