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Can't believe that I didn't publish the changes that I had made originally...

First order of business is to restructure the article so that it has increased readability. Added the following sentence to the introduction and reorganized the entire article to revolve around this statement.

Currently, there exist four major life processes that have been identified as influenced by quantum effects: enzyme catalysis, sensory processes, energy transference, and information encoding.[1]

Notes to self

Light reactions

Photons converted to energy (ATP, NADPH)


Calvin Cycle

Uses energy to build G3P, precursor to glucose


Chloroplast -> Thylakoids (Stacked as Granum).

Chlorophyll is part of membrane bound proteins in the thylakoids

Photosystem

Chlorophylls make up photosystems (excitation and photon passing between chlorophyl)

Photon passed to reaction center complex, which transfers electron to primary electron acceptor. Later, this missing electron is enzymatically taken from water


Photosystem II converts photon energy into free electron. Electron then passed to plastoquinone, cytochrome and then Photosystem I. NADP is the final electron acceptor. This passing pumps H+ inside the thylakoid lumen to then power ATP synthase

Photosynthesis

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Photosynthesis refers to the biological process that photosynthetic cells use to synthesize organic compounds from inorganic starting materials using sunlight.[2] What has been primarily implicated as reflecting non-trivial quantum behaviors is the light reaction stage of photosynthesis. In this stage, photons are absorbed by the membrane-bound photosystems. Photosystems contain two major domains, the light harvesting complex (antennae) and the reaction center. These antennae vary among organisms. For example, bacteria use circular aggregates of chlorophyll pigments, while plants use membrane-embedded protein and chlorophyll complexes.[3][4] Regardless, photons are first captured by the antennae and passed on to the reaction center complex. Various pigment-protein complexes, such as the FMO complex in green sulfur bacteria, are responsible for transferring energy from antennae to reaction site. The photon driven excitation of the reaction center complex mediates its oxidation and the reduction the primary electron acceptor, a component of the reaction center complex. Much like the electron transport chain of the mitochondria, a linear series of oxidations and reductions drives proton (H+) pumping across the thylakoid membrane, the development of a proton motive force, and energetic coupling to the synthesis of ATP.

Previous understandings of electron excitation transference (EET) from light-harvesting antennae to the reaction center have relied on the Förster theory of incoherent EET, postulating weak electron coupling between chromophores and incoherent hopping from one to another. This theory has largely been disproven by FT electron spectroscopy experiments that show electron absorption and transfer show an efficiency of above 99%,[5] which cannot be explained by classical mechanical models. Instead, as early as 1938, scientists theorized that quantum coherence was the mechanism for excitation energy transfer. Indeed, the structure and nature of the photosystem places it in the quantum realm, with EET ranging from the femto to nanosecond scale, covering sub-nanometer to nanometer distances.[6] The effects of quantum coherence on EET in photosynthesis are best understoood through state and process coherence. State coherence refers to the extent of individual superpositions of ground and excited states for quantum entities, such as excitons. Process coherence, on the other hand, refers to degree of coupling between multiple quantum entities and their evolution as either dominated by unitary or dissipative parts, which compete with one another. Both these types of coherences are implicated in photosynthetic EET, where a exciton is coherently delocalized over several chromophores.[7] This delocalization allows for the system to simultaneously explore several energy paths and use constructive and destructive interference to guide the path of the exciton's wave packet. It is presumed that natural selection has favored the most efficient path to the reaction center. Experimentally, the interaction between the different frequency wave packets, made possible by long-lived coherence, will produce quantum beats.[8]

