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The Toxic Effects of Oxygen on Brain Metabolism and on Tissue Enzymes 2

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The Toxic Effects of Oxygen on Brain Metabolism and on Tissue Enzymes 2 Vol. 40 OXYGEN POISONING OF BRAIN TISSUE 171 Meyer, A. L. (1927). Amer. J. Phy8iol. 82, 370. Reiman, C. K. & Minot, A. S. (1920). J. biol. Chem. 42, 329. Michaelis, M. & Quastel, J. H. (1941). Biochem. J. 85, 518. Schales, 0. (1938). Ber. dtsch. chem. Ge8. 71, 447. Ochoa, S. (1939). Nature, Lond., 144, 834. Sollmann, T. H. (1942). Manual of Pharmacology, 6th -ed. Ochoa, S. (1943). J. biol. Chem. 151, 493. New York: Saunders. Penfield, W. & Erickson, T. C. (1941). Epilep8y and Cerebral Soskin, S. & Taubenhaus, M. (1943). J. Pharmacol. 78, 49. Localization. London: Baillibre, Tindall and Cox. Stadie, W. C. (1943). Personal communication. Peters, R. A. (1940). Personal communication. Stadie, W. C. & Riggs, B. C. (1944). J. biol. Chem. 154, 687. Potter, V. R. & Elvehjem, C. A. (1936). J. biol. Chem. 114, Stadie, W. C., Riggs, B. C. & Haugaard, N. (1944). Amer. J. 495. med. Sci. 207, 84. Quastel, J. H. (1939). Phy8iol. Rev. 19, 135. Still, J. L. (1941). Biochem. J. 35, 380. Quastel, J. H. (1943). Personal communication. Warburg, 0. (1930). The Metabolism of Tumours (trans. Quastel, J. H. & Wheatley, A. H. M. (1932). Biochem. J. F. Dickens). London: Constable and Co. 26, 725. Weil-Malherbe, H. (1938). Biochem. J. 32, 2257. The Toxic Effects of Oxygen on Brain Metabolism and on Tissue Enzymes 2. TISSUE ENZYMES BY F. DICKENS, National In8titute for Medical Research, London, N. W. 3, and Cancer Research Laboratory, Royal Victoria Infirmary, Newcastle-upon-Tyne (Received 23 October 1945) The evidence in Part 1 (Dickens, 1946) enables the present paper, some general evidence is collected following working hypothesis of the mode of action on the mode of inactivation by oxygen ofsome other of oxygen on brain metabolism to be advanced enzymes, particularly those which, like pyruvate with some confidence. oxidase, may play a part in brain metabolism. These (1) Exposure to unphysiologically high tensions ofoxygen experiments are of a preliminary and exploratory causes irreversible damage to brain respiration and gly- character, and serve mainly to define some con- colysis. ditions under which this type of inhibition may be (2) This damage is sustained by the enzymes themselves expected to occur, and to investigate some examples rather than by their coenzymes, as shown by the lack of of protection against oxygen poisoning in enzyme general protection in presence of excess of the more im- systems. portant coenzymes. (3) The following conditions tend to protect against The general nature of the inactivation oxygen poisoning: Presence of (a) glucose or (as shown in of enzymes by oxygen this paper) manganese ions, which protect succinoxidase in finely divided brain tissue; (b) ions of manganese, cobalt, A list has been compiled of enzymes known to be or magnesium (and probably calcium), which protect the sensitive to oxygen, or capable of inactivation by whole oxidative system in brain slices, with decreasing comparatively mild oxidants, and therefore open to activity in the order of the above series. the suspicion of being oxygen-sensitive under the (4) The brain enzymes poisoned by oxygen are mainly right conditions (Table 1). These observations were those concerned in carbohydrate metabolism. Oxidation widely scattered, and probably others could be ofglucose, fructose, lactate and pyruvate is inhibited, while the succinoxidase system, at least in intact tissue (slices) added: the only review found to bear on this subject, is much more resistant. There is support for the view that apart from the excellent one by Stadie, Riggs & the inactivation of an -SH component of the pyruvate Haugaard (1944) which appeared after this work oxidase system may be a primary stage in oxygen poisoning, was completed, is that of Hellerman (1937), which the resulting interference with resynthesis of adenosine is limited to hydrolytic enzymes. As this author triphosphate could then lead to general breakdown of rightly remarks: 'In most enzyme studies, the effect aerobic and anaerobic carbohydrate metabolism. of an ever present reagent, the oxygen of the air, (5) It is, however, not excluded that, in addition to the has been generally neglected.' pyruvate oxidase, another and earlier stage of carbohydrate There is another reason why such a list is in- metabolism might be inhibited, thus poisoning directly the oxidation of and fructose. evitably incomplete, and that is the enormous effect glucose on oxygen susceptibility of traces of contaminants, It is hoped later to study the effect of oxygen on especially -SH compounds and metallic ions, but components of the pyruvic oxidase system. In the also other substances less well defined. The following 172 F. DICKENS