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Interaction of potassium cyanide with the [Ni-4Fe-5S] active site cluster of CO dehydrogenase from Carboxydothermus hydrogenoformans

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Interaction of potassium cyanide with the [Ni-4Fe-5S] active site cluster of CO dehydrogenase from Carboxydothermus hydrogenoformans. / Ha, Seung-Wook; Korbas, Malgorzata; Klepsch, Mirjam; Meyer-Klaucke, Wolfram; Meyer, Ortwin; Svetlitchnyi, Vitali.

In: J BIOL CHEM, Vol. 282, No. 14, 06.04.2007, p. 10639-46.

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

Harvard

Ha, S-W, Korbas, M, Klepsch, M, Meyer-Klaucke, W, Meyer, O & Svetlitchnyi, V 2007, 'Interaction of potassium cyanide with the [Ni-4Fe-5S] active site cluster of CO dehydrogenase from Carboxydothermus hydrogenoformans', J BIOL CHEM, vol. 282, no. 14, pp. 10639-46. https://doi.org/10.1074/jbc.M610641200

APA

Ha, S-W., Korbas, M., Klepsch, M., Meyer-Klaucke, W., Meyer, O., & Svetlitchnyi, V. (2007). Interaction of potassium cyanide with the [Ni-4Fe-5S] active site cluster of CO dehydrogenase from Carboxydothermus hydrogenoformans. J BIOL CHEM, 282(14), 10639-46. https://doi.org/10.1074/jbc.M610641200

Vancouver

Ha S-W, Korbas M, Klepsch M, Meyer-Klaucke W, Meyer O, Svetlitchnyi V. Interaction of potassium cyanide with the [Ni-4Fe-5S] active site cluster of CO dehydrogenase from Carboxydothermus hydrogenoformans. J BIOL CHEM. 2007 Apr 6;282(14):10639-46. https://doi.org/10.1074/jbc.M610641200

Bibtex

@article{ae70858b1a0b4cf697391e9d6a07ab33,
title = "Interaction of potassium cyanide with the [Ni-4Fe-5S] active site cluster of CO dehydrogenase from Carboxydothermus hydrogenoformans",
abstract = "The Ni-Fe carbon monoxide (CO) dehydrogenase II (CODHII(Ch)) from the anaerobic CO-utilizing hydrogenogenic bacterium Carboxydothermus hydrogenoformans catalyzes the oxidation of CO, presumably at the Ni-(micro(2)S)-Fe1 subsite of the [Ni-4S-5S] cluster in the active site. The CO oxidation mechanism proposed on the basis of several CODHII(Ch) crystal structures involved the apical binding of CO at the nickel ion and the activation of water at the Fe1 ion of the cluster. To understand how CO interacts with the active site, we have studied the reactivity of the cluster with potassium cyanide and analyzed the resulting type of nickel coordination by x-ray absorption spectroscopy. Cyanide acts as a competitive inhibitor of reduced CODHII(Ch) with respect to the substrate CO and is therefore expected to mimic the substrate. It inhibits the enzyme reversibly, forming a nickel cyanide. In this reaction, one of the four square-planar sulfur ligands of nickel is replaced by the carbon atom of cyanide, suggesting removal of the micro(2)S from the Ni-(micro(2)S)-Fe1 subsite. Upon reactivation of the inhibited enzyme, cyanide is released, and the square-planar coordination of nickel by 4S ligands is recovered, which includes the reformation of the Ni-(micro(2)S)-Fe1 bridge. The results are summarized in a model of the CO oxidation mechanism at the [Ni-4Fe-5S] active site cluster of CODHII(Ch) from C. hydrogenoformans.",
keywords = "Absorptiometry, Photon, Aldehyde Oxidoreductases, Bacterial Proteins, Binding Sites, Carbon Monoxide, Clostridium, Iron, Multienzyme Complexes, Nickel, Oxidation-Reduction, Potassium Cyanide, Sulfur, Journal Article, Research Support, Non-U.S. Gov't",
author = "Seung-Wook Ha and Malgorzata Korbas and Mirjam Klepsch and Wolfram Meyer-Klaucke and Ortwin Meyer and Vitali Svetlitchnyi",
year = "2007",
month = apr,
day = "6",
doi = "10.1074/jbc.M610641200",
language = "English",
volume = "282",
pages = "10639--46",
journal = "J BIOL CHEM",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "14",

