Zobrazeno 1 - 10 of 12 pro vyhledávání: '"N. J. Blackburn"'
1
The CuA domain of Thermus thermophilus ba3-type cytochrome c oxidase at 1.6 A resolution
Autor: P A, Williams, N J, Blackburn, D, Sanders, H, Bellamy, E A, Stura, J A, Fee, D E, McRee
Publikováno v: Nature structural biology. 6(6)
The structure of the CuA-containing, extracellular domain of Thermus thermophilus ba3-type cytochrome c oxidase has been determined to 1.6 A resolution using multiple X-ray wavelength anomalous dispersion (MAD). The Cu2S2 cluster forms a planar rhomb
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::1028afb1b1f03ee53a886b84746f253b
https://pubmed.ncbi.nlm.nih.gov/10360350
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3
Copper K-extended x-ray absorption fine structure studies of oxidized and reduced dopamine beta-hydroxylase. Confirmation of a sulfur ligand to copper(I) in the reduced enzyme
Autor: N J, Blackburn, S S, Hasnain, T M, Pettingill, R W, Strange
Publikováno v: The Journal of biological chemistry. 266(34)
The structure of the copper sites in oxidized and reduced dopamine beta-hydroxylase has been studied by extended x-ray absorption fine structure spectroscopy using a restrained refinement approach to data analysis. An histidine-rich active site has b
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::99ad77c9b496f95da83d02911d4250b2
https://pubmed.ncbi.nlm.nih.gov/1744110
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4
Carbonmonoxy dopamine beta-hydroxylase. Structural characterization by Fourier transform infrared, fluorescence, and x-ray absorption spectroscopy
Autor: T M, Pettingill, R W, Strange, N J, Blackburn
Publikováno v: The Journal of biological chemistry. 266(26)
The carbon monoxide complex of ascorbate-reduced dopamine beta-hydroxylase has been prepared and characterized by Fourier transform infrared, fluorescence, and x-ray absorption spectroscopies. CO has previously been shown to be a competitive inhibito
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::eb78098264977bb9392edef49f6ad1f9
https://pubmed.ncbi.nlm.nih.gov/1894598
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5
Characterization of a carbon monoxide complex of reduced dopamine beta-hydroxylase. Evidence for inequivalence of the Cu(I) centers
Autor: N J, Blackburn, T M, Pettingill, K S, Seagraves, R T, Shigeta
Publikováno v: The Journal of biological chemistry. 265(26)
Ascorbate-reduced dopamine beta-hydroxylase (DBH) is inhibited by CO in a competitive manner with respect to molecular O2. Measurement of the stoichiometry of CO binding indicates 0.50 CO bound per Cu(I), which provides the first evidence that the Cu
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::4071d40cd0809df555bf3f1df841ac85
https://pubmed.ncbi.nlm.nih.gov/2394729
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7
Kinetic and e.p.r. studies of cyanide and azide binding to the copper sites of dopamine (3,4-dihydroxyphenethylamine) beta-mono-oxygenase
Autor: N J Blackburn, D Collison, J Sutton, F E Mabbs
Publikováno v: The Biochemical journal. 220(2)
The kinetics of inhibition of dopamine (3,4-dihydroxyphenethylamine) beta-mono-oxygenase by cyanide (CN-) and azide (N3-) ions have been investigated by using steady-state methods. Both anions show complex non-competitive-inhibition patterns with res
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c6c002ed9a713212f75c4e46550cdd2
https://pubmed.ncbi.nlm.nih.gov/6331417
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