Cytochrome b6f complex explained

Symbol:B6F
Cytochrome b6f complex
Tcdb:3.D.3
Opm Family:92
Opm Protein:4pv1
Membranome Superfamily:258

The cytochrome b6f complex (plastoquinol/plastocyanin reductase or plastoquinol/plastocyanin oxidoreductase;) is an enzyme found in the thylakoid membrane in chloroplasts of plants, cyanobacteria, and green algae, that catalyzes the transfer of electrons from plastoquinol to plastocyanin:

plastoquinol + 2 oxidized plastocyanin + 2 H+ [side 1]

\rightleftharpoons

plastoquinone + 2 reduced plastocyanin + 4 H+ [side 2].[1] The reaction is analogous to the reaction catalyzed by cytochrome bc1 (Complex III) of the mitochondrial electron transport chain. During photosynthesis, the cytochrome b6f complex is one step along the chain that transfers electrons from Photosystem II to Photosystem I, and at the same time pumps protons into the thylakoid space, contributing to the generation of an electrochemical (energy) gradient[2] that is later used to synthesize ATP from ADP.

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 structures 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 the 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 and of energy between the two photosynthetic reaction center complexes, Photosystem II and 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.[16] This cycle, driven by the energy of P700+, contributes to the creation of a proton gradient that can be used to drive ATP synthesis. It has been shown that this cycle is essential for photosynthesis,[17] helping to maintain the proper ratio of ATP/NADPH production for carbon fixation.[18] [19]

The p-side quinol deprotonation-oxidation reactions within the cytochrome b6f complex have been implicated in the generation of reactive oxygen species.[20] 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.[21]

Reaction mechanism

The cytochrome b6f complex is responsible for "non-cyclic" (1) and "cyclic" (2) electron transfer between two mobile redox carriers, plastoquinol (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)[16]

This reaction occurs through the Q cycle as in Complex III.[22] Plastoquinol acts as the electron carrier, transferring its two electrons to high- and low-potential electron transport chains (ETC) via a mechanism called electron bifurcation.[23] The complex contains up to three plastoquinone molecules that form an electron transfer network that are responsible for the operation of the Q cycle and its redox-sensing and catalytic functions in photosynthesis.[24]

Q cycle

First half of Q cycle

  1. 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.
  2. The reduced iron-sulfur center transfers its electron through cytochrome f to Pc.
  3. In the low-potential ETC, SQ transfers its electron to heme bp of cytochrome b6.
  4. Heme bp then transfers the electron to heme bn.
  5. Heme bn reduces Q with one electron to form SQ.

Second half of Q cycle

  1. A second QH2 binds to the complex.
  2. In the high-potential ETC, one electron reduces another oxidized Pc.
  3. 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.
  4. The oxidized Q and the reduced QH2 that has been regenerated diffuse into the membrane.

Cyclic electron transfer

Unlike 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.[25] The exact mechanism of the reduction of plastoquinone by ferredoxin is still under investigation. One proposal is that there exists a ferredoxin:plastoquinone-reductase or an NADP dehydrogenase.[25] 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:[23] [26]