I946 typical experiences are quoted as excellent examples Table 1 (cont.) of the extraordinary complexity of the oxygen Enzyme poisoning of enzyme systems: nature* Enzyme class Authority B. Inactivation by exposure to oxygen under special cir- (a) Urea8e. Perlzweig (1932) showed that aeration of cumstances, or by mild oxidants: preservation by -SR crystalline urease weakened its action, and believed this compounds. (Less satisfactory evidence than the pre- ceding.) Table 1. Enzyme8 8en8&tive to oxygen or to mild oxidants -SH (?) Myokinase Kalckar (1943) Enzyme -SH Transaminase Cohen, Hekhius & nature* Enzyme class Authority Sober (1942) A. Inactivation by exposure to gaseous oxygen (or air) -SH Triosephosphate Rapkine (1938), Rap- dehydrogenase kine & Trpinac (1939) (a) Proteolytic M Zymohexase (of Warburg & Christian -SH Cathepsin: tissue Bailey, Belfer, Eder & autolysis Bradley (1942) yeast)t (1942) -SH (?) Cerebrosidase Hellerman (1937, -SH Papain Hellerman (1937) p. 466) -SH Proteases, Peptidase Irving, Fruton & Berg- * mann Enzyme nature. -SH indicates evidence that an (1942) intact sulphydryl group is considered necessary for activity. (b) Hydrolytic ('deamidizing') X indicates that the enzyme either contains a metal as M Arginase Edlbacher, Kraus & part of its prosthetic group, or requires metallic ions for Leuthardt (1933), its activity. F indicates that the enzyme contains a flavo- Hellerman (1937) protein. (The first and second of these classes are often combined; both an -SH group and an activating metal -SH Urease Perlzweig (1932), Sum- being necessary. The classification of some of these enzymes ner & Poland (1933) cannot be considered as final.) (c) Fe-porphyrins t Zymohexase of animal tissues shows only inhibition by metallic ions, and is stable to oxidants (Herbert, Gordon, M Hydrogenase Steephenson & Stickland Subrahmanyan & Green, 1940). (1 1931), Hobermann & Rtittenberg (1943) to be due to removal of a sulphydryl component by oxida- M 'Pasteur enzyme' WEarburg (1926), Stern tion. The still more highly purified enzyme is, however, Melnick (1941) practically insensitive to the action of air, but is rendered M Catalase Mairks, G. W. (1936) sensitive again on the addition of minute amounts of copper (Eprolonged experi- salts (Hellerman, Perkins & Clark, 1933). maents) (b) Arginase behaves very similarly: cruder preparations M Cytochrome oxidase Diickens (this paper) are readily inactivated by oxygen, while purified ones are (d) Oxidases, etc. much less sensitive, or completely insensitive (Edlbacher, Pyruvic oxidase Bairron (1936), Mann Kraus & Leuthardt, 1933; Klein & Zeise, 1933, 1935). Quastel (1946), Arginase preparations are activated by metallic ions (Mn, D)ickens (1946) Fe, Co, Ni, Zn, Cd, and possibly others-cf. Richards -SH Succinoxidase Le,hmann, J. (1935), & Hellerman, 1940). Hellerman (1937) believes that the LiEebricht & Massart action of these metals is to form co-ordination compounds (19937), Bohr & Bean linking the enzyme molecule with that of the substrate. (19p40-1), Stadie (1943), (e) Pho8phoglucomutawe. This enzyme, which is necessary Diickens (this paper) for breakdown and synthesis of glycogen, is of peculiar -SH Choline oxidase Diickens (this paper) interest, since the present work has shown that at different of it can exhibit a wide variation of F Xanthine oxidase Di zxon (1925), Dixon & stages purification KCodama (1926) sensitivity to air. F d-Amino-acid oxidase StEladie (1943) Gill & Lehmann (1939) showed that there was a very slight increase in the amount of Robison-ester formed from F Cytochrome-c reduc- Haaas, Horecker & Hog- glycogen by muscle extract when the experiment was made tase ness (1940): (possibly) in absence of air. ? Fatty acid dehydro- Shapiro & Wertheimer Like many other oxygen-sensitive enzymes, phospho- genase (]1943) glucomutase is highly susceptible to the influence of traces -SH Triosephosphate de- Dickens (this paper) of metals; cobalt, magnesium and manganese strongly hydrogenase accelerate, nickel feebly so, and zinc retards the activity ? Formic acid dehydro- Gale (1939) of the enzyme. Concentrated solutions of reduced gluta- genase thione and oxidized glutathione respectively, accelerate, (e) Phosphorases and retard its activity (Cori, Colowick & Cori, 1938; Gill -SR Phosphoglucomutase Gill & Lehmann (1939), & Lehmann, 1939; Lehmann, 1939; and present work). Dickens (this paper) Although these properties suggest a direct connexion be- -SH (?) Neuberg ester phos- Engelhardt & Sakov tween oxido-reduction potential and activity, the relation- phorase (phospho- (1943) ship is, in fact, involved, e.g. substances such as insulin glucokinase) or caffeine are also inhibitory. The best way ofcircumventing V91. 40 OXYGEN POISONING OF ENZYMES 173 the experimental difficulties has in practice proved to be: of sensitivity of these enzymes on their
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