Look on the positive side! The orientation, identification and bioenergetics of 'Archaeal' membrane-bound nitrate reductases

Rosa Maria Martinez-Espinosa, Elizabeth J. Dridge, Maria J. Bonete, Julea N. Butt, Clive S. Butler, Frank Sargent, David J. Richardson

    Research output: Contribution to journalReview article

    81 Citations (Scopus)

    Abstract

    Many species of Bacteria and Archaea respire nitrate using a molybdenum-dependent membrane-bound respiratory system called Nar. Classically, the 'Bacterial' Nar system is oriented such that nitrate reduction takes place on the inside of this membrane. However, the active site subunit of the 'Archaeal' Nar systems has a twin arginine ('RR') motif, which is a suggestion of translocation to the outside of the cytoplasmic membrane. These 'Archaeal' type of nitrate reductases are part of a group of molybdoenzymes with an 'RR' motif that are predicted to have an aspartate ligand to the molybdenum ion. This group includes selenate reductases and possible sequence signatures are described that serve to distinguish the Nar nitrate reductases from the selenate reductases. The 'RR' sequences of nitrate reductases of Archaea and some that have recently emerged in Bacteria are also considered and it is concluded that there is good evidence for there being both Archaeal and Bacterial examples of Nar-type nitrate reductases with an active site on the outside of the cytoplasmic membrane. Finally, the bioenergetic consequences of nitrate reduction on the outside of the cytoplasmic membrane have been explored.

    Original languageEnglish
    Pages (from-to)129-139
    Number of pages11
    JournalFEMS Microbiology Letters
    Volume276
    Issue number2
    DOIs
    Publication statusPublished - Nov 2007

    Cite this

    Martinez-Espinosa, R. M., Dridge, E. J., Bonete, M. J., Butt, J. N., Butler, C. S., Sargent, F., & Richardson, D. J. (2007). Look on the positive side! The orientation, identification and bioenergetics of 'Archaeal' membrane-bound nitrate reductases. FEMS Microbiology Letters, 276(2), 129-139. https://doi.org/10.1111/j.1574-6968.2007.00887.x