Study of the localization of the cofactor-binding centre in the nitrogenase Mo-Fe-protein by the triplet probe method

S. Yu Druzhinin; V. R. Fogel'; L. A. Syrtsova; A. I. Kotel'nikov; G. I. Likhtenshtein

Study of the localization of the cofactor-binding centre in the nitrogenase Mo-Fe-protein by the triplet probe method

S. Yu Druzhinin, V. R. Fogel', L. A. Syrtsova, A. I. Kotel'nikov, G. I. Likhtenshtein

Research output: Contribution to journal › Article › peer-review

Abstract

An approach is developed permitting by the triplet probe method to study the localization of the cofactors in enzymes and the nature of their protein ligands. With this approach it is shown that the Fe-Mo cofactor of the nitrogenase enzyme is situated close to the surface of the protein globule and is partially accessible to triplet probes in solution. The accessible histidine and amino groups do not form part of the centre binding the cofactor.

Original language	English
Pages (from-to)	13-18
Number of pages	6
Journal	Biophysics (Russian Federation)
Volume	31
Issue number	1
State	Published - 1 Dec 1986
Externally published	Yes

ASJC Scopus subject areas

Biophysics

Cite this

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abstract = "An approach is developed permitting by the triplet probe method to study the localization of the cofactors in enzymes and the nature of their protein ligands. With this approach it is shown that the Fe-Mo cofactor of the nitrogenase enzyme is situated close to the surface of the protein globule and is partially accessible to triplet probes in solution. The accessible histidine and amino groups do not form part of the centre binding the cofactor.",

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AU - Druzhinin, S. Yu

AU - Fogel', V. R.

AU - Syrtsova, L. A.

AU - Kotel'nikov, A. I.

AU - Likhtenshtein, G. I.

PY - 1986/12/1

Y1 - 1986/12/1

N2 - An approach is developed permitting by the triplet probe method to study the localization of the cofactors in enzymes and the nature of their protein ligands. With this approach it is shown that the Fe-Mo cofactor of the nitrogenase enzyme is situated close to the surface of the protein globule and is partially accessible to triplet probes in solution. The accessible histidine and amino groups do not form part of the centre binding the cofactor.

AB - An approach is developed permitting by the triplet probe method to study the localization of the cofactors in enzymes and the nature of their protein ligands. With this approach it is shown that the Fe-Mo cofactor of the nitrogenase enzyme is situated close to the surface of the protein globule and is partially accessible to triplet probes in solution. The accessible histidine and amino groups do not form part of the centre binding the cofactor.

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Study of the localization of the cofactor-binding centre in the nitrogenase Mo-Fe-protein by the triplet probe method

Abstract

ASJC Scopus subject areas

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