The metastases of Einstein's 1905 constant-speed-of-light malignancy definitively killed physics, but this branch of science was already in agony in 1905, overwhelmed by the metastases of another malignancy - the second law of thermodynamics:
Jos Uffink: "I therefore argue for the view that THE SECOND LAW HAS NOTHING TO DO WITH THE ARROW OF TIME...Before one can claim that acquaintance with the Second Law is as indispensable to a cultural education as Macbeth or Hamlet, it should obviously be clear what this law states. This question is surprisingly difficult. The Second Law made its appearance in physics around 1850, but a half century later it was already surrounded by so much confusion that the British Association for the Advancement of Science decided to appoint a special committee with the task of providing clarity about the meaning of this law. However, its final report (Bryan 1891) did not settle the issue. Half a century later, the physicist/philosopher Bridgman still complained that there are almost as many formulations of the second law as there have been discussions of it. And EVEN TODAY, THE SECOND LAW REMAINS SO OBSCURE that it continues to attract new efforts at clarification." http://philsci-archive.pitt.edu/313/1/engtot.pdf
Clifford Truesdell, The Tragicomical History of Thermodynamics, 1822-1854, p. 6: "Finally, I confess to a heartfelt hope - very slender but tough - that even some thermodynamicists of the old tribe will study this book, master the contents, and so share in my discovery: Thermodynamics need never have been the DISMAL SWAMP OF OBSCURITY that from the first it was and that today in common instruction it is; in consequence, it need not so remain."...p. 333: "Clausius' verbal statement of the "Second Law" makes no sense, for "some other change connected therewith" introduces two new and unexplained concepts: "other change" and "connection" of changes. Neither of these finds any place in Clausius' formal structure. All that remains is a Mosaic prohibition. A century of philosophers and journalists have acclaimed this commandment; a century of mathematicians have shuddered and averted their eyes from the unclean." https://www.amazon.com/Tragicomical-Thermodynamics-1822-1854-Mathematics-Physical/dp/1461394465
One cannot expect the "dismal swamp of obscurity" to be inhabited by honest creatures, can one? Consider the most preposterous prediction of the second law of thermodynamics:
"As is true of any catalyst, enzymes do not alter the equilibrium point of the reaction. This means that the enzyme accelerates the forward and reverse reaction by precisely the same factor." http://www.columbia.edu/itc/chemistry/ARCHIVE/chem-c2407_f99/problems/kinetics1.pdf
Since the prediction is obviously absurd (both common sense and empirical reality contradict it), scientists should have applied reductio ad absurdum and rejected the false underlying premise, the second law of thermodynamics, long ago (logic forbids the combination "true premise, absurd prediction"):
"Catalysis is usually construed to facilitate equilibrium being attained more easily and quickly, or occasionally less so (anticatalysis), but not to alter the position of equilibrium, i.e., not to alter the equilibrium constant Keq. Indeed, it is sometimes stated that if catalysis could alter Keq, then it could be employed to violate the Second Law of Thermodynamics. Consider the following cycle, executed isothermally. Insert a catalyst that alters a system’s position of equilibrium or Keq. Then withdraw the catalyst, allowing the system to return (albeit more slowly in the absence of catalysis) to its initial state. The catalyst can then be re-inserted, and the cycle repeated. If, for example, the volume of the system is a function of Keq, then such a cycle could be employed to drive the motion of a piston, thus doing work. It is sometimes stated that such a cycle would violate the Second Law of Thermodynamics, because it represents a heat engine doing work while operating in a cycle despite isothermality [1]. Nevertheless, cases wherein catalysis does alter Keq are known." https://www.longdom.org/open-access...ational-system-a-secondlaw-paradox-31803.html
"CpI is a good catalyst for both H+ reduction and H2 oxidation, exhibiting kcat values of 5800 s−1 and 19 500 s−1, respectively (Table S2, Supporting Information). Not all hydrogenases are good catalysts for both H+ reduction and H2 oxidation, with several examples exhibiting a distinct and often dramatic “catalytic bias” exerting a disproportionate rate acceleration in one direction of the reaction relative to the other." https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8653774/
