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Journal of Bacteriology, March 2005, p. 1937-1944, Vol. 187, No. 6
0021-9193/05/$08.00+0     doi:10.1128/JB.187.6.1937-1944.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Menaquinone-Specific Prenyl Reductase from the Hyperthermophilic Archaeon Archaeoglobus fulgidus

Hisashi Hemmi,* Yoshihiro Takahashi, Kyohei Shibuya, Toru Nakayama, and Tokuzo Nishino

Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University, Sendai, Miyagi, Japan

Received 12 August 2004/ Accepted 19 October 2004

Four genes that encode the homologues of plant geranylgeranyl reductase were isolated from a hyperthermophilic archaeon Archaeoglobus fulgidus, which produces menaquinone with a fully saturated heptaprenyl side chain, menaquinone-7(14H). The recombinant expression of one of the homologues in Escherichia coli led to a distinct change in the quinone profile of the host cells, although the homologue is the most distantly related to the geranylgeranyl reductase. The new compounds found in the profile had successively longer elution times than those of ordinary quinones from E. coli, i.e., menaquinone-8 and ubiquinone-8, in high-performance liquid chromatography on a reversed-phase column. Structural analyses of the new compounds by electron impact-mass spectrometry indicated that their molecular masses progressively increase relative to the ordinary quinones at a rate of 2 U but that they still contain quinone head structures, strongly suggesting that the compounds are quinones with partially saturated prenyl side chains. In vitro assays with dithionite as the reducing agent showed that the prenyl reductase is highly specific for menaquinone-7, rather than ubiquinone-8 and prenyl diphosphates. This novel enzyme noncovalently binds flavin adenine dinucleotide, similar to geranylgeranyl reductase, but was not able to utilize NAD(P)H as the electron donor, unlike the plant homologue.

* Corresponding author. Mailing address: Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University, Aoba-yama 07, Sendai, Miyagi 980-8579, Japan. Phone: 81-22-217-7272. Fax: 81-22-217-7293. E-mail: hhemmi{at}seika.che.tohoku.ac.jp.

Journal of Bacteriology, March 2005, p. 1937-1944, Vol. 187, No. 6
0021-9193/05/$08.00+0     doi:10.1128/JB.187.6.1937-1944.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Lee, P. C., Salomon, C., Mijts, B., Schmidt-Dannert, C. (2008). Biosynthesis of Ubiquinone Compounds with Conjugated Prenyl Side Chains. Appl. Environ. Microbiol. 74: 6908-6917 [Abstract] [Full Text]  
  • Gomez Maqueo Chew, A., Frigaard, N.-U., Bryant, D. A. (2008). Identification of the bchP Gene, Encoding Geranylgeranyl Reductase in Chlorobaculum tepidum. J. Bacteriol. 190: 747-749 [Abstract] [Full Text]  
  • Nishimura, Y., Eguchi, T. (2006). Biosynthesis of Archaeal Membrane Lipids: Digeranylgeranylglycerophospholipid Reductase of the Thermoacidophilic Archaeon Thermoplasma acidophilum. J Biochem 139: 1073-1081 [Abstract] [Full Text]  


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