Red chlorophyll catabolite reductase

Red chlorophyll catabolite reductase
Identifiers
EC no.1.3.7.12
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins
RCC_reductase
Identifiers
SymbolRCC_reductase
PfamPF06405
InterProIPR009439
Available protein structures:
PDB  IPR009439 PF06405 (ECOD; PDBsum)  
AlphaFold

The red chlorophyll catabolite reductase (RCC reductase) family of proteins consists of several reductase enzymes. They act together with pheophorbide a oxygenase to catalyse the cleavage of pheophorbide a to give stereoisomers of a compound which is the primary chlorophyll breakdown product as plants senesce.[1][2]

Function

Pheophorbide is a product of chlorophyll breakdown and a derivative of pheophytin where both the central magnesium ion has been removed and the phytol tail has been hydrolyzed.[3]

Two steps
 
 
Rightward reaction arrow
 
 
 

Red chlorophyll catabolite reductase acts while the product of pheophorbide a oxygenase (red chlorophyll catabolite) is still held within that protein.[4] The oxygenase is a Rieske protein containing an iron–sulfur cluster that requires reduced ferredoxin to function.[5] The reductase also requires ferredoxin.[6][7]

pheophorbide
 
Oxygenase
 
 
Rightward reaction arrow
 
 
 
2D representation of the chemical structure of Q27120845.
red chlorophyll catabolite
Reductase
 
 
Rightward reaction arrow
 
 
 
2D representation of the chemical structure of Q27120875.
primary fluorescent
chlorophyll catabolite

The fluorescent product can exist in two diastereomeric forms. All plants in a given genera produce a single isomer.[1][4]

References

  1. 1 2 Hörtensteiner S (2006). "Chlorophyll degradation during senescence". Annual Review of Plant Biology. 57: 55–77. doi:10.1146/annurev.arplant.57.032905.105212. PMID 16669755.
  2. ↑ Ougham H, Hörtensteiner S, Armstead I, Donnison I, King I, Thomas H, et al. (September 2008). "The control of chlorophyll catabolism and the status of yellowing as a biomarker of leaf senescence". Plant Biology. 10 Suppl 1: 4–14. doi:10.1111/j.1438-8677.2008.00081.x. PMID 18721307.
  3. ↑ Chen K, Preuss A, Hackbarth S, Wacker M, Langer K, Röder B (July 2009). "Novel photosensitizer-protein nanoparticles for photodynamic therapy: photophysical characterization and in vitro investigations". Journal of Photochemistry and Photobiology B: Biology. 96 (1): 66–74. doi:10.1016/j.jphotobiol.2009.04.006. PMID 19442534.
  4. 1 2 Pruzinská A, Anders I, Aubry S, Schenk N, Tapernoux-Lüthi E, Müller T, et al. (January 2007). "In vivo participation of red chlorophyll catabolite reductase in chlorophyll breakdown". The Plant Cell. 19 (1): 369–387. doi:10.1105/tpc.106.044404. PMC 1820978. PMID 17237353.
  5. ↑ Pruzinská A, Tanner G, Anders I, Roca M, Hörtensteiner S (December 2003). "Chlorophyll breakdown: pheophorbide a oxygenase is a Rieske-type iron-sulfur protein, encoded by the accelerated cell death 1 gene". Proceedings of the National Academy of Sciences of the United States of America. 100 (25): 15259–15264. doi:10.1073/pnas.2036571100. PMC 299977. PMID 14657372.
  6. ↑ Enzyme 1.3.7.12 at KEGG Pathway Database.
  7. ↑ Wüthrich KL, Bovet L, Hunziker PE, Donnison IS, Hörtensteiner S (January 2000). "Molecular cloning, functional expression and characterisation of RCC reductase involved in chlorophyll catabolism". The Plant Journal. 21 (2): 189–198. doi:10.1046/j.1365-313x.2000.00667.x. PMID 10743659.
This article incorporates text from the public domain Pfam and InterPro: IPR009439