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

In vivo participation of red chlorophyll catabolite reductase in chlorophyll breakdown.

The Plant cell - 1 Jan 2007

Pruzinská Adriana, Anders Iwona, Aubry Sylvain, Schenk Nicole, Tapernoux-Lüthi Esther, Müller Thomas, Kräutler Bernhard, Hörtensteiner Stefan

Abstract excerpt

A central reaction of chlorophyll breakdown, porphyrin ring opening of pheophorbide a to the primary fluorescent chlorophyll catabolite (pFCC), requires pheophorbide a oxygenase (PAO) and red chlorophyll catabolite reductase (RCCR), with red chlorophyll catabolite (RCC) as a presumably PAO-bound...

Read the complete abstract on PubMed

Topics

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

Share to Apoptosis Regulatory Proteins
Share to Chlorophyll
Share to Fluorescence

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Conformation

Share to Mutagenesis, Insertional

Share to Oxidoreductases

Share to Oxygenases

Share to Pigments, Biological

Source

Open in PubMed Open full text

Identifiers

PMID: 17237353
DOI: 10.1105/tpc.106.044404
PMCID: PMC1820978

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-17237353-2026-09-02.2. 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

In vivo participation of red chlorophyll catabolite reductase in chlorophyll breakdown.PMID 17237353Read ↗

Chlorophyll breakdown in senescent Arabidopsis leaves. Characterization of chlorophyll catabolites and of chlorophyll catabolic enzymes involved in the degreening reaction.Semantic proximity Read ↗

Chlorophyll degradation during senescence.Semantic proximity Read ↗

The control of chlorophyll catabolism and the status of yellowing as a biomarker of leaf senescence.Semantic proximity Read ↗

Chlorophyll breakdown: pheophorbide a oxygenase is a Rieske-type iron-sulfur protein, encoded by the accelerated cell death 1 gene.Semantic proximity Read ↗

Knockdown of OsPAO and OsRCCR1 cause different plant death phenotypes in rice.Semantic proximity Read ↗

Pheophorbide a May Regulate Jasmonate Signaling during Dark-Induced Senescence.Semantic proximity Read ↗

Upregulated expression of RESPIRATORY BURST OXIDASE HOMOLOG D underlies lesion-mimic phenotype in dark-treated Arabidopsis pheide a oxygenase mutant leaves.Semantic proximity Read ↗

Suppression of Chloroplastic Alkenal/One Oxidoreductase Represses the Carbon Catabolic Pathway in Arabidopsis Leaves during Night.Semantic proximity Read ↗

Rice 7-Hydroxymethyl Chlorophyll a Reductase Is Involved in the Promotion of Chlorophyll Degradation and Modulates Cell Death Signaling.Semantic proximity Read ↗

A comparative analysis of the NADPH thioredoxin reductase C-2-Cys peroxiredoxin system from plants and cyanobacteria.Semantic proximity Read ↗

Redox-control of chlorophyll biosynthesis mainly depends on thioredoxins.Semantic proximity Read ↗

Overexpression of protochlorophyllide oxidoreductase C regulates oxidative stress in Arabidopsis.Semantic proximity Read ↗

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