"Catalytic bias refers to the relative rate preference of a catalyst for either the forward or reverse direction. In enzymatic metal cofactor-based oxidation–reduction catalysis, the tuning of catalytic bias plays an underlying role in controlling rates of reactivity. For this, enzymes have evolved complex active sites that can exist in multiple oxidation states with differing reduction potentials in order to achieve challenging multi-step, oxidation–reduction reactions. Conceivably, the relative stability of the intermediates that contribute to determining the rate-limiting step of the catalytic cycle could impose catalytic bias, although mechanisms for this concept are just beginning to be realized. As one example, recent work on Clostridium pasteurianum [FeFe]-hydrogenases which catalyze reversible hydrogen oxidation have shown that the differential stabilization/destabilization of active site oxidation states through either static or dynamic protein interactions can preferentially promote either the hydrogen oxidation or proton reduction direction of the reaction." https://onlinelibrary.wiley.com/doi/abs/10.1002/9781119951438.eibc2770
"However, many enzymes reversibly convert their substrate and product, and if one is interested in catalysis in only one direction, it may be necessary to prevent the reverse reaction...This is the first demonstration, on a specific example, that slowing a step that is rate limiting only when the enzyme works in one direction is a general mechanism for biasing the enzyme in the other direction." https://hal.science/hal-01977597/document
"PtO-clusters were found to have a pivotal role in unidirectional suppression of undesirable H2 oxidation [the backward reaction] in photocatalytic water cleavage process. More importantly, these PtO-clusters can also demonstrate excellent efficiency in hydrogen evolution rate [the forward reaction]." https://www.nature.com/articles/ncomms3500
"Interestingly, although [FeFe]-hydrogenases all possess the same active site H cluster, they display a large range of H2 gas oxidation and proton reduction activities, with some displaying a dramatic catalytic bias, that is, the propensity of a catalyst to effect rate of acceleration in one reaction direction over the other. " https://europepmc.org/article/pmc/pmc8653774
"The protein scaffold around an enzyme’s catalytic core exquisitely controls reactivity, including the direction and rate of chemical processes. Scientists refer to this fine tuning as “catalytic bias”—and how it occurs remains widely debated...A research team from three U.S. Department of Energy (DOE) national laboratories and four universities found that subtle changes to the environment surrounding some enzymes can not only change the rate of a cellular reaction by a staggering six orders of magnitude but also its direction. That reversal—the root of the catalytic bias dilemma—is like speeding in one direction at 10 miles-per-second, then going in the opposite direction at 1,000,000 miles-per-second." https://www.pnnl.gov/news-media/remarkable-rate-return-catalytic-bias
"Traditional catalysis is a central pivot around which much of the industrial and biological worlds turn. Positive catalysts satisfy three general principles. First, they increase reaction rates by providing lower activation energies for rate-limiting steps. Second, they are not consumed by their net reactions although they are intimately involved in them. Third, they do not alter final thermodynamic equilibria of their reactions. Epicatalysts bend this third principle in that they shift the final gas-phase equilibria of reactions." https://www.sciencedirect.com/science/article/pii/S2213138818301838
"In 2000, a simple, foundational thermodynamic paradox was proposed: a sealed blackbody cavity contains a diatomic gas and a radiometer whose apposing vane surfaces dissociate and recombine the gas to different degrees (A_2 ⇌ 2A). As a result of differing desorption rates for A and A_2 , there arise between the vane faces permanent pressure and temperature differences, either of which can be harnessed to perform work, in apparent conflict with the second law of thermodynamics. Here we report on the first experimental realization of this paradox, involving the dissociation of low-pressure hydrogen gas on high-temperature refractory metals (tungsten and rhenium) under blackbody cavity conditions. The results, corroborated by other laboratory studies and supported by theory, confirm the paradoxical temperature difference and point to physics beyond the traditional understanding of the second law." https://link.springer.com/article/10.1007/s10701-014-9781-5
"This has resulted in a deeper understanding of the hydrogenase model system and the ability to directly influence catalytic bias. Thus, the work presented here represents key progress towards developing unidirectional catalysts, and demonstrates the possibility of targeted, rational design and implementation of unidirectional catalysts." https://scholarworks.montana.edu/xmlui/handle/1/14621
"When enzymes are optimized for biotechnological purposes, the goal often is to increase stability or catalytic efficiency. However, many enzymes reversibly convert their substrate and product, and if one is interested in catalysis in only one direction, it may be necessary to prevent the reverse reaction...We evidence a novel strategy for tuning the catalytic bias of an oxidoreductase, which consists in modulating the rate of a step that is limiting only in one direction of the reaction, without modifying the properties of the active site." https://pubs.acs.org/doi/10.1021/ja301802r