While quantum photosynthesis is still an emerging field, there have been many experimental results that support the quantum coherence understanding of photosynthetic EET. A 2007 study claimed the identification of electronic quantum coherence[9] at −196 °C (77 K). Another theoretical study from 2010 provided evidence that quantum coherence lives as long as 300 femtoseconds at biologically relevant temperatures (4 °C or 277 K). In that same year, experiments conducted on photosynthetic cryptophyte algae using two-dimensional photon echo spectroscopy yielded further confirmation for long-term quantum coherence.[10] These studies suggest that, through evolution, nature has developed a way of protecting quantum coherence to enhance the efficiency of photosynthesis. However, critical follow-up studies question the interpretation of these results. Single molecule spectroscopy now shows the quantum characteristics of photosynthesis without the interference of static disorder, and some studies use this method to assign reported signatures of electronic quantum coherence to nuclear dynamics occurring in chromophores.[11][12][13][14][15][16][17] A number of proposals emerged to explain unexpectedly long coherence. According to one proposal, if each site within the complex feels its own environmental noise, the electron will not remain in any local minimum due to both quantum coherence and thermal environment, but proceed to the reaction site via quantum walks.[18][19][20] Another proposal is that the rate of quantum coherence and electron tunneling create an energy sink that moves the electron to the reaction site quickly.[21] Other work suggested that geometric symmetries in the complex may favor efficient energy transfer to the reaction center, mirroring perfect state transfer in quantum networks.[22] Furthermore, experiments with artificial dye molecules cast doubts on the interpretation that quantum effects last any longer than one hundred femtoseconds.[23]

In 2017, the first control experiment with the original FMO protein under ambient conditions confirmed that electronic quantum effects are washed out within 60 femtoseconds, while the overall exciton transfer takes a time on the order of a few picoseconds.[24] In 2020 a review based on a wide collection of control experiments and theory concluded that the proposed quantum effects as long lived electronic coherences in the FMO system does not hold.[25] Instead, research investigating transport dynamics suggests that interactions between electronic and vibrational modes of excitation in FMO complexes require a semi-classical, semi-quantum explanation for the transfer of exciton energy. In other words, while quantum coherence dominates in the short-term, a classical description is most accurate to describe long-term behavior of the excitons.[26]

Another process in photosynthesis that has almost 100% efficiency is charge transfer, again suggesting that quantum mechanical phenomena are at play.[17] In 1966, a study on the photosynthetic bacterium Chromatium found that at temperatures below 100 K, cytochrome oxidation is temperature-independent, slow (on the order of milliseconds), and very low in activation energy. The authors, Don DeVault and Britton Chase, postulated that these characteristics of electron transfer are indicative of quantum tunneling, whereby electrons penetrate a potential barrier despite possessing less energy than is classically necessary.[27]




Pigment-protein complexes (PPCs)

Photosynthetic organisms absorb light energy through the process of electron excitement in antennae. These antennae vary among organisms. For example, bacteria use ring-like antennae, while plants use chlorophyll pigments to absorb photons. Photosynthesis creates Frenkel excitons, which provide a separation of charge that cells convert into usable chemical energy. The energy collected in reaction sites must be transferred quickly before it is lost to fluorescence or thermal vibrational motion.

Various structures, such as the FMO complex in green sulfur bacteria, are responsible for transferring energy from antennae to a reaction site.  FT electron spectroscopy studies of electron absorption and transfer show an efficiency of above 99%,[5] which cannot be explained by classical mechanical models like the diffusion model. Instead, as early as 1938, scientists theorized that quantum coherence was the mechanism for excitation energy transfer.

Scientists have looked for experimental evidence of this proposed energy transfer mechanism. A 2007 study claimed the identification of electronic quantum coherence[9] at −196 °C (77 K). Another theoretical study from 2010 provided evidence that quantum coherence lives as long as 300 femtoseconds at biologically relevant temperatures (4 °C or 277 K). In that same year, experiments conducted on photosynthetic cryptophyte algae using two-dimensional photon echo spectroscopy yielded further confirmation for long-term quantum coherence.[10] These studies suggest that, through evolution, nature has developed a way of protecting quantum coherence to enhance the efficiency of photosynthesis. However, critical follow-up studies question the interpretation of these results. Single molecule spectroscopy now shows the quantum characteristics of photosynthesis without the interference of static disorder, and some studies use this method to assign reported signatures of electronic quantum coherence to nuclear dynamics occurring in chromophores.[11][12][13][14][15][16][17] A number of proposals emerged to explain unexpectedly long coherence. According to one proposal, if each site within the complex feels its own environmental noise, the electron will not remain in any local minimum due to both quantum coherence and thermal environment, but proceed to the reaction site via quantum walks.[18][19][20] Another proposal is that the rate of quantum coherence and electron tunneling create an energy sink that moves the electron to the reaction site quickly.[21] Other work suggested that geometric symmetries in the complex may favor efficient energy transfer to the reaction center, mirroring perfect state transfer in quantum networks.[22] Furthermore, experiments with artificial dye molecules cast doubts on the interpretation that quantum effects last any longer than one hundred femtoseconds.[23]

