Document Detail

The copper coordination group in "blue" copper proteins: evidence from resonance Raman spectra.
MedLine Citation:
PMID:  804316     Owner:  NLM     Status:  MEDLINE    
Tunable dye laser excitation in the intense similar to 600-nm absorption band of azurin, plastocyanin, and ceruloplasmin provides resonance enhanced Raman spectra. They consist of a complex set of bands, at least three or four in number, between 350 and 473 cm-1, which are assignable to Cu-N or Cu-O bond stretching, and a weak band near 270 cm-1, which probably arises from Cu-S stretching. A weak band at 765 cm-1 found in plastocyanin may arise from C-S stretching. Analysis of the Raman intensity pattern, as well as of the nature of the resonant electronic transition, leads to a model of the "blue" copper site involving approximately trigonal-bipyramidal coordination, with a sulfur and two nitrogen ligands in the equatorial plane, and less strongly bound nitrogen or oxygen ligands at axial positions. This arrangement would be well poised for stabilization of Cu(I) upon reduction.
V Miskowski; S P Tang; T G Spiro; E Shapiro; T H Moss
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biochemistry     Volume:  14     ISSN:  0006-2960     ISO Abbreviation:  Biochemistry     Publication Date:  1975 Mar 
Date Detail:
Created Date:  1975-07-07     Completed Date:  1975-07-07     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  1244-50     Citation Subset:  IM    
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MeSH Terms
Bacterial Proteins*
Models, Chemical
Plant Proteins*
Pseudomonas aeruginosa / analysis
Scattering, Radiation
Spectrum Analysis
Reg. No./Substance:
0/Bacterial Proteins; 0/Ligands; 0/Plant Proteins; 12284-43-4/Azurin; 7440-50-8/Copper; 7704-34-9/Sulfur; 7727-37-9/Nitrogen; 9014-09-9/Plastocyanin; EC

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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