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• W2031566293 abstract "ESR spectra of the tight binding Cu(II) complex of bovine serum albumin (BSA) has been studied using S-band. At physiological pH, only one form of copper binding to BSA was detected from the ESR spectra. From previous X-band ESR spectra, nitrogen superhyperfine splittings were observable in the gxxx region; however, the resolution of the g¦¦ region was not sufficient to confirm the exact donor atoms of the complex. Using low-frequency ESR (2–4 GHz) at 77 K, we have resolved the nitrogen superhyperfine structure in the g¦¦ region. A computer simulation method has been developed for distinguishing between three and four nitrogen donor atoms. The Hyde-Froncisz theory of g and A strain broadening has been modified to use a field-swept calculation for the line shape. The observed intensity pattern and the computer simulation of such spectra positively confirm the structure of Cu(II) ion coordinated to four in-plane nitrogen atoms in frozen aqueous solutions of Cu(II)-BSA complexes at physiological pH. This is the first time that this binding site has been confirmed on the protein instead of a protein fragment or model compound. This work is another example of the usefulness of the S-band ESR technique for characterizing the metal-protein interactions when random variation in g factors cause line broadening in conventional X-band ESR spectra." @default.
• W2031566293 created "2016-06-24" @default.
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• W2031566293 date "1985-11-01" @default.
• W2031566293 modified "2023-10-03" @default.
• W2031566293 title "Direct Evidence of Nitrogen Coupling in the Copper(II) Complex of Bovine Serum Albumin by S-Band Electron Spin Resonance Technique" @default.
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• W2031566293 doi "https://doi.org/10.1016/0162-0134(85)80015-5" @default.
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