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Biochemistry (Moscow)

, Volume 73, Issue 2, pp 171–177 | Cite as

Formation of a cross-linking complex of dinitrogenase reductase-activating glycohydrolase (DRAG) with membrane proteins from Rhodospirillum rubrum chromatophores

  • N. AkentievaEmail author
Article

Abstract

Association of dinitrogenase reductase-activating glycohydrolase (DRAG) with membrane proteins of chromatophores has been investigated. The formation of a multicomponent complex between DRAG and membrane proteins was demonstrated in the presence of glutaraldehyde and EDC/NHS (N-(3-dimethylaminopropyl)-N′-ethylcarbodiimide hydrochloride/hydroxy-2,5-dioxopyrrolidine-3-sulfonic acid sodium salt). Complex formation was observed both in native chromatophore membrane and in chromatophores treated with 0.5 M NaCl in the presence of homogeneous DRAG and glutaraldehyde in cross-reaction. The molecular weight of the complex was around 200 kD, which is consistent with the association of DRAG with three or more chromatophore membrane proteins. A specific complex with molecular weight of about 75 kD was formed only in the presence of EDC/NHS in the cross-linking reaction. It was demonstrated that ammonium transport protein and P11 protein are possible candidates for association with DRAG in chromatophore membranes.

Key words

nitrogen fixation nitrogenase dinitrogenase reductase-activating glycohydrolase cross-linking complex membranes 

Abbreviations

DRAG

dinitrogenase reductase-activating gly-cohydrolase

DRAT

dinitrogenase reductase-ADP-ribosyl-transferase

EDC

N-(3-dimethylaminopropyl)-N′-ethylcar-bodiimide hydrochloride

IPTG

isopropyl β-D-thiogalactopy-ranoside

LB

Luria-Bertani medium

PVDF

Tropifluor™ polyvinylidene difluoride membrane

sulfo-NHS

hydroxy-2,5-dioxopyrrolidine-3-sulfonic acid sodium salt

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Copyright information

© Pleiades Publishing, Ltd. 2008

Authors and Affiliations

  1. 1.Washington University in Saint LouisSaint LouisUSA

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