Exploring the gas access routes in a [NiFeSe] hydrogenase using crystals pressurized with krypton and oxygen

Sónia Zacarias, Adriana Temporão, Philippe Carpentier, Peter van der Linden, Inês A.C. Pereira, Pedro M. Matias

Research output: Contribution to journalArticlepeer-review

Abstract

Hydrogenases are metalloenzymes that catalyse both H2 evolution and uptake. They are gas-processing enzymes with deeply buried active sites, so the gases diffuse through channels that connect the active site to the protein surface. The [NiFeSe] hydrogenases are a special class of hydrogenases containing a selenocysteine as a nickel ligand; they are more catalytically active and less O2-sensitive than standard [NiFe] hydrogenases. Characterisation of the channel system of hydrogenases is important to understand how the inhibitor oxygen reaches the active site to cause oxidative damage. To this end, crystals of Desulfovibrio vulgaris Hildenborough [NiFeSe] hydrogenase were pressurized with krypton and oxygen, and a method for tracking labile O2 molecules was developed, for mapping a hydrophobic channel system similar to that of the [NiFe] enzymes as the major route for gas diffusion.

Original languageEnglish
Pages (from-to)863-874
Number of pages12
JournalJournal of Biological Inorganic Chemistry
Volume25
Issue number6
DOIs
Publication statusPublished - 1 Sep 2020

Keywords

  • Gas channels
  • High-pressure derivatization
  • Hydrogenase
  • Selenium

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