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

Improved O2-tolerance in variants of a H2-evolving [NiFe]-hydrogenase from Klebsiella oxytoca HP1.

FEBS letters - 2 Apr 2015

Huang Gang-Feng, Wu Xiao-Bing, Bai Li-Ping, Liu Ke, Jiang Li-Jing, Long Min-Nan, Chen Qing-Xi

Abstract excerpt

In this study, we investigated the mechanism of O2 tolerance of Klebsiella oxytoca HP1 H2-evolving hydrogenase 3 (KHyd3) by mutational analysis and three-dimensional structure modeling. Results revealed that certain surface amino acid residues of KHyd3 large subunit, in particular those at the outer entrance of the gas channel, have a visible effect on its oxygen tolerance. Additionally, solution pH,...

Read the complete abstract on PubMed

Topics

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

Share to Anaerobiosis
Share to Biocatalysis
Share to Dose-Response Relationship, Drug

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrogen

Share to Hydrogen-Ion Concentration

Share to Hydrogenase

Share to Oxygen

Share to Protein Subunits

Source

Identifiers

PMID: 25747389
DOI: 10.1016/j.febslet.2015.02.027

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Improved O2-tolerance in variants of a H2-evolving [NiFe]-hydrogenase from Klebsiella oxytoca HP1.PMID 25747389Read ↗

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

Microbial hydrogen splitting in the presence of oxygen.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 ↗

Hydrogen-producing conditions and mutation mechanisms of a highly efficient mutant strain Ethanoligenens harbinense YR-3.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 ↗

An archaeal transcription factor EnfR with a novel 'eighth note' fold controls hydrogen production of a hyperthermophilic archaeon Thermococcus onnurineus NA1.Semantic proximity Read ↗

[FeFe] hydrogenases and their evolution: a genomic perspective.Semantic proximity Read ↗

Distinct physiological roles of the three [NiFe]-hydrogenase orthologs in the hyperthermophilic archaeon Thermococcus kodakarensis.Semantic proximity Read ↗

Investigation of Cyc1 protein structure stability after H53I mutation using computational approaches to improve redox potential.Semantic proximity Read ↗

[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 ↗

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

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