Jos Uffink: "I therefore argue for the view that THE SECOND LAW HAS NOTHING TO DO WITH THE ARROW OF TIME...Before one can claim that acquaintance with the Second Law is as indispensable to a cultural education as Macbeth or Hamlet, it should obviously be clear what this law states. This question is surprisingly difficult. The Second Law made its appearance in physics around 1850, but a half century later it was already surrounded by so much confusion that the British Association for the Advancement of Science decided to appoint a special committee with the task of providing clarity about the meaning of this law. However, its final report (Bryan 1891) did not settle the issue. Half a century later, the physicist/philosopher Bridgman still complained that there are almost as many formulations of the second law as there have been discussions of it. And EVEN TODAY, THE SECOND LAW REMAINS SO OBSCURE that it continues to attract new efforts at clarification." http://philsci-archive.pitt.edu/313/1/engtot.pdf
Clifford Truesdell, The Tragicomical History of Thermodynamics, 1822-1854, p. 6: "Finally, I confess to a heartfelt hope - very slender but tough - that even some thermodynamicists of the old tribe will study this book, master the contents, and so share in my discovery: Thermodynamics need never have been the DISMAL SWAMP OF OBSCURITY that from the first it was and that today in common instruction it is; in consequence, it need not so remain."...p. 333: "Clausius' verbal statement of the "Second Law" makes no sense, for "some other change connected therewith" introduces two new and unexplained concepts: "other change" and "connection" of changes. Neither of these finds any place in Clausius' formal structure. All that remains is a Mosaic prohibition. A century of philosophers and journalists have acclaimed this commandment; a century of mathematicians have shuddered and averted their eyes from the unclean." https://www.amazon.com/Tragicomical-Thermodynamics-1822-1854-Mathematics-Physical/dp/1461394465
One cannot expect the "dismal swamp of obscurity" to be inhabited by honest creatures, can one? Consider the most preposterous prediction of the second law of thermodynamics:
"As is true of any catalyst, enzymes do not alter the equilibrium point of the reaction. This means that the enzyme accelerates the forward and reverse reaction by precisely the same factor." http://www.columbia.edu/itc/chemistry/ARCHIVE/chem-c2407_f99/problems/kinetics1.pdf
Since the prediction is obviously absurd (both common sense and empirical reality contradict it), scientists should have applied reductio ad absurdum and rejected the false underlying premise, the second law of thermodynamics, long ago (logic forbids the combination "true premise, absurd prediction"):
"Catalysis is usually construed to facilitate equilibrium being attained more easily and quickly, or occasionally less so (anticatalysis), but not to alter the position of equilibrium, i.e., not to alter the equilibrium constant Keq. Indeed, it is sometimes stated that if catalysis could alter Keq, then it could be employed to violate the Second Law of Thermodynamics. Consider the following cycle, executed isothermally. Insert a catalyst that alters a system’s position of equilibrium or Keq. Then withdraw the catalyst, allowing the system to return (albeit more slowly in the absence of catalysis) to its initial state. The catalyst can then be re-inserted, and the cycle repeated. If, for example, the volume of the system is a function of Keq, then such a cycle could be employed to drive the motion of a piston, thus doing work. It is sometimes stated that such a cycle would violate the Second Law of Thermodynamics, because it represents a heat engine doing work while operating in a cycle despite isothermality [1]. Nevertheless, cases wherein catalysis does alter Keq are known." https://www.longdom.org/open-access...ational-system-a-secondlaw-paradox-31803.html
"CpI is a good catalyst for both H+ reduction and H2 oxidation, exhibiting kcat values of 5800 s−1 and 19 500 s−1, respectively (Table S2, Supporting Information). Not all hydrogenases are good catalysts for both H+ reduction and H2 oxidation, with several examples exhibiting a distinct and often dramatic “catalytic bias” exerting a disproportionate rate acceleration in one direction of the reaction relative to the other." https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8653774/
"Catalytic bias refers to the relative rate preference of a catalyst for either the forward or reverse direction. In enzymatic metal cofactor-based oxidation–reduction catalysis, the tuning of catalytic bias plays an underlying role in controlling rates of reactivity. For this, enzymes have evolved complex active sites that can exist in multiple oxidation states with differing reduction potentials in order to achieve challenging multi-step, oxidation–reduction reactions. Conceivably, the relative stability of the intermediates that contribute to determining the rate-limiting step of the catalytic cycle could impose catalytic bias, although mechanisms for this concept are just beginning to be realized. As one example, recent work on Clostridium pasteurianum [FeFe]-hydrogenases which catalyze reversible hydrogen oxidation have shown that the differential stabilization/destabilization of active site oxidation states through either static or dynamic protein interactions can preferentially promote either the hydrogen oxidation or proton reduction direction of the reaction." https://onlinelibrary.wiley.com/doi/abs/10.1002/9781119951438.eibc2770
