Effect of the methionine ligand on the reorganization energy of the type-1 copper site of nitrite Reductase
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Effect of the methionine ligand on the reorganization energy of the type-1 copper site of nitrite Reductase. / Farver, Ole; Wijma, Hein J.; MacPherson, Iain; Tocheva, Elitza I.; Pecht, Israel; Verbeet, Martin Ph.; Murphy, Michael E. P.; Canters, Gerard W.
In: Journal of the American Chemical Society, Vol. 129, No. 5, 2007.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Effect of the methionine ligand on the reorganization energy of the type-1 copper site of nitrite Reductase
AU - Farver, Ole
AU - Wijma, Hein J.
AU - MacPherson, Iain
AU - Tocheva, Elitza I.
AU - Pecht, Israel
AU - Verbeet, Martin Ph.
AU - Murphy, Michael E. P.
AU - Canters, Gerard W.
PY - 2007
Y1 - 2007
N2 - Copper-containing nitrite reductase harbors a type-1 and a type-2 Cu site. The former acts as the electron acceptor site of the enzyme, and the latter is the site of catalytic action. The effect of the methionine ligand on the reorganization energy of the type-1 site was explored by studying the electron-transfer kinetics between NiR (wild type (wt) and the variants Met150Gly and Met150Thr) with Fe(II)EDTA and Fe(II)HEDTA. The mutations increased the reorganization energy by 0.3 eV (30 kJ mol-1). A similar increase was found from pulse radiolysis experiments on the wt NIR and three variants (Met150Gly, Met150His, and Met150Thr). Binding of the nearby Met62 to the type-1 Cu site in Met150Gly (under influence of an allosteric effector) lowered the reorganization energy back to approximately the wt value. According to XRD data the structure of the reduced type-1 site in Met150Gly NiR in the presence of an allosteric effector is similar to that in the reduced wt NiR (solved to 1.85 Å), compatible with the similarity in reorganization energy.
AB - Copper-containing nitrite reductase harbors a type-1 and a type-2 Cu site. The former acts as the electron acceptor site of the enzyme, and the latter is the site of catalytic action. The effect of the methionine ligand on the reorganization energy of the type-1 site was explored by studying the electron-transfer kinetics between NiR (wild type (wt) and the variants Met150Gly and Met150Thr) with Fe(II)EDTA and Fe(II)HEDTA. The mutations increased the reorganization energy by 0.3 eV (30 kJ mol-1). A similar increase was found from pulse radiolysis experiments on the wt NIR and three variants (Met150Gly, Met150His, and Met150Thr). Binding of the nearby Met62 to the type-1 Cu site in Met150Gly (under influence of an allosteric effector) lowered the reorganization energy back to approximately the wt value. According to XRD data the structure of the reduced type-1 site in Met150Gly NiR in the presence of an allosteric effector is similar to that in the reduced wt NiR (solved to 1.85 Å), compatible with the similarity in reorganization energy.
KW - Former Faculty of Pharmaceutical Sciences
U2 - 10.1021/ja064763j
DO - 10.1021/ja064763j
M3 - Journal article
C2 - 17227014
VL - 129
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
SN - 0002-7863
IS - 5
ER -
ID: 2288949