This article is missing information about taxonomic distribution of EC 1.3.1.33; InterPro refs for both. Please expand the article to include this information. Further details may exist on the talk page.(March 2022)
light-dependent protochlorophyllide reductase
Identifiers
EC no.
1.3.1.33
CAS no.
68518-04-7
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light-independent protochlorophyllide reductase
Crystallographic structure of heterooctamer of a dark-operative protochlorophyllide oxidoreductase from Prochlorococcus marinus.[1]
Identifiers
EC no.
1.3.7.7
Databases
IntEnz
IntEnz view
BRENDA
BRENDA entry
ExPASy
NiceZyme view
KEGG
KEGG entry
MetaCyc
metabolic pathway
PRIAM
profile
PDB structures
RCSB PDB PDBe PDBsum
Search
PMC
articles
PubMed
articles
NCBI
proteins
In enzymology, protochlorophyllide reductases (POR)[2][3] are enzymes that catalyze the conversion from protochlorophyllide to chlorophyllide a. They are oxidoreductases participating in the biosynthetic pathway to chlorophylls.[4][5]
There are two structurally unrelated proteins with this sort of activity, referred to as light-dependent (LPOR) and dark-operative (DPOR). The light- and NADPH-dependent reductase is part of the short-chain dehydrogenase/reductase (SDR) superfamily and is found in plants and oxygenic photosynthetic bacteria,[6][7] while the ATP-dependent dark-operative version is a completely different protein, consisting of three subunits that exhibit significant sequence and quaternary structure similarity to the three subunits of nitrogenase.[8] This enzyme may be evolutionary older; due to its bound iron-sulfur clusters is highly sensitive to free oxygen and does not function if the atmospheric oxygen concentration exceeds about 3%.[9] It is possible that evolutionary pressure associated with the great oxidation event resulted in the development of the light-dependent system.
The light-dependent version (EC 1.3.1.33) uses NADPH:
protochlorophyllide + NADPH + H+ chlorophyllide a + NADP+
While the light-independent or dark-operative version (EC 1.3.7.7) uses ATP and ferredoxin:[10][11][12]
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O = chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
^PDB: 2ynm; Moser J, Lange C, Krausze J, Rebelein J, Schubert WD, Ribbe MW, Heinz DW, Jahn D (2013). "Structure of ADP-aluminium fluoride-stabilized protochlorophyllide oxidoreductase complex". Proc Natl Acad Sci U S A. 110 (6): 2094–2098. Bibcode:2013PNAS..110.2094M. doi:10.1073/pnas.1218303110. PMC 3568340. PMID 23341615.
^Griffiths WT (1978). "Reconstitution of chlorophyllide formation by isolated etioplast membranes". Biochem. J. 174 (3): 681–92. doi:10.1042/bj1740681. PMC 1185970. PMID 31865.
^Apel K, Santel HJ, Redlinger TE, Falk H (1980). "The protochlorophyllide holochrome of barley (Hordeum vulgare L.) Isolation and characterization of the NADPH:protochlorophyllide oxidoreductase". Eur. J. Biochem. 111 (1): 251–8. doi:10.1111/j.1432-1033.1980.tb06100.x. PMID 7439188.
^Willows, Robert D. (2003). "Biosynthesis of chlorophylls from protoporphyrin IX". Natural Product Reports. 20 (6): 327–341. doi:10.1039/B110549N. PMID 12828371.
^Bollivar, David W. (2007). "Recent advances in chlorophyll biosynthesis". Photosynthesis Research. 90 (2): 173–194. doi:10.1007/s11120-006-9076-6. PMID 17370354. S2CID 23808539.
^Dong, Chen-Song; Zhang, Wei-Lun; Wang, Qiao; Li, Yu-Shuai; Wang, Xiao; Zhang, Min; Liu, Lin (2020-04-14). "Crystal structures of cyanobacterial light-dependent protochlorophyllide oxidoreductase". Proceedings of the National Academy of Sciences. 117 (15): 8455–8461. doi:10.1073/pnas.1920244117. ISSN 0027-8424. PMC 7165480. PMID 32234783.
^Yuichi Fujita and Carl E. Bauer (2000). Reconstitution of Light-independent Protochlorophyllide Reductase from Purified Bchl and BchN-BchB Subunits. J. Biol. Chem., Vol. 275, Issue 31, 23583-23588. [1]
^S.Yamazaki, J.Nomata, Y.Fujita (2006) Differential operation of dual protochlorophyllide reductases for chlorophyll biosynthesis in response to environmental oxygen levels in the cyanobacterium Leptolyngbya boryana. Plant Physiology, 2006, 142, 911-922 [2]
^Fujita Y, Matsumoto H, Takahashi Y, Matsubara H (March 1993). "Identification of a nifDK-like gene (ORF467) involved in the biosynthesis of chlorophyll in the cyanobacterium Plectonema boryanum". Plant & Cell Physiology. 34 (2): 305–14. PMID 8199775.
^Nomata J, Ogawa T, Kitashima M, Inoue K, Fujita Y (April 2008). "NB-protein (BchN-BchB) of dark-operative protochlorophyllide reductase is the catalytic component containing oxygen-tolerant Fe-S clusters". FEBS Letters. 582 (9): 1346–50. doi:10.1016/j.febslet.2008.03.018. PMID 18358835.
^Muraki N, Nomata J, Ebata K, Mizoguchi T, Shiba T, Tamiaki H, et al. (May 2010). "X-ray crystal structure of the light-independent protochlorophyllide reductase". Nature. 465 (7294): 110–4. Bibcode:2010Natur.465..110M. doi:10.1038/nature08950. PMID 20400946. S2CID 4427639.
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