Metallobiochemistry Part C: Spectroscopic and Physical - download pdf or read online

By John N. Abelson, Melvin I. Simon, James F. Riordan, Bert L. Vallee

ISBN-10: 0121821277

ISBN-13: 9780121821272

This quantity of Methods in Enzymology and its spouse quantity 227 offers spectrosopic and actual tools for the decision of steel ion environments in metalloenzymes and metalloproteins

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Extra resources for Metallobiochemistry Part C: Spectroscopic and Physical Methods for Probing Metal Ion Environments in Metalloenzymes and Metalloproteins

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Thus, the 500 nm transition must be associated with azide binding to the paramagnetic type 2 copper. Although there is a peak in the low-temperature MCD spectrum in the region of the intense 400 nm absorption band, its intensity does not correlate with the increase in the 400 nm absorption intensity with increasing azide concentration. The 385 nm low-temperature MCD feature first increases, then decreases in magnitude with increasing azide concentration and corresponds to less than 10% of the type 3 sites for which the hydroxide bridge shown in Fig.

Am. Chem. Soc. 111, 5198 (1989). 39 F. Tuczek and E. I. Solomon, Inorg. Chem.. in press. 048eV lY FIG. 13. The thiolate-copper bond. The approximated blue copper site used in the SCFX a S W calculations has methyl thiolate (SCH 3-) substituted for cysteine, dimethyl thioether [S(CH3)2] for methionine, and ammonia (NH3) for the imidazole rings of the histidine residues. 34'35The left-hand side shows the S C F - X a S W wave function contours for the highest occupied orbitals of methyl thiolate. The right-hand side gives the contours for the ~-, pseudoo-, and o- bonds the thiolate forms on coordination to the copper site.

G. , and J. W. D. Connolly, in "Computational Methods for Large Molecules and Localized States in Solids" (F. Herman, A. D. McLean, and R. K. ), Plenum, New York, 1973. 26 j. W. D. Connolly, in "Modern Theoretical Chemistry" (G. A. ), Vol. 7. pp. 105-132. Plenum, New York, 1977. [1] ELECTRONIC ABSORPTION OF COPPER PROTEINS 17 Hamiltonian parameters; see Refs. 27-30) yield the predicted spectrum given in Fig. 7A. 3° The calculated charge transfer energies and relative band intensities agree well with the experimental spectrum.

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Metallobiochemistry Part C: Spectroscopic and Physical Methods for Probing Metal Ion Environments in Metalloenzymes and Metalloproteins by John N. Abelson, Melvin I. Simon, James F. Riordan, Bert L. Vallee


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