An X-ray absorption spectroscopy study of the interactions of Ni2+ with yeast enolase.
An x-ray absorption spectroscopy (XAS) study was carried out at pH 7.6 on solutions of Ni2+ and yeast enolase depleted of its physiological cofactor (Mg2+) in the presence or absence of substrate/product, the very strongly bound competitive inhibitor 2-phosphonoacetohydroxamate and Mg2+. Both "conformational" and "catalytic" Ni2+ are distorted octahedral in coordination, in agreement with several spectroscopic studies but in contrast to the coordination in the crystal at pH 6.0. The data are consistent with direct coordination of what must be the catalytic Ni2+ to the phosphate of the substrate, in agreement with some previous data but in disagreement with recent interpretations by other workers. The ligands around the metal ions obtained from the x-ray structure give simulated XAS spectra in good agreement with the observed spectra.
Wang
S
S
Center for Metalloenzyme Studies, University of Georgia, Athens, USA.
Scott
R A
RA
Lebioda
L
L
Zhou
Z H
ZH
Brewer
J M
JM
D001665:Binding Sites; D008274:Magnesium / Q000378:metabolism; D008958:Models, Molecular; D009532:Nickel / Q000378:metabolism*; D010751:Phosphopyruvate Hydratase / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013057:Spectrum Analysis
D009532:Nickel; D010751:Phosphopyruvate Hydratase; D008274:Magnesium