}

RIS

TY - JOUR

T1 - Interaction of potassium cyanide with the [Ni-4Fe-5S] active site cluster of CO dehydrogenase from Carboxydothermus hydrogenoformans

AU - Ha, Seung-Wook

AU - Korbas, Malgorzata

AU - Klepsch, Mirjam

AU - Meyer-Klaucke, Wolfram

AU - Meyer, Ortwin

AU - Svetlitchnyi, Vitali

PY - 2007/4/6

Y1 - 2007/4/6

N2 - The Ni-Fe carbon monoxide (CO) dehydrogenase II (CODHII(Ch)) from the anaerobic CO-utilizing hydrogenogenic bacterium Carboxydothermus hydrogenoformans catalyzes the oxidation of CO, presumably at the Ni-(micro(2)S)-Fe1 subsite of the [Ni-4S-5S] cluster in the active site. The CO oxidation mechanism proposed on the basis of several CODHII(Ch) crystal structures involved the apical binding of CO at the nickel ion and the activation of water at the Fe1 ion of the cluster. To understand how CO interacts with the active site, we have studied the reactivity of the cluster with potassium cyanide and analyzed the resulting type of nickel coordination by x-ray absorption spectroscopy. Cyanide acts as a competitive inhibitor of reduced CODHII(Ch) with respect to the substrate CO and is therefore expected to mimic the substrate. It inhibits the enzyme reversibly, forming a nickel cyanide. In this reaction, one of the four square-planar sulfur ligands of nickel is replaced by the carbon atom of cyanide, suggesting removal of the micro(2)S from the Ni-(micro(2)S)-Fe1 subsite. Upon reactivation of the inhibited enzyme, cyanide is released, and the square-planar coordination of nickel by 4S ligands is recovered, which includes the reformation of the Ni-(micro(2)S)-Fe1 bridge. The results are summarized in a model of the CO oxidation mechanism at the [Ni-4Fe-5S] active site cluster of CODHII(Ch) from C. hydrogenoformans.

AB - The Ni-Fe carbon monoxide (CO) dehydrogenase II (CODHII(Ch)) from the anaerobic CO-utilizing hydrogenogenic bacterium Carboxydothermus hydrogenoformans catalyzes the oxidation of CO, presumably at the Ni-(micro(2)S)-Fe1 subsite of the [Ni-4S-5S] cluster in the active site. The CO oxidation mechanism proposed on the basis of several CODHII(Ch) crystal structures involved the apical binding of CO at the nickel ion and the activation of water at the Fe1 ion of the cluster. To understand how CO interacts with the active site, we have studied the reactivity of the cluster with potassium cyanide and analyzed the resulting type of nickel coordination by x-ray absorption spectroscopy. Cyanide acts as a competitive inhibitor of reduced CODHII(Ch) with respect to the substrate CO and is therefore expected to mimic the substrate. It inhibits the enzyme reversibly, forming a nickel cyanide. In this reaction, one of the four square-planar sulfur ligands of nickel is replaced by the carbon atom of cyanide, suggesting removal of the micro(2)S from the Ni-(micro(2)S)-Fe1 subsite. Upon reactivation of the inhibited enzyme, cyanide is released, and the square-planar coordination of nickel by 4S ligands is recovered, which includes the reformation of the Ni-(micro(2)S)-Fe1 bridge. The results are summarized in a model of the CO oxidation mechanism at the [Ni-4Fe-5S] active site cluster of CODHII(Ch) from C. hydrogenoformans.

KW - Absorptiometry, Photon

KW - Aldehyde Oxidoreductases

KW - Bacterial Proteins

KW - Binding Sites

KW - Carbon Monoxide

KW - Clostridium

KW - Iron

KW - Multienzyme Complexes

KW - Nickel

KW - Oxidation-Reduction

KW - Potassium Cyanide

KW - Sulfur

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1074/jbc.M610641200

DO - 10.1074/jbc.M610641200

M3 - SCORING: Journal article

C2 - 17277357

VL - 282

SP - 10639

EP - 10646

JO - J BIOL CHEM

JF - J BIOL CHEM

SN - 0021-9258

IS - 14

ER -