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

Role of methionine-239, an amino acid residue in the mobile-loop region of the NADH-binding domain (domain I) of proton-translocating transhydrogenase.

Biochemistry - 2 Dec 1997

Grimley R L, Quirk P G, Bizouarn T, Thomas C M, Jackson J B

Abstract excerpt

Transhydrogenase couples the transfer of hydride equivalents between NAD(H) and NADP(H) to proton translocation across a membrane. The one-dimensional proton NMR spectrum of the recombinant NAD(H)-binding domain (domain I) of transhydrogenase from Rhodospirillum rubrum reveals well-defined resona...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Binding Sites
Share to Biological Transport

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Catalysis

Share to Methionine

Share to Molecular Sequence Data

Share to Mutation

Share to Protein Conformation

Source

Identifiers

PMID: 9398196
DOI: 10.1021/bi971832l

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-9398196-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Role of methionine-239, an amino acid residue in the mobile-loop region of the NADH-binding domain (domain I) of proton-translocating transhydrogenase.PMID 9398196Read ↗

Mutations at tyrosine-235 in the mobile loop region of domain I protein of transhydrogenase from Rhodospirillum rubrum strongly inhibit hydride transfer.Semantic proximity Read ↗

The role of invariant amino acid residues at the hydride transfer site of proton-translocating transhydrogenase.Semantic proximity Read ↗

Redox-sensitive loops D and E regulate NADP(H) binding in domain III and domain I-domain III interactions in proton-translocating Escherichia coli transhydrogenase.Semantic proximity Read ↗

A change in ionization of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase regulates both hydride transfer and nucleotide release.Semantic proximity Read ↗

Roles of individual amino acids in helix 14 of the membrane domain of proton-translocating transhydrogenase from Escherichia coli as deduced from cysteine mutagenesis.Semantic proximity Read ↗

Identification of a region involved in the communication between the NADP(H) binding domain and the membrane domain in proton pumping E. coli transhydrogenase.Semantic proximity Read ↗

Essential glycine in the proton channel of Escherichia coli transhydrogenase.Semantic proximity Read ↗

Proton-translocating nicotinamide nucleotide transhydrogenase of Escherichia coli. Involvement of aspartate 213 in the membrane-intercalating domain of the beta subunit in energy transduction.Semantic proximity Read ↗

Critical Role of Water Molecules in Proton Translocation by the Membrane-Bound Transhydrogenase.Semantic proximity Read ↗

Review and Hypothesis. New insights into the reaction mechanism of transhydrogenase: Swivelling the dIII component may gate the proton channel.Semantic proximity Read ↗

Functional split and crosslinking of the membrane domain of the beta subunit of proton-translocating transhydrogenase from Escherichia coli.Semantic proximity Read ↗

Roles of subunit NuoL in the proton pumping coupling mechanism of NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli.Semantic proximity Read ↗

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