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Novel binuclear copper chromophores in biology: The CuA and Cuz sites in bacterial nitrous oxide reductase by F. Neese; W.G. Zumft; W.E. Antholine; P.M.H. Kroneck is a Chemistry article available to read on EtoBox.

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The copper sites of the bacterial enzyme nitrous oxide reductase (N2OR) [ 1 ] have been investigated by a variety of spectroscopic methods including multifrequency EPR, ENDOR, MCD and EXAFS. EPR and ENDOR spectra for the purple mixed-valence [Cu(1.5+)...Cu(1.5+)], S=1/2 site (CUA) were obtained after insertion of either 63Cu or 65Cu or both 65Cu and [l 5N]histidin e [2,3]. The Cu hyperfine parameters obtained were indicative of a highly covalent Cu site. The total Cu character (CUA1 + Cure) in the ground state wave function required to describe the spin density distribution was 31-37% compared to 41% for type-1 Cu in plastocyanin. This value does not completely account for the reduction of gmax from 2.23 of type-1 Cu in plastocyanin to 2.18 of CuA in N2OR. Remaining discrepancies were discussed in terms of different alignments of the principal axes for the hypothetical monomeric Cure and CUAZ in [Cu(1.5+)...Cu(1.5+)]. Based on X-ray structural data of CUA in cytochrome c oxidase, MO calculations on a mixed-valence [(NH3)Cu(1.5+)(SCH3)2Cu(1.5+)(NH3)] + sulfur-bridged core were used to interpret the spectroscopic data. An assignment has been made in terms of a covalent planar rhomb [

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Author

F. Neese; W.G. Zumft; W.E. Antholine; P.M.H. Kroneck

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 0162-0134)

Published

1997

Language

EN

Field

Chemistry (Physical Sciences)