プラストキノール・プラストシアニン還元酵素、プラストキノール・プラストシアニンレダクターゼ
WordNet
- an enzyme that catalyses the biochemical reduction of some specified substance
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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/07/24 21:31:46」(JST)
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| Cytochrome b6f complex | |||||||||
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Crystal structure of the cytochrome b6f complex from C. reinhardtii (1q90). Hydrocarbon boundaries of the lipid bilayer are shown by red and blue dots.
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| EC number | 1.10.99.1 | ||||||||
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| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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The cytochrome b6f complex (plastoquinol—plastocyanin reductase; EC 1.10.99.1) is an enzyme found in the thylakoid membrane in chloroplasts of plants, cyanobacteria, and green algae, catalyzing the transfer of electrons from plastoquinol to plastocyanin.[1] The reaction is analogous to the reaction catalyzed by cytochrome bc1 (Complex III) of the mitochondrial electron transport chain. For photosynthesis, the cytochrome b6f complex transfers electrons between the two reaction complexes from Photosystem II to Photosystem I, whereby introducing protons into the thylakoid space to generate an electrochemical gradient [2] that stores energy for ATP synthesis.
Contents
- 1 Enzyme structure
- 2 Biological function
- 3 Reaction mechanism
- 3.1 Q cycle
- 3.2 Cyclic electron transfer
- 4 References
- 5 External links
Enzyme structure
The cytochrome b6f complex is a dimer, with each monomer composed of eight subunits.[3] These consist of four large subunits: a 32 kDa cytochrome f with a c-type cytochrome, a 25 kDa cytochrome b6 with a low- and high-potential heme group, a 19 kDa Rieske iron-sulfur protein containing a [2Fe-2S] cluster, and a 17 kDa subunit IV; along with four small subunits (3-4 kDa): PetG, PetL, PetM, and PetN.[3][4] The total molecular weight is 217 kDa.
The crystal structure of cytochrome b6f complexes from Chlamydomonas reinhardtii, Mastigocladus laminosus, and Nostoc sp. PCC 7120 have been determined.[2][5][6][7][8][9]
The core of the complex is structurally similar to cytochrome bc1 core. Cytochrome b6 and subunit IV are homologous to cytochrome b[10] and the Rieske iron-sulfur proteins of the two complexes are homologous.[11] However, cytochrome f and cytochrome c1 are not homologous.[12]
Cytochrome b6f contains seven prosthetic groups.[13][14] Four are found in both cytochrome b6f and bc1: the c-type heme of cytochrome c1 and f, the two b-type hemes (bp and bn) in bc1 and b6f, and the [2Fe-2S] cluster of the Rieske protein. Three unique prosthetic groups are found in cytochrome b6f: chlorophyll a, β-carotene, and heme cn (also known as heme x).[5]
The inter-monomer space within the core of the cytochrome b6f complex dimer is occupied by lipids,[9] which provides directionality to heme-heme electron transfer through modulation of the intra-protein dielectric environment.[15]
Biological function
In photosynthesis, the cytochrome b6f complex functions to mediate the transfer of electrons between the two photosynthetic reaction center complexes, from Photosystem II to Photosystem I, while transferring protons from the chloroplast stroma across the thylakoid membrane into the lumen.[2] Electron transport via cytochrome b6f is responsible for creating the proton gradient that drives the synthesis of ATP in chloroplasts.[4]
In a separate reaction, the cytochrome b6f complex plays a central role in cyclic photophosphorylation, when NADP+ is not available to accept electrons from reduced ferredoxin.[1] This cycle results in the creation of a proton gradient by cytochrome b6f, which can be used to drive ATP synthesis. It has also been shown that this cycle is essential for photosynthesis,[16] in which it is proposed to help maintain the proper ratio of ATP/NADPH production for carbon fixation.[17][18]
The p-side quinol deprotonation-oxidation reactions within the cytochrome b6f complex have been implicated in the generation of reactive oxygen species.[19] An integral chlorophyll molecule located within the quinol oxidation site has been suggested to perform a structural, non-photochemical function in enhancing the rate of formation of the reactive oxygen species, possibly to provide a redox-pathway for intra-cellular communication.[20]
Reaction mechanism
The cytochrome b6f complex is responsible for "non-cyclic" (1) and "cyclic" (2) electron transfer between two mobile redox carriers, plastoquinone (QH2) and plastocyanin (Pc):
| H2O | → | photosystem II | → | QH2 | → | Cyt b6f | → | Pc | → | photosystem I | → | NADPH | (1) |
| QH2 | → | Cyt b6f | → | Pc | → | photosystem I | → | Q | (2) | ||||
Cytochrome b6f catalyzes the transfer of electrons from plastoquinol to plastocyanin, while pumping two protons from the stroma into the thylakoid lumen:
- QH2 + 2Pc(Cu2+) + 2H+ (stroma) → Q + 2Pc(Cu+) + 4H+ (lumen)[1]
This reaction occurs through the Q cycle as in Complex III.[21] Plastoquinone acts as the electron carrier, transferring its two electrons to high- and low-potential electron transport chains (ETC) via a mechanism called electron bifurcation.[22]
Q cycle
Q cycle of cytochrome b6f
First half of Q cycle
- QH2 binds to the positive 'p' side (lumen side) of the complex. It is oxidized to a semiquinone (SQ) by the iron-sulfur center (high-potential ETC) and releases two protons to the thylakoid lumen.
