The Model [NiFe]-Hydrogenases of Escherichia coli

F. Sargent (Lead / Corresponding author)

Research output: Chapter in Book/Report/Conference proceedingChapter (peer-reviewed)

41 Citations (Scopus)

Abstract

In Escherichia coli, hydrogen metabolism plays a prominent role in anaerobic physiology. The genome contains the capability to produce and assemble up to four [NiFe]-hydrogenases, each of which are known, or predicted, to contribute to different aspects of cellular metabolism. In recent years, there have been major advances in the understanding of the structure, function, and roles of the E. coli [NiFe]-hydrogenases. The membrane-bound, periplasmically oriented, respiratory Hyd-1 isoenzyme has become one of the most important paradigm systems for understanding an important class of oxygen-tolerant enzymes, as well as providing key information on the mechanism of hydrogen activation per se. The membrane-bound, periplasmically oriented, Hyd-2 isoenzyme has emerged as an unusual, bidirectional redox valve able to link hydrogen oxidation to quinone reduction during anaerobic respiration, or to allow disposal of excess reducing equivalents as hydrogen gas. The membrane-bound, cytoplasmically oriented, Hyd-3 isoenzyme is part of the formate hydrogenlyase complex, which acts to detoxify excess formic acid under anaerobic fermentative conditions and is geared towards hydrogen production under those conditions. Sequence identity between some Hyd-3 subunits and those of the respiratory NADH dehydrogenases has led to hypotheses that the activity of this isoenzyme may be tightly coupled to the formation of transmembrane ion gradients. Finally, the E. coli genome encodes a homologue of Hyd-3, termed Hyd-4, however strong evidence for a physiological role for E. coli Hyd-4 remains elusive. In this review, the versatile hydrogen metabolism of E. coli will be discussed and the roles and potential applications of the spectrum of different types of [NiFe]-hydrogenases available will be explored.

Original languageEnglish
Title of host publicationAdvances in Bacterial Electron Transport Systems and Their Regulation
EditorsRobert K. Poole
Place of PublicationLondon
PublisherElsevier
Pages433-507
Number of pages75
ISBN (Electronic)9780128052396
ISBN (Print)9780128048238
DOIs
Publication statusPublished - 5 May 2016

Publication series

NameAdvances in Microbial Physiology
Volume68
ISSN (Print)0065-2911

Keywords

  • Bacterial membrane biology
  • Biohydrogen production
  • Escherichia coli
  • Formate hydrogenlyase
  • Respiratory hydrogen oxidation
  • [NiFe]-hydrogenase

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    Cite this

    Sargent, F. (2016). The Model [NiFe]-Hydrogenases of Escherichia coli. In R. K. Poole (Ed.), Advances in Bacterial Electron Transport Systems and Their Regulation (pp. 433-507). (Advances in Microbial Physiology; Vol. 68). Elsevier. https://doi.org/10.1016/bs.ampbs.2016.02.008