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

Site-directed mutagenesis of cytochrome c shows that an invariant Phe is not essential for function.

Nature - 1 Jan 2000

Pielak G J, Mauk A G, Smith M

Abstract excerpt

Phenylalanine 87 of yeast iso-1-cytochrome c (Phe 82 in horse heart and bonito) is phylogenetically conserved and occurs near the surface of the protein. It has been suggested that this residue is directly involved in electron transfer between cytochrome c and cytochrome c peroxidase (CCP) and ma...

Topics

Amino Acid Sequence
Cytochrome c Group
Electron Transport
Mutation
Phenylalanine
Saccharomyces cerevisiae
Structure-Activity Relationship

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 2981414
DOI: 10.1038/313152a0

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-2981414-2026-08-30.1. 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.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Site-directed mutagenesis of cytochrome c shows that an invariant Phe is not essential for function.PMID 2981414Read ↗

The function of the Saccharomyces cerevisiae iso-1-cytochrome c gene is independent of the codon at invariant residue Phe82 when the gene is present on a low-copy-number vector.Semantic proximity Read ↗

Temperature-sensitive variants of Saccharomyces cerevisiae iso-1-cytochrome c produced by random mutagenesis of codons 43 to 54.Semantic proximity Read ↗

Exploring the interface between the N- and C-terminal helices of cytochrome c by random mutagenesis within the C-terminal helix.Semantic proximity Read ↗

Replacement of cysteine-107 of Saccharomyces cerevisiae iso-1-cytochrome c with threonine: improved stability of the mutant protein.Semantic proximity Read ↗

Functional mapping reveals the importance of yeast cytochrome b C-terminal region in assembly and function of the bc1 complex.Semantic proximity Read ↗

Effect of active site and surface mutations on the reduction potential of yeast cytochrome c peroxidase and spectroscopic properties of the oxidized and reduced enzyme.Semantic proximity Read ↗

The importance of mutation, then and now: studies with yeast cytochrome c.Semantic proximity Read ↗

Structural and functional characterization of phosphomimetic mutants of cytochrome c at threonine 28 and serine 47.Semantic proximity Read ↗

Mutant Cytochrome C as a Potential Detector of Superoxide Generation: Effect of Mutations on the Function and Properties.Semantic proximity Read ↗

QO site deficiency can be compensated by extragenic mutations in the hinge region of the iron-sulfur protein in the bc1 complex of Saccharomyces cerevisiae.Semantic proximity Read ↗

Rational design of a more stable yeast iso-1-cytochrome c.Semantic proximity Read ↗

Replacement of an electron transfer pathway in cytochrome c peroxidase with a surrogate peptide.Semantic proximity Read ↗

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