In 2017, the first control experiment with the original FMO protein under ambient conditions confirmed that electronic quantum effects are washed out within 60 femtoseconds, while the overall exciton transfer takes a time on the order of a few picoseconds.[24] In 2020 a review based on a wide collection of control experiments and theory concluded that the proposed quantum effects as long lived electronic coherences in the FMO system does not hold.[25] Instead, research investigating transport dynamics suggests that interactions between electronic and vibrational modes of excitation in FMO complexes require a semi-classical, semi-quantum explanation for the transfer of exciton energy. In other words, while quantum coherence dominates in the short-term, a classical description is most accurate to describe long-term behavior of the excitons.[26]

Another process in photosynthesis that has almost 100% efficiency is charge transfer, again suggesting that quantum mechanical phenomena are at play.[17] In 1966, a study on the photosynthetic bacterium Chromatium found that at temperatures below 100 K, cytochrome oxidation is temperature-independent, slow (on the order of milliseconds), and very low in activation energy. The authors, Don DeVault and Britton Chase, postulated that these characteristics of electron transfer are indicative of quantum tunneling, whereby electrons penetrate a potential barrier despite possessing less energy than is classically necessary.[27]


Mitochondria

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Organelles, such as mitochondria, are thought to utilize quantum tunneling in order to translate intracellular energy.[28] Traditionally, mitochondria are known to generate most of the cell's energy in the form of chemical ATP. Mitochondria conversion of biomass into chemical ATP is 60-70% efficient, which is superior than the classical regime of man-made engines.[29] To achieve chemical ATP, researchers have found that a preliminary stage before chemical conversion is necessary; this step, via the quantum tunneling of electrons and hydrogen ions (H+), requires a deeper look at the quantum physics that occurs within the organelle.[30]

Mitochondria have been demonstrated to utilize quantum tunneling in its function as the powerhouse of eukaryotic cell. Similar to the light reactions in the thylakoid, linearly associated membrane bound proteins comprising the electron transport chain (ETC) energetically link the reduction of O2 with the development of a proton motive gradient (H+) across the inner membrane of the mitochondria. This energy stored as a proton motive gradient is then coupled with the synthesis of ATP. It is significant that the mitochondrion conversion of biomass into chemical ATP achieves 60-70% thermodynamic efficiency, far superior to that of man-made engines.[29] This high degree of efficiency is largely attributed to the quantum tunnelling of electrons in the ETC and of protons in the proton motive gradient. Indeed, quantum electron tunneling has already been demonstrated in certain elements of the ETC including NADH:ubiquinone oxidoreductase (Complex I) and CoQH2-cytochrome c reductase (Complex III).[31][32]

Because tunneling is a quantum mechanism, it is important to understand how this process may occur for particle transfer in a biological system. In quantum mechanics, both electrons and protons are quantum entities that exhibit wave-particle duality, exhibiting both particle and wave like properties depending on the method of experimental observation.[33] Quantum tunneling is a direct consequence of this wave-like nature of quantum entities that permits the passing-through of a potential energy barrier that would otherwise restrict the entity. [34] Moreover, it depends on the shape and size of a potential barrier, relative to the incoming energy of a particle.[35] Because the incoming particle can be defined by a wave equation its wave function, its tunneling probability is dependent upon the potential barrier's shape in an exponential way. For example, meaning that if the barrier is akin to a very wide chasm relatively wide, the incoming particle's probability to tunnel will decrease. The potential barrier, in some sense, can come in the form of an actual biomaterial barrier. Mitochondria are encompassed by a membrane structure that is akin to the cellular membrane The inner mitochondria membrane which houses the various components of the ETC is on the order of ~75 Å (~7.5 nm) thick.[29] The inner membrane of a mitochondrion must be overcome to permit signals (in the form of electrons, protons, H+) to transfer from the site of emittance (internal to the mitochondria) and the site of acceptance (i.e. the electron transport chain proteins).[36] In order to transfer particles, the membrane of the mitochondria must have the correct density of phospholipids to conduct a relevant charge distribution that attracts the particle in question. For instance, for a greater density of phospholipids, the membrane contributes to a greater conductance of protons.[36]

Unnecessary to this article. All this information is found in the wiki link to ETC

More technically, the form of the mitochondria is the matrix, with inner mitochondrial membranes (IMM) and inner membrane spaces (IMS), all housing protein sites. Mitochondria produce ATP by the oxidation of hydrogen ions from carbohydrates and fats. This process utilizes electrons in an electron transport chain (ETP). The genealogy of electron transport proceeds as follows: Electrons from NADH are transferred to NADH dehydrogenase (complex I protein), which is located in the IMM.[37] Electrons from complex I are transferred to coenzyme Q to make CoQH2; next, electrons flow to cytochrome-containing IMM protein (complex III), which further pushes electrons to cytochrome c, where electrons flow to complex IV; complex IV is the final IMM protein complex of the ETC respiratory chain.[37] This final protein allows electrons to reduce oxygen from an O2 molecule to a single O, so that it can bind to the hydrogen ions to produce H2O. The energy produced from the movement of electrons through the ETC induces proton movement (known as H+ pumping) out of the mitochondria matrix into the IMS.[38] Because any charge movement creates a magnetic field, the IMS now houses a capacitance across the matrix. The capacitance is akin to potential energy, or what is known as a potential barrier. This potential energy guides ATP synthesis via complex V (ATP synthase), which conflates ADP with another P to create ATP by pushing protons (H+) back into the matrix (this process is known as oxidative phosphorylation). Finally, the outer mitochondrial membrane (OMM) houses a voltage-dependent anion channel called the VDAC.[37] This site is important for converting energy signals into electro-chemical outputs for ATP transfer.