"However, many enzymes reversibly convert their substrate and product, and if one is interested in catalysis in only one direction, it may be necessary to prevent the reverse reaction...This is the first demonstration, on a specific example, that slowing a step that is rate limiting only when the enzyme works in one direction is a general mechanism for biasing the enzyme in the other direction." https://hal.science/hal-01977597/document
"PtO-clusters were found to have a pivotal role in unidirectional suppression of undesirable H2 oxidation [the backward reaction] in photocatalytic water cleavage process. More importantly, these PtO-clusters can also demonstrate excellent efficiency in hydrogen evolution rate [the forward reaction]." https://www.nature.com/articles/ncomms3500
"Interestingly, although [FeFe]-hydrogenases all possess the same active site H cluster, they display a large range of H2 gas oxidation and proton reduction activities, with some displaying a dramatic catalytic bias, that is, the propensity of a catalyst to effect rate of acceleration in one reaction direction over the other. " https://europepmc.org/article/pmc/pmc8653774
"The protein scaffold around an enzyme’s catalytic core exquisitely controls reactivity, including the direction and rate of chemical processes. Scientists refer to this fine tuning as “catalytic bias”—and how it occurs remains widely debated...A research team from three U.S. Department of Energy (DOE) national laboratories and four universities found that subtle changes to the environment surrounding some enzymes can not only change the rate of a cellular reaction by a staggering six orders of magnitude but also its direction. That reversal—the root of the catalytic bias dilemma—is like speeding in one direction at 10 miles-per-second, then going in the opposite direction at 1,000,000 miles-per-second." https://www.pnnl.gov/news-media/remarkable-rate-return-catalytic-bias
"Traditional catalysis is a central pivot around which much of the industrial and biological worlds turn. Positive catalysts satisfy three general principles. First, they increase reaction rates by providing lower activation energies for rate-limiting steps. Second, they are not consumed by their net reactions although they are intimately involved in them. Third, they do not alter final thermodynamic equilibria of their reactions. Epicatalysts bend this third principle in that they shift the final gas-phase equilibria of reactions." https://www.sciencedirect.com/science/article/pii/S2213138818301838
"In 2000, a simple, foundational thermodynamic paradox was proposed: a sealed blackbody cavity contains a diatomic gas and a radiometer whose apposing vane surfaces dissociate and recombine the gas to different degrees (A_2 ⇌ 2A). As a result of differing desorption rates for A and A_2 , there arise between the vane faces permanent pressure and temperature differences, either of which can be harnessed to perform work, in apparent conflict with the second law of thermodynamics. Here we report on the first experimental realization of this paradox, involving the dissociation of low-pressure hydrogen gas on high-temperature refractory metals (tungsten and rhenium) under blackbody cavity conditions. The results, corroborated by other laboratory studies and supported by theory, confirm the paradoxical temperature difference and point to physics beyond the traditional understanding of the second law." https://link.springer.com/article/10.1007/s10701-014-9781-5
"This has resulted in a deeper understanding of the hydrogenase model system and the ability to directly influence catalytic bias. Thus, the work presented here represents key progress towards developing unidirectional catalysts, and demonstrates the possibility of targeted, rational design and implementation of unidirectional catalysts." https://scholarworks.montana.edu/xmlui/handle/1/14621
"When enzymes are optimized for biotechnological purposes, the goal often is to increase stability or catalytic efficiency. However, many enzymes reversibly convert their substrate and product, and if one is interested in catalysis in only one direction, it may be necessary to prevent the reverse reaction...We evidence a novel strategy for tuning the catalytic bias of an oxidoreductase, which consists in modulating the rate of a step that is limiting only in one direction of the reaction, without modifying the properties of the active site." https://pubs.acs.org/doi/10.1021/ja301802r
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