- The reduced iron-sulfur center transfers its electron through cytochrome f to Pc.
- In the low-potential ETC, SQ transfers its electron to heme bp of cytochrome b6.
- Heme bp then transfers the electron to heme bn.
- Heme bn reduces Q with one electron to form SQ.
Second half of Q cycle
- A second QH2 binds to the complex.
- In the high-potential ETC, one electron reduces another oxidized Pc.
- In the low-potential ETC, the electron from heme bn is transferred to SQ, and the completely reduced Q2− takes up two protons from the stroma to form QH2.
- The oxidized Q and the reduced QH2 that has been regenerated diffuse into the membrane.
Cyclic electron transfer
In contrast to Complex III, cytochrome b6f catalyzes another electron transfer reaction that is central to cyclic photophosphorylation. The electron from ferredoxin (Fd) is transferred to plastoquinone and then the cytochrome b6f complex to reduce plastocyanin, which is reoxidized by P700 in Photosystem I.[23] The exact mechanism for how plastoquinone is reduced by ferredoxin is still under investigation. One proposal is that there exists a ferredoxin:plastoquinone-reductase or an NADP dehydrogenase.[23] Since heme x does not appear to be required for the Q cycle and is not found in Complex III, it has been proposed that it is used for cyclic photophosphorylation by the following mechanism:[22][24]
- Fd (red) + heme x (ox) → Fd (ox) + heme x (red)
- heme x (red) + Fd (red) + Q + 2H+ → heme x (ox) + Fd (ox) + QH2
References
- ^ a b c Berg, Jeremy M. (Jeremy M.); Tymoczko, John L.; Stryer, Lubert.; Stryer, Lubert. Biochemistry. (2007). Biochemistr. New York: W.H. Freeman. ISBN 978-0-7167-8724-2.
- ^ a b c Hasan, SS.; Yamashita, E.; Baniulis, D.; Cramer, WA. (Feb 2013). "Quinone-dependent proton transfer pathways in the photosynthetic cytochrome b6f complex.". PNAS 110 (11): 4297–302. doi:10.1073/pnas.1222248110. PMC 3600468. PMID 23440205.
- ^ a b Whitelegge, JP.; Zhang, H.; Aguilera, R.; Taylor, RM.; Cramer, WA. (Oct 2002). "Full subunit coverage liquid chromatography electrospray ionization mass spectrometry (LCMS+) of an oligomeric membrane protein: cytochrome b(6)f complex from spinach and the cyanobacterium Mastigocladus laminosus.". Mol Cell Proteomics 1 (10): 816–27. doi:10.1074/mcp.m200045-mcp200. PMID 12438564.
- ^ a b Voet, Donald J. (2011). Biochemistry / Donald J. Voet ; Judith G. Voet. New York, NY: Wiley, J. ISBN 978-0-470-57095-1.
- ^ a b Stroebel, D.; Choquet, Y.; Popot, JL.; Picot, D. (Nov 2003). "An atypical haem in the cytochrome b(6)f complex.". Nature 426 (6965): 413–8. doi:10.1038/nature02155. PMID 14647374.
- ^ Yamashita, E.; Zhang, H.; Cramer, WA. (Jun 2007). "Structure of the cytochrome b6f complex: quinone analogue inhibitors as ligands of heme cn.". J Mol Biol 370 (1): 39–52. doi:10.1016/j.jmb.2007.04.011. PMC 1993820. PMID 17498743.
- ^ Baniulis, D.; Yamashita, E.; Whitelegge, JP.; Zatsman, AI.; Hendrich, MP.; Hasan, SS.; Ryan, CM.; Cramer, WA. (Apr 2009). "Structure-Function, Stability, and Chemical Modification of the Cyanobacterial Cytochrome b6f Complex from Nostoc sp. PCC 7120.". J Biol Chem 284 (15): 9861–9. doi:10.1074/jbc.M809196200. PMC 2665108. PMID 19189962.
