Biological Catalysis of the Exchange Reaction Between Water and Hydrogen

Hoberman, Henry D.; Rittenberg, D.

doi:10.1016/s0021-9258(18)72430-7

Cited by 101 publications

(14 citation statements)

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“…Hydrogenase is inactivated by oxygen, the "Knallgas" reaction only occurring when hydrogen is in excess, although some bacteria (Bacillus pycnoticus) can react in mixