Zobrazeno 1 - 10
of 18
pro vyhledávání: '"C. P. SCHOLES"'
Publikováno v:
Journal of Biological Chemistry. 263:3588-3591
We measured an electronic change at cysteine ligand(s) of the CuA2+ center brought on by reduction of other metal centers within cytochrome c oxidase, notably cytochrome a. This change specifically manifested itself as a modification in magnetic hype
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::04aeba6e75cf8af04f5fb55898e82417
https://doi.org/10.1016/s0021-9258(18)68965-3
https://doi.org/10.1016/s0021-9258(18)68965-3
Publikováno v:
Scopus-Elsevier
The techniques of EPR and electron nuclear double resonance (ENDOR) were used to probe structure and electronic distribution at the nitric oxide (NO)-ligated heme alpha 3 in the nitrosylferrocytochrome alpha 3 moiety of fully reduced cytochrome c oxi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f0b30299d2386800f84fa098e4326923
https://doi.org/10.1016/s0021-9258(18)32198-7
https://doi.org/10.1016/s0021-9258(18)32198-7
Publikováno v:
Journal of Biological Chemistry. 263:8420-8429
The resolution of new features in the 1H electron nuclear double resonance (ENDOR) spectrum of the oxidized CuA site in beef heart cytochrome c oxidase is presented. In a previous study, we assigned resonances in the CuA ENDOR spectrum to hyperfine i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::92b9847f2ef4169121a0b40e417d7857
https://doi.org/10.1016/s0021-9258(18)68494-7
https://doi.org/10.1016/s0021-9258(18)68494-7
Publikováno v:
Journal of the American Chemical Society. 105:7553-7556
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bf10069a618aaf87425fbad969008c98
https://doi.org/10.1021/ja00364a014
https://doi.org/10.1021/ja00364a014
Interaction in cytochrome c oxidase between cytochrome a3 ligated with nitric oxide and cytochrome a
Publikováno v:
Scopus-Elsevier
EPR spectra of nitric oxide complexes of cytochrome c oxidase were studied as a function of temperature in the fully reduced form and in a mixed valence form. In the 12-77 K range, temperature-dependent motion changed the EPR spectral line shape of t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8031381d7a9f35575207bfac982b0132
https://doi.org/10.1016/s0021-9258(20)81894-8
https://doi.org/10.1016/s0021-9258(20)81894-8
Publikováno v:
Scopus-Elsevier
Using low frequency 2 to 4 GHz EPR at 10 K, we have resolved previously unseen hyperfine structure associated with the EPR-detectable copper signal of cytochrome c oxidase. The observed hyperfine structure appears consistent with hyperfine coupling t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e45490065510bc0e365a5ac333cf7adc
https://doi.org/10.1016/s0021-9258(18)35967-2
https://doi.org/10.1016/s0021-9258(18)35967-2
Publikováno v:
Chemischer Informationsdienst. 17
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f86b8955648f2d9b6fce936555077634
https://doi.org/10.1002/chin.198630044
https://doi.org/10.1002/chin.198630044
Publikováno v:
Chemischer Informationsdienst. 15
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1e77a75a02353033d6910e9e665e99a6
https://doi.org/10.1002/chin.198414048
https://doi.org/10.1002/chin.198414048
Publikováno v:
The Journal of biological chemistry. 260(5)
A histidine auxotroph of Saccharomyces cerevisiae has been used to metabolically incorporate [1,3-15N2] histidine into yeast cytochrome c oxidase. Electron nuclear double resonance (ENDOR) spectroscopy of cytochrome a in the [15N]histidine-substitute
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::0d51034d62e04e8bc958e67093d06295
https://pubmed.ncbi.nlm.nih.gov/2982841
https://pubmed.ncbi.nlm.nih.gov/2982841
Publikováno v:
The Journal of biological chemistry. 263(8)
We measured an electronic change at cysteine ligand(s) of the CuA2+ center brought on by reduction of other metal centers within cytochrome c oxidase, notably cytochrome a. This change specifically manifested itself as a modification in magnetic hype
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::c575fc7c57d9e18daefd2e04b6528bbb
https://pubmed.ncbi.nlm.nih.gov/2831193
https://pubmed.ncbi.nlm.nih.gov/2831193