  1. Fd (red) + heme x (ox) → Fd (ox) + heme x (red)
  2. heme x (red) + Fd (red) + Q + 2H+ → heme x (ox) + Fd (ox) + QH2

Further reading

External links

Notes and References

  1. https://www.enzyme-database.org/query.php?ec=7.1.1.6 ExplorEnz: EC 7.1.1.6
  2. Hasan SS, Yamashita E, Baniulis D, Cramer WA . Quinone-dependent proton transfer pathways in the photosynthetic cytochrome b6f complex . Proceedings of the National Academy of Sciences of the United States of America . 110 . 11 . 4297–302 . Mar 2013 . 23440205 . 3600468 . 10.1073/pnas.1222248110 . free .
  3. Whitelegge JP, Zhang H, Aguilera R, Taylor RM, Cramer WA . 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 . Molecular & Cellular Proteomics . 1 . 10 . 816–27 . Oct 2002 . 12438564 . 10.1074/mcp.m200045-mcp200 . free .
  4. Book: Voet . Donald J. . Voet . Judith G. . vanc . Biochemistry . 2011 . Wiley, J . New York, NY . 978-0-470-57095-1 .
  5. Stroebel D, Choquet Y, Popot JL, Picot D . An atypical haem in the cytochrome b(6)f complex . Nature . 426 . 6965 . 413–8 . Nov 2003 . 14647374 . 10.1038/nature02155 . 130033 .
  6. Yamashita E, Zhang H, Cramer WA . Structure of the cytochrome b6f complex: quinone analogue inhibitors as ligands of heme cn . Journal of Molecular Biology . 370 . 1 . 39–52 . Jun 2007 . 17498743 . 1993820 . 10.1016/j.jmb.2007.04.011 .
  7. Baniulis D, Yamashita E, Whitelegge JP, Zatsman AI, Hendrich MP, Hasan SS, Ryan CM, Cramer WA . Structure-Function, Stability, and Chemical Modification of the Cyanobacterial Cytochrome b6f Complex from Nostoc sp. PCC 7120 . The Journal of Biological Chemistry . 284 . 15 . 9861–9 . Apr 2009 . 19189962 . 2665108 . 10.1074/jbc.M809196200 . free .
  8. Hasan SS, Stofleth JT, Yamashita E, Cramer WA . Lipid-induced conformational changes within the cytochrome b6f complex of oxygenic photosynthesis . Biochemistry . 52 . 15 . 2649–54 . Apr 2013 . 23514009 . 4034689 . 10.1021/bi301638h .
  9. Hasan SS, Cramer WA . Internal lipid architecture of the hetero-oligomeric cytochrome b6f complex . Structure . 22 . 7 . 1008–15 . Jul 2014 . 24931468 . 4105968 . 10.1016/j.str.2014.05.004 .
  10. Widger WR, Cramer WA, Herrmann RG, Trebst A . 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 . Proceedings of the National Academy of Sciences of the United States of America . 81 . 3 . 674–8 . Feb 1984 . 6322162 . 344897 . 10.1073/pnas.81.3.674 . free .
  11. Carrell CJ, Zhang H, Cramer WA, Smith JL . Biological identity and diversity in photosynthesis and respiration: structure of the lumen-side domain of the chloroplast Rieske protein . Structure . 5 . 12 . 1613–25 . Dec 1997 . 9438861 . 10.1016/s0969-2126(97)00309-2 . free .
  12. Martinez SE, Huang D, Szczepaniak A, Cramer WA, Smith JL . Crystal structure of chloroplast cytochrome f reveals a novel cytochrome fold and unexpected heme ligation . Structure . 2 . 2 . 95–105 . Feb 1994 . 8081747 . 10.1016/s0969-2126(00)00012-5 . free .
  13. Baniulis D, Yamashita E, Zhang H, Hasan SS, Cramer WA . Structure-function of the cytochrome b6f complex . Photochemistry and Photobiology . 84 . 6 . 1349–58 . 2008 . 19067956 . 10.1111/j.1751-1097.2008.00444.x . 44992397 .
  14. Cramer WA, Zhang H, Yan J, Kurisu G, Smith JL . Evolution of photosynthesis: time-independent structure of the cytochrome b6f complex . Biochemistry . 43 . 20 . 5921–9 . May 2004 . 15147175 . 10.1021/bi049444o .
  15. Hasan SS, Zakharov SD, Chauvet A, Stadnytskyi V, Savikhin S, Cramer WA . A map of dielectric heterogeneity in a membrane protein: the hetero-oligomeric cytochrome b6f complex . The Journal of Physical Chemistry B . 118 . 24 . 6614–25 . Jun 2014 . 24867491 . 4067154 . 10.1021/jp501165k .
  16. Book: Berg . Jeremy M. . Tymoczko . John L. . Stryer . Lubert . Stryer . Lubert . vanc . Biochemistry . registration . 2007 . W.H. Freeman . New York . 978-0-7167-8724-2 .
  17. Munekage Y, Hashimoto M, Miyake C, Tomizawa K, Endo T, Tasaka M, Shikanai T . Cyclic electron flow around photosystem I is essential for photosynthesis . Nature . 429 . 6991 . 579–82 . Jun 2004 . 15175756 . 10.1038/nature02598 . 2004Natur.429..579M . 4421776 .
  18. Book: Robert E. Blankenship . Blankenship . Robert E. . vanc . Molecular mechanisms of photosynthesis . 2002 . Blackwell Science . Oxford ; Malden, MA . 978-0-632-04321-7 .
  19. Cyclic photophosphorylation and electron transport . Biochimica et Biophysica Acta (BBA) - Bioenergetics . Derek . Bendall. 1995 . vanc . 10.1016/0005-2728(94)00195-B . 1229 . 23–38. free .
  20. Baniulis D, Hasan SS, Stofleth JT, Cramer WA . Mechanism of enhanced superoxide production in the cytochrome b(6)f complex of oxygenic photosynthesis . Biochemistry . 52 . 50 . 8975–83 . Dec 2013 . 24298890 . 4037229 . 10.1021/bi4013534 .
  21. Hasan SS, Proctor EA, Yamashita E, Dokholyan NV, Cramer WA . Traffic within the cytochrome b6f lipoprotein complex: gating of the quinone portal . Biophysical Journal . 107 . 7 . 1620–8 . Oct 2014 . 25296314 . 4190601 . 10.1016/j.bpj.2014.08.003 . 2014BpJ...107.1620H .
  22. Cramer WA, Soriano GM, Ponomarev M, Huang D, Zhang H, Martinez SE, Smith JL . Some New Structural Aspects and Old Controversies Concerning the Cytochrome b6f Complex of Oxygenic Photosynthesis . Annual Review of Plant Physiology and Plant Molecular Biology . 47 . 477–508 . Jun 1996 . 15012298 . 10.1146/annurev.arplant.47.1.477 .
  23. Cramer WA, Zhang H, Yan J, Kurisu G, Smith JL . Transmembrane traffic in the cytochrome b6f complex . Annual Review of Biochemistry . 75 . 769–90 . 2006 . 16756511 . 10.1146/annurev.biochem.75.103004.142756 .
  24. Malone LA, Qian P, Mayneord GE, Hitchcock A, Farmer DA, Thompson RF, Swainsbury DJ, Ranson NA, Hunter CN, Johnson MP . 6 . Cryo-EM Structure of the Spinach Cytochrome B 6 F Complex at 3.6 Å Resolution . Nature . 575 . 7783 . 535–539 . November 2019 . 31723268 . 10.1038/s41586-019-1746-6 . 207987984 .
  25. Joliot P, Joliot A . Cyclic electron transfer in plant leaf . Proceedings of the National Academy of Sciences of the United States of America . 99 . 15 . 10209–14 . Jul 2002 . 12119384 . 10.1073/pnas.102306999 . 126649. free . 2002PNAS...9910209J .
  26. Cramer WA, Yan J, Zhang H, Kurisu G, Smith JL . Structure of the cytochrome b6f complex: new prosthetic groups, Q-space, and the 'hors d'oeuvres hypothesis' for assembly of the complex . Photosynthesis Research . 85 . 1 . 133–43 . 2005 . 15977064 . 10.1007/s11120-004-2149-5 . 2005PhoRe..85..133C . 20731696 .

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