- ^ Hasan, SS.; Stofleth, JT.; Yamashita, E.; Cramer, WA. (Apr 2013). "Lipid-induced conformational changes within the cytochrome b6f complex of oxygenic photosynthesis.". Biochemistry 52 (15): 2649–54. doi:10.1021/bi301638h. PMC 4034689. PMID 23514009.
- ^ a b Hasan, SS.; Cramer, WA. (Jun 2014). "Internal lipid architecture of the hetero-oligomeric cytochrome b6f complex.". Structure 22 (7): 1008–15. doi:10.1016/j.str.2014.05.004. PMC 4105968. PMID 24931468.
- ^ Widger, WR.; Cramer, WA.; Herrmann, RG.; Trebst, A. (Feb 1984). "Sequence homology and structural similarity between cytochrome b of mitochondrial complex III and the chloroplast b6-f complex: position of the cytochrome b hemes in the membrane.". Proc Natl Acad Sci U S A 81 (3): 674–8. doi:10.1073/pnas.81.3.674. PMC 344897. PMID 6322162.
- ^ Carrell, CJ.; Zhang, H.; Cramer, WA.; Smith, JL. (Dec 1997). "Biological identity and diversity in photosynthesis and respiration: structure of the lumen-side domain of the chloroplast Rieske protein.". Structure 5 (12): 1613–25. doi:10.1016/s0969-2126(97)00309-2. PMID 9438861.
- ^ Martinez, SE.; Huang, D.; Szczepaniak, A.; Cramer, WA.; Smith, JL. (Feb 1994). "Crystal structure of chloroplast cytochrome f reveals a novel cytochrome fold and unexpected heme ligation.". Structure 2 (2): 95–105. doi:10.1016/s0969-2126(00)00012-5. PMID 8081747.
- ^ Baniulis, D.; Yamashita, E.; Zhang, H.; Hasan, SS.; Cramer, WA. (2008). "Structure-function of the cytochrome b6f complex.". Photochem Photobiol 84 (6): 1349–58. doi:10.1111/j.1751-1097.2008.00444.x. PMID 19067956.
- ^ Cramer, WA.; Zhang, H.; Yan, J.; Kurisu, G.; Smith, JL. (May 2004). "Evolution of photosynthesis: time-independent structure of the cytochrome b6f complex.". Biochemistry 43 (20): 5921–9. doi:10.1021/bi049444o. PMID 15147175.
- ^ Hasan, SS.; Zakharov, SD.; Chauvet, A.; Stadnytski, V.; Savikhin, S.; Cramer, WA. (Jun 2014). "A map of dielectric heterogeneity in a membrane protein: the hetero-oligomeric cytochrome b6f complex.". J Phys Chem B 118 (24): 6614–25. doi:10.1021/jp501165k. PMC 4067154. PMID 24867491.
- ^ Munekage, Y.; Hashimoto, M.; Miyake, C.; Tomizawa, K.; Endo, T.; Tasaka, M.; Shikanai, T. (Jun 2004). "Cyclic electron flow around photosystem I is essential for photosynthesis.". Nature 429 (6991): 579–82. doi:10.1038/nature02598. PMID 15175756.
- ^ Blankenship, Robert E. (2002). Molecular mechanisms of photosynthesis. Oxford ; Malden, MA: Blackwell Science. ISBN 978-0-632-04321-7.
- ^ Bendall, Derek. "Cyclic photophosphorylation and electron transport". Biochimica et Biophysica Acta (BBA) - Bioenergetics. doi:10.1016/0005-2728(94)00195-B.
|accessdate=requires|url=(help) - ^ Baniulis*, D.; Hasan*, SS.; Stofleth, JT.; Yamashita, E.; Cramer, WA. (Dec 2013). "Mechanism of enhanced superoxide production in the cytochrome b(6)f complex of oxygenic photosynthesis (*equal first authorship).". Biochemistry 52 (50): 8975–83. doi:10.1021/bi4013534. PMC 4037229. PMID 24298890.
- ^ Hasan, SS.; Proctor, EA.; Dokholyan, NV.; Yamashita, E.; Dokholyan, NV.; Cramer, WA. (Oct 2014). "Traffic within the cytochrome b6f lipoprotein complex: gating of the quinone portal.". Biophysical J 107 (7): 1620–8. doi:10.1016/j.bpj.2014.08.003. PMC 4190601. PMID 25296314.
- ^ Cramer, WA.; Soriano, GM.; Ponomarev, M.; Huang, D.; Zhang, H.; Martinez, SE.; Smith, JL. (Jun 1996). "SOME NEW STRUCTURAL ASPECTS AND OLD CONTROVERSIES CONCERNING THE CYTOCHROME b6f COMPLEX OF OXYGENIC PHOTOSYNTHESIS.". Annu Rev Plant Physiol Plant Mol Biol 47: 477–508. doi:10.1146/annurev.arplant.47.1.477. PMID 15012298.
- ^ a b Cramer, WA.; Zhang, H.; Yan, J.; Kurisu, G.; Smith, JL. (2006). "Transmembrane traffic in the cytochrome b6f complex.". Annu Rev Biochem 75: 769–90. doi:10.1146/annurev.biochem.75.103004.142756. PMID 16756511.
- ^ a b "cyclic electron transfer in plant leaf". PNAS. doi:10.1073/pnas.102306999.
|accessdate=requires|url=(help) - ^ Cramer, WA.; Yan, J.; Zhang, H.; Kurisu, G.; Smith, JL. (2005). "Structure of the cytochrome b6f complex: new prosthetic groups, Q-space, and the 'hors d'oeuvres hypothesis' for assembly of the complex.". Photosynth Res 85 (1): 133–43. doi:10.1007/s11120-004-2149-5. PMID 15977064.
External links
- 1Q90 - PDB structure of cytochrome b6f complex from Chlamydomonas reinhardtii (first structure from a eukaryotic source)
- 1VF5 - PDB structure of cytochrome b6f complex from Mastigocladus laminosus (first structure from a prokaryotic source)
- 2D2C - PDB structure of cytochrome b6f complex from Mastigocladus laminosus (structure with quinone-analog DBMIB)
- 2E74 - PDB structure of cytochrome b6f complex from Mastigocladus laminosus (first structure with unoccupied p-side quinol-oxidation site)
- 2E75 - PDB structure of cytochrome b6f complex from Mastigocladus laminosus (first structure with quinone-analog NQNO)
- 2E76 - PDB structure of cytochrome b6f complex from Mastigocladus laminosus (structure with dual-site binding of quiol-analog TDS)
- 2ZT9 - PDB structure of cytochrome b6f complex from Nostoc sp. PCC 7120 (first structure from a mesophilic prokaryotic source)
- 4H13 - PDB structure of cytochrome b6f complex from Mastigocladus laminosus (structure used to define proton entry pathways on n-side)
- 4H0L - PDB structure of cytochrome b6f complex from Mastigocladus laminosus (structure used to define proton entry pathways on n-side)
- 4I7Z - PDB structure of cytochrome b6f complex from Mastigocladus laminosus (evidence of Rieske protein flexibility in b6f)
- 4PV1 - PDB structure of cytochrome b6f complex from Mastigocladus laminosus (evidence of narrow quinol-oxidation site portal)
- 4H44 - PDB structure of cytochrome b6f complex from Nostoc sp. PCC 7120 (structure used to define proton-entry and exit pathways)
- 4OGQ - PDB structure of cytochrome b6f complex from Nostoc sp. PCC 7120 (highest resolution structure, with extensive lipid-component)
- Structure-Function Studies of the Cytochrome b6f Complex - Current research on cytochrome b6f in William Cramer's Lab at Purdue University, USA
- UMich Orientation of Proteins in Membranes families/superfamily-3 - Calculated positions of b6f and related complexes in membranes
- Cytochrome b6f Complex at the US National Library of Medicine Medical Subject Headings (MeSH)
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English Journal
- Ocean science. Photosynthesis in the open ocean.
- Zehr JP, Kudela RM.SourceDepartment of Ocean Sciences, University of California, 1156 High Street, Santa Cruz, CA 95064, USA. zehrj@ucsc.edu
- Science (New York, N.Y.).Science.2009 Nov 13;326(5955):945-6.
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Related Links
- ID GO:0009496 Name plastoquinol--plastocyanin reductase activity Ontology Molecular Function Definition Catalysis of the reaction: 2 H(+)[side 1] + 2 oxidized plastocyanin + plastoquinol-1 = 2 H(+)[side 2] + 2 reduced ...
- "Plastoquinol-Plastocyanin Reductase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings). ... This graph shows the total number of publications written about ...
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| リンク元 | 「プラストキノール・プラストシアニン還元酵素」「プラストキノール・プラストシアニンレダクターゼ」 |
| 関連記事 | 「reductase」 |
「プラストキノール・プラストシアニン還元酵素」
「プラストキノール・プラストシアニンレダクターゼ」
「reductase」
- n.