Effect of the methionine ligand on the reorganization energy of the type-1 copper site of nitrite Reductase

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

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

Harvard

Farver, O, Wijma, HJ, MacPherson, I, Tocheva, EI, Pecht, I, Verbeet, MP, Murphy, MEP & Canters, GW 2007, 'Effect of the methionine ligand on the reorganization energy of the type-1 copper site of nitrite Reductase', Journal of the American Chemical Society, vol. 129, no. 5. https://doi.org/10.1021/ja064763j

APA

Farver, O., Wijma, H. J., MacPherson, I., Tocheva, E. I., Pecht, I., Verbeet, M. P., Murphy, M. E. P., & Canters, G. W. (2007). Effect of the methionine ligand on the reorganization energy of the type-1 copper site of nitrite Reductase. Journal of the American Chemical Society, 129(5). https://doi.org/10.1021/ja064763j

Vancouver

Farver O, Wijma HJ, MacPherson I, Tocheva EI, Pecht I, Verbeet MP et al. Effect of the methionine ligand on the reorganization energy of the type-1 copper site of nitrite Reductase. Journal of the American Chemical Society. 2007;129(5). https://doi.org/10.1021/ja064763j

Author

Farver, Ole ; Wijma, Hein J. ; MacPherson, Iain ; Tocheva, Elitza I. ; Pecht, Israel ; Verbeet, Martin Ph. ; Murphy, Michael E. P. ; Canters, Gerard W. / Effect of the methionine ligand on the reorganization energy of the type-1 copper site of nitrite Reductase. In: Journal of the American Chemical Society. 2007 ; Vol. 129, No. 5.

Bibtex

@article{80b27480c2aa11dcbee902004c4f4f50,
title = "Effect of the methionine ligand on the reorganization energy of the type-1 copper site of nitrite Reductase",
abstract = "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 {\AA}), compatible with the similarity in reorganization energy.",
keywords = "Former Faculty of Pharmaceutical Sciences",
author = "Ole Farver and Wijma, {Hein J.} and Iain MacPherson and Tocheva, {Elitza I.} and Israel Pecht and Verbeet, {Martin Ph.} and Murphy, {Michael E. P.} and Canters, {Gerard W.}",
year = "2007",
doi = "10.1021/ja064763j",
language = "English",
volume = "129",
journal = "Journal of the American Chemical Society",
issn = "0002-7863",
publisher = "ACS Publications",
number = "5",

}

RIS

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