Role for the nitrogenase MoFe protein alpha-subunit in FeMo-cofactor binding and catalysis.

doi:10.1038/343188a0

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

Back to search

Article

Role for the nitrogenase MoFe protein alpha-subunit in FeMo-cofactor binding and catalysis.

Nature - 11 Jan 1990

Scott D J, May H D, Newton W E, Brigle K E, Dean D R

Abstract excerpt

Two components constitute Mo-dependent nitrogenase (EC 1.18.6.1)--the Fe protein (a homodimer encoded by nifH) and the MoFe protein (an alpha 2 beta 2 tetramer encoded by nifDK). The MoFe protein provides the substrate-binding site and probably contains six prosthetic groups of two types--four Fe...

Topics

Amino Acid Sequence
Azotobacter
Base Sequence
Electron Spin Resonance Spectroscopy
Ferredoxins
Genes, Bacterial
Macromolecular Substances
Molecular Sequence Data
Molybdoferredoxin
Mutation
Nitrogen Fixation
Nitrogenase
Oligonucleotide Probes
Protein Binding
Sequence Homology, Nucleic Acid

Source

Open in PubMed

Identifiers

PMID: 2153269
DOI: 10.1038/343188a0

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-2153269-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics