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 proceedingChapter

4 Citations (Scopus)

Abstract

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
Pages169-201
Number of pages33
ISBN (Print)9780128163610
DOIs
Publication statusPublished - 1 Jan 2018

Publication series

NameMethods in Enzymology
Volume613
ISSN (Print)0076-6879
ISSN (Electronic)1557-7988

Keywords

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

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