Characterization of the [NiFeSe] hydrogenase from Desulfovibrio vulgaris Hildenborough

Sónia Zacarias, Marisela Vélez, Marcos Pita, Antonio L. De Lacey, Pedro M. Matias, Inês A.C. Pereira

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

9 Citations (Scopus)


The [NiFeSe] hydrogenases are a subgroup of the well-characterized family of [NiFe] hydrogenases, in which a selenocysteine is a ligand to the nickel atom in the binuclear NiFe active site instead of cysteine. These enzymes display very interesting catalytic properties for biological hydrogen production and bioelectrochemical applications: high H2 production activity, bias for H2 evolution, low H2 inhibition, and some degree of O2 tolerance. Here we describe the methodologies employed to study the [NiFeSe] hydrogenase isolated from the sulfate-reducing bacteria D. vulgaris Hildenborough and the creation of a homologous expression system for production of variant forms of the enzyme.

Original languageEnglish
Title of host publicationMethods in Enzymology
EditorsFraser Armstrong
PublisherElsevier Academic Press Inc
Number of pages33
ISBN (Print)9780128163610
Publication statusPublished - 1 Jan 2018

Publication series

NameMethods in Enzymology
ISSN (Print)0076-6879
ISSN (Electronic)1557-7988


  • Desulfovibrio vulgaris Hildenborough
  • Hydrogen
  • Infrared spectroscopy
  • Oxygen tolerance
  • Selenocysteine
  • Sulfate-reducing bacteria
  • X-ray crystallography
  • [NiFeSe] hydrogenases


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