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References

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  1. ^ Brookes, Jennifer C. (May 2017). "Quantum effects in biology: golden rule in enzymes, olfaction, photosynthesis and magnetodetection". Proceedings of the Royal Society A: Mathematical, Physical and Engineering Sciences. 473 (2201): 20160822. Bibcode:2017RSPSA.47360822B. doi:10.1098/rspa.2016.0822. ISSN 1364-5021. PMC 5454345. PMID 28588400.
  2. ^ Mathis, Paul (2000-12). "Photosynthesis by D.O. Hall and K.K. Rao, Cambridge, Cambridge, CB2 2RU, U.K., ISBN 0 521 64257 4, £ 35, University Press". Plant Science. 160 (1): 179–180. doi:10.1016/s0168-9452(00)00371-x. ISSN 0168-9452. {{cite journal}}: Check date values in: |date= (help)
  3. ^ Sumi, Hitoshi (2001-01). "Bacterial photosynthesis begins with quantum‐mechanical coherence". The Chemical Record. 1 (6): 480–493. doi:10.1002/tcr.10004. ISSN 1527-8999. {{cite journal}}: Check date values in: |date= (help)
  4. ^ Lokstein, Heiko; Renger, Gernot; Götze, Jan P. (2021-01). "Photosynthetic Light-Harvesting (Antenna) Complexes—Structures and Functions". Molecules. 26 (11): 3378. doi:10.3390/molecules26113378. ISSN 1420-3049. PMC 8199901. PMID 34204994. {{cite journal}}: Check date values in: |date= (help)CS1 maint: PMC format (link) CS1 maint: unflagged free DOI (link)
  5. ^ a b Dostál, Jakub; Mančal, Tomáš; Augulis, Ramūnas; Vácha, František; Pšenčík, Jakub; Zigmantas, Donatas (July 2012). "Two-dimensional electronic spectroscopy reveals ultrafast energy diffusion in chlorosomes". Journal of the American Chemical Society. 134 (28): 11611–11617. doi:10.1021/ja3025627. PMID 22690836.
  6. ^ Keren, Nir; Paltiel, Yossi (2018-06). "Photosynthetic Energy Transfer at the Quantum/Classical Border". Trends in Plant Science. 23 (6): 497–506. doi:10.1016/j.tplants.2018.03.007. ISSN 1360-1385. {{cite journal}}: Check date values in: |date= (help)
  7. ^ Kassal, Ivan; Yuen-Zhou, Joel; Rahimi-Keshari, Saleh (2013-02-07). "Does Coherence Enhance Transport in Photosynthesis?". The Journal of Physical Chemistry Letters. 4 (3): 362–367. doi:10.1021/jz301872b. ISSN 1948-7185.
  8. ^ Keren, Nir; Paltiel, Yossi (2018-06). "Photosynthetic Energy Transfer at the Quantum/Classical Border". Trends in Plant Science. 23 (6): 497–506. doi:10.1016/j.tplants.2018.03.007. ISSN 1360-1385. {{cite journal}}: Check date values in: |date= (help)
  9. ^ a b Engel, Gregory S.; Calhoun, Tessa R.; Read, Elizabeth L.; Ahn, Tae-Kyu; Mančal, Tomáš; Cheng, Yuan-Chung; et al. (April 2007). "Evidence for wavelike energy transfer through quantum coherence in photosynthetic systems" (PDF). Nature. 446 (7137): 782–786. Bibcode:2007Natur.446..782E. doi:10.1038/nature05678. PMID 17429397. S2CID 13865546.
  10. ^ a b Collini, Elisabetta; Wong, Cathy Y.; Wilk, Krystyna E.; Curmi, Paul M. G.; Brumer, Paul; Scholes, Gregory D. (February 2010). "Coherently wired light-harvesting in photosynthetic marine algae at ambient temperature". Nature. 463 (7281): 644–647. Bibcode:2010Natur.463..644C. doi:10.1038/nature08811. PMID 20130647. S2CID 4369439.
  11. ^ a b Tempelaar, R.; Jansen, T. L. C.; Knoester, J. (November 2014). "Vibrational beatings conceal evidence of electronic coherence in the FMO light-harvesting complex". The Journal of Physical Chemistry B. 118 (45): 12865–12872. doi:10.1021/jp510074q. PMID 25321492.
  12. ^ a b Christensson, Niklas; Kauffmann, Harald F.; Pullerits, Tõnu; Mančal, Tomáš (June 2012). "Origin of long-lived coherences in light-harvesting complexes". The Journal of Physical Chemistry B. 116 (25): 7449–7454. arXiv:1201.6325. Bibcode:2012arXiv1201.6325C. doi:10.1021/jp304649c. PMC 3789255. PMID 22642682.
