C-13 NMR-STUDIES OF THE INFLUENCE OF AXIAL LIGAND ORIENTATION ON HEMEELECTRONIC-STRUCTURE

Authors
TURNER DL SALGUEIRO CA SCHENKELS P LEGALL J XAVIER AV
Citation
Dl. Turner et al., C-13 NMR-STUDIES OF THE INFLUENCE OF AXIAL LIGAND ORIENTATION ON HEMEELECTRONIC-STRUCTURE, Biochimica et biophysica acta. Protein structure and molecular enzymology, 1246(1), 1995, pp. 24-28
Citations number
20
Categorie Soggetti
Biology,Biophysics
Journal title
Biochimica et biophysica acta. Protein structure and molecular enzymology → ACNP
ISSN journal
01674838
Volume
1246
Issue
1
Year of publication
1995
Pages
24 - 28
Database
ISI
SICI code
0167-4838(1995)1246:1<24:CNOTIO>2.0.ZU;2-L
Abstract
Three-quarters of the carbon-13 resonances of nuclei attached to the f our haems of Desulfovibrio vulgaris ferricytochrome c(3) are assigned. Preliminary analysis of their Fermi contact interactions shows that t he shifts are directly related to the orientation of both of the axial histidine ligands in each case and the approach can therefore be used to obtain structural information in other cytochromes with bis-histid inyl coordination. The implications for the control of redox potential in cytochromes are discussed.