George Orwell: "Crimestop means the faculty of stopping short, as though by instinct, at the threshold of any dangerous thought. It includes the power of not grasping analogies, of failing to perceive logical errors, of misunderstanding the simplest arguments if they are inimical to Ingsoc, and of being bored or repelled by any train of thought which is capable of leading in a heretical direction. Crimestop, in short, means protective stupidity."
Crimestop in the world of Clausius and Einstein is immeasurably more overwhelming than in Big Brother's world. Just a few examples.
It is well known that, if a catalyst (enzyme) does not accelerate the forward and reverse reactions "equally" ("by precisely the same factor"), then it violates the second law of thermodynamics:
"In the presence of a catalyst, BOTH THE FORWARD AND REVERSE REACTION RATES WILL SPEED UP EQUALLY, thereby allowing the system to reach equilibrium faster. However, it is very important to keep in mind that the addition of a catalyst has no effect whatsoever on the final equilibrium position of the reaction. It simply gets it there faster...If the addition of catalysts could possibly alter the equilibrium state of the reaction, this would violate the second rule of thermodynamics." https://courses.lumenlearning.com/introchem/chapter/the-effect-of-a-catalyst/
"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
Catalysts (enzymes) that violate the second law of thermodynamics are actually commonplace, largely discussed in the literature, employed in promising technologies, but theoretical physicists and theoretical chemists stop short, "as though by instinct", at the threshold of the unbearable thought that the sacrosanct second law of thermodynamics might be false:
"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...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
"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
Crimestop in the world of Clausius and Einstein is immeasurably more overwhelming than in Big Brother's world. Just a few examples.
It is well known that, if a catalyst (enzyme) does not accelerate the forward and reverse reactions "equally" ("by precisely the same factor"), then it violates the second law of thermodynamics:
"In the presence of a catalyst, BOTH THE FORWARD AND REVERSE REACTION RATES WILL SPEED UP EQUALLY, thereby allowing the system to reach equilibrium faster. However, it is very important to keep in mind that the addition of a catalyst has no effect whatsoever on the final equilibrium position of the reaction. It simply gets it there faster...If the addition of catalysts could possibly alter the equilibrium state of the reaction, this would violate the second rule of thermodynamics." https://courses.lumenlearning.com/introchem/chapter/the-effect-of-a-catalyst/
"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
Catalysts (enzymes) that violate the second law of thermodynamics are actually commonplace, largely discussed in the literature, employed in promising technologies, but theoretical physicists and theoretical chemists stop short, "as though by instinct", at the threshold of the unbearable thought that the sacrosanct second law of thermodynamics might be false:
"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...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
"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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