  13. ^ a b Butkus, Vytautas; Zigmantas, Donatas; Valkunas, Leonas; Abramavicius, Darius (2012). "Vibrational vs. electronic coherences in 2D spectrum of molecular systems". Chemical Physics Letters. 545: 40–43. arXiv:1201.2753. Bibcode:2012CPL...545...40B. doi:10.1016/j.cplett.2012.07.014. ISSN 0009-2614. S2CID 96663719.
  14. ^ a b Tiwari, Vivek; Peters, William K.; Jonas, David M. (2012-12-24). "Electronic resonance with anticorrelated pigment vibrations drives photosynthetic energy transfer outside the adiabatic framework". Proceedings of the National Academy of Sciences. 110 (4): 1203–1208. doi:10.1073/pnas.1211157110. ISSN 0027-8424. PMC 3557059. PMID 23267114.
  15. ^ a b Thyrhaug, Erling; Žídek, Karel; Dostál, Jakub; Bína, David; Zigmantas, Donatas (May 2016). "Exciton Structure and Energy Transfer in the Fenna-Matthews-Olson Complex". The Journal of Physical Chemistry Letters. 7 (9): 1653–1660. doi:10.1021/acs.jpclett.6b00534. PMID 27082631. S2CID 26355154.
  16. ^ a b Fujihashi, Yuta; Fleming, Graham R.; Ishizaki, Akihito (June 2015). "Impact of environmentally induced fluctuations on quantum mechanically mixed electronic and vibrational pigment states in photosynthetic energy transfer and 2D electronic spectra". The Journal of Chemical Physics. 142 (21): 212403. arXiv:1505.05281. Bibcode:2015JChPh.142u2403F. doi:10.1063/1.4914302. PMID 26049423. S2CID 1082742.
  17. ^ a b c d Marais, Adriana; Adams, Betony; Ringsmuth, Andrew K.; et al. (November 2018). "The future of quantum biology". Journal of the Royal Society, Interface. 15 (148): 20180640. doi:10.1098/rsif.2018.0640. PMC 6283985. PMID 30429265.
  18. ^ a b Mohseni, Masoud; Rebentrost, Patrick; Lloyd, Seth; Aspuru-Guzik, Alán (November 2008). "Environment-assisted quantum walks in photosynthetic energy transfer". The Journal of Chemical Physics. 129 (17): 174106. arXiv:0805.2741. Bibcode:2008JChPh.129q4106M. doi:10.1063/1.3002335. PMID 19045332. S2CID 938902.
  19. ^ a b Plenio, M. B.; Huelga, S. F. (2008-11-01). "Dephasing-assisted transport: quantum networks and biomolecules – IOPscience". New Journal of Physics. 10 (11): 113019. arXiv:0807.4902. Bibcode:2008NJPh...10k3019P. doi:10.1088/1367-2630/10/11/113019. S2CID 12172391.
  20. ^ a b Lloyd, S. (2014-03-10). Optimal Energy Transport in Photosynthesis (Speech). From Atomic to Mesoscale: The Role of Quantum Coherence in Systems of Various Complexities. Institute for Theoretical, Atomic and Molecular and Optical Physics, Harvard-Smithsonian Center for Astrophysics, Cambridge, Massachusetts. Retrieved 2019-09-30.
  21. ^ a b Lee, H. (2009). "Quantum Coherence Accelerating Photosynthetic Energy Transfer". Ultrafast Phenomena XVI. Springer Series in Chemical Physics. Vol. 92. pp. 607–609. Bibcode:2009up16.book..607L. doi:10.1007/978-3-540-95946-5_197. ISBN 978-3-540-95945-8. Archived from the original on February 3, 2021. {{cite book}}: |journal= ignored (help)
  22. ^ a b Walschaers, Mattia; Fernandez-de-Cossio Diaz, Jorge; Mulet, Roberto; Buchleitner, Andreas (November 2013). "Optimally designed quantum transport across disordered networks". Physical Review Letters. 111 (18): 180601. arXiv:1207.4072. Bibcode:2013PhRvL.111r0601W. doi:10.1103/PhysRevLett.111.180601. PMID 24237498. S2CID 40710862.
  23. ^ a b Halpin, A.; Johnson, P. J. M.; Tempelaar, R.; Murphy, R. S.; Knoester, J.; Jansen, T. L. C.; Miller, R. J. D. (March 2014). "Two-dimensional spectroscopy of a molecular dimer unveils the effects of vibronic coupling on exciton coherences". Nature Chemistry. 6 (3): 196–201. Bibcode:2014NatCh...6..196H. doi:10.1038/nchem.1834. PMID 24557133. S2CID 5059005.
