Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Original design of an oxygen-tolerant [NiFe] hydrogenase: major effect of a valine-to-cysteine mutation near the active site.

Journal of the American Chemical Society - 2 Feb 2011

Liebgott Pierre-Pol, de Lacey Antonio L, Burlat Bénédicte, Cournac Laurent, Richaud Pierre, Brugna Myriam, Fernandez Victor M, Guigliarelli Bruno, Rousset Marc, Léger Christophe, Dementin Sébastien

Abstract excerpt

Hydrogenases are efficient biological catalysts of H(2) oxidation and production. Most of them are inhibited by O(2), and a prerequisite for their use in biotechnological applications under air is to improve their oxygen tolerance. We have previously shown that exchanging the residue at position...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Aerobiosis
Share to Carbon Monoxide

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Deuterium Exchange Measurement

Share to Electrochemistry

Share to Gram-Negative Bacteria

Share to Hydrogen

Share to Hydrogenase

Share to Spectrum Analysis

Source

Identifiers

PMID: 21175174
DOI: 10.1021/ja108787s

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-21175174-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Original design of an oxygen-tolerant [NiFe] hydrogenase: major effect of a valine-to-cysteine mutation near the active site.PMID 21175174Read ↗

[NiFe]-hydrogenases revisited: nickel-carboxamido bond formation in a variant with accrued O2-tolerance and a tentative re-interpretation of Ni-SI states.Semantic proximity Read ↗

A glutamate is the essential proton transfer gate during the catalytic cycle of the [NiFe] hydrogenase.Semantic proximity Read ↗

Distal [FeS]-Cluster Coordination in [NiFe]-Hydrogenase Facilitates Intermolecular Electron Transfer.Semantic proximity Read ↗

O₂migration rates in [NiFe] hydrogenases. A joint approach combining free-energy calculations and kinetic modeling.Semantic proximity Read ↗

Mechanistic insight into the blocking of CO diffusion in [NiFe]-hydrogenase mutants through multiscale simulation.Semantic proximity Read ↗

Microbial hydrogen splitting in the presence of oxygen.Semantic proximity Read ↗

Principles of sustained enzymatic hydrogen oxidation in the presence of oxygen--the crucial influence of high potential Fe-S clusters in the electron relay of [NiFe]-hydrogenases.Semantic proximity Read ↗

[FeFe]- and [NiFe]-hydrogenase diversity, mechanism, and maturation.Semantic proximity Read ↗

Characterization of the Bottlenecks and Pathways for Inhibitor Dissociation from [NiFe] Hydrogenase.Semantic proximity Read ↗

Going beyond Structure: Nickel-Substituted Rubredoxin as a Mechanistic Model for the [NiFe] Hydrogenases.Semantic proximity Read ↗

Single-Amino Acid Modifications Reveal Additional Controls on the Proton Pathway of [FeFe]-Hydrogenase.Semantic proximity Read ↗

Insights into the structure of the active site of the O2-tolerant membrane bound [NiFe] hydrogenase of R. eutropha H16 by molecular modelling.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.