ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2013
Influence of the protein structure surrounding the active site on the catalytic activity of [NiFeSe] hydrogenases.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 23 citations in OpenAlex.
- Selenium-More than Just a Fortuitous Sulfur Substitute in Redox Biology.Molecules (Basel, Switzerland) · 2023Review
- Studying OScientific reports · 2020Article
- HFrontiers in microbiology · 2019Article
- The direct role of selenocysteine in [NiFeSe] hydrogenase maturation and catalysis.Nature chemical biology · 2017Article
- H2 -Fueled ATP Synthesis on an Electrode: Mimicking Cellular Respiration.Angewandte Chemie (International ed. in English) · 2016Article
- Synthetic Active Site Model of the [NiFeSe] Hydrogenase.Chemistry (Weinheim an der Bergstrasse, Germany) · 2015Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
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Abstract
A combined experimental and theoretical study of the catalytic activity of a [NiFeSe] hydrogenase has been performed by H/D exchange mass spectrometry and molecular dynamics simulations. Hydrogenases are enzymes that catalyze the heterolytic cleavage or production of H2. The [NiFeSe] hydrogenases belong to a subgroup of the [NiFe] enzymes in which a selenocysteine is a ligand of the nickel atom in the active site instead of cysteine. The aim of this research is to determine how much the specific catalytic properties of this hydrogenase are influenced by the replacement of a sulfur by selenium in the coordination of the bimetallic active site versus the changes in the protein structure surrounding the active site. The pH dependence of the D2/H(+) exchange activity and the high isotope effect observed in the Michaelis constant for the dihydrogen substrate and in the single exchange/double exchange ratio suggest that a "cage effect" due to the protein structure surrounding the active site is modulating the enzymatic catalysis. This "cage effect" is supported by molecular dynamics simulations of the diffusion of H2 and D2 from the outside to the inside of the protein, which show different accumulation of these substrates in a cavity next to the active site.
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