  24. ^ a b Duan, H. -G.; Prokhorenko, V. I.; Cogdell, R.; Ashraf, K.; Stevens, A. L.; Thorwart, M.; Miller, R. J. D. (August 2017). "Nature does not rely on long-lived electronic quantum coherence for photosynthetic energy transfer". Proceedings of the National Academy of Sciences of the United States of America. 114 (32): 8493–8498. arXiv:1610.08425. Bibcode:2017PNAS..114.8493D. doi:10.1073/pnas.1702261114. PMC 5559008. PMID 28743751.
  25. ^ a b Cao, Jianshu; Cogdell, Richard J.; Coker, David F.; et al. (April 2020). "Quantum biology revisited". Science Advances. 6 (14): eaaz4888. Bibcode:2020SciA....6.4888C. doi:10.1126/sciadv.aaz4888. PMC 7124948. PMID 32284982.
  26. ^ a b Huelga, S. F.; Plenio, M. B. (2013-07-01). "Vibrations, quanta and biology". Contemporary Physics. 54 (4): 181–207. arXiv:1307.3530. Bibcode:2013ConPh..54..181H. doi:10.1080/00405000.2013.829687. ISSN 0010-7514. S2CID 15030104.
  27. ^ a b DeVault, D.; Chance, B. (November 1966). "Studies of photosynthesis using a pulsed laser. I. Temperature dependence of cytochrome oxidation rate in chromatium. Evidence for tunneling". Biophysical Journal. 6 (6): 825–847. Bibcode:1966BpJ.....6..825D. doi:10.1016/S0006-3495(66)86698-5. PMC 1368046. PMID 5972381.
  28. ^ Nunn, Alistair V. W.; Guy, Geoffrey W.; Bell, Jimmy D. (August 2016). "The quantum mitochondrion and optimal health". Biochemical Society Transactions. 44 (4): 1101–1110. doi:10.1042/BST20160096. PMC 5264502. PMID 27528758.
  29. ^ a b c Morowitz, H. (1968). Energy Flow in Biology. New York and London: Academic Press. pp. 55–56, 103–105, 116.
  30. ^ Zewail, Ahmed H. (2008). Physical biology : from atoms to medicine. London, UK: Imperial College Press. ISBN 978-1-84816-201-3. OCLC 294759396.
  31. ^ Hayashi, Tomoyuki; Stuchebrukhov, Alexei A. (2011-05-12). "Quantum Electron Tunneling in Respiratory Complex I". The Journal of Physical Chemistry B. 115 (18): 5354–5364. doi:10.1021/jp109410j. ISSN 1520-6106. PMC 4230448. PMID 21495666.{{cite journal}}: CS1 maint: PMC format (link)
  32. ^ Hagras, Muhammad A.; Hayashi, Tomoyuki; Stuchebrukhov, Alexei A. (2015-11-19). "Quantum Calculations of Electron Tunneling in Respiratory Complex III". The Journal of Physical Chemistry B. 119 (46): 14637–14651. doi:10.1021/acs.jpcb.5b09424. ISSN 1520-6106.
  33. ^ Bennett, James P.; Onyango, Isaac G. (2021-02). "Energy, Entropy and Quantum Tunneling of Protons and Electrons in Brain Mitochondria: Relation to Mitochondrial Impairment in Aging-Related Human Brain Diseases and Therapeutic Measures". Biomedicines. 9 (2): 225. doi:10.3390/biomedicines9020225. ISSN 2227-9059. PMC 7927033. PMID 33671585. {{cite journal}}: Check date values in: |date= (help)CS1 maint: PMC format (link) CS1 maint: unflagged free DOI (link)
  34. ^ "Quantum Theory", A Unified Grand Tour of Theoretical Physics, 2nd edition, Taylor & Francis, pp. 123–145, 2015-05-05, ISBN 978-0-429-10829-7, retrieved 2023-11-08
  35. ^ Arndt, Markus; Juffmann, Thomas; Vedral, Vlatko (December 2009). "Quantum physics meets biology". HFSP Journal. 3 (6): 386–400. arXiv:0911.0155. doi:10.2976/1.3244985. PMC 2839811. PMID 20234806.
  36. ^ a b Davies, P. C. (January 2008). "A quantum origin of life?". Quantum aspects of life. Imperial College Press. pp. 3–18. doi:10.1142/9781848162556_0001. ISBN 978-1-84816-253-2.
  37. ^ a b c Friedman, J. R.; Nunnari, J. (January 2014). "Mitochondrial form and function". Nature. 505 (7483): 335–343. Bibcode:2014Natur.505..335F. doi:10.1038/nature12985. PMC 4075653. PMID 24429632.
  38. ^ Midzak, A.; Papadopoulos, V. (2016-07-29). "Adrenal Mitochondria and Steroidogenesis: From Individual Proteins to Functional Protein Assemblies". Frontiers in Endocrinology. 7: 106. doi:10.3389/fendo.2016.00106. PMC 4965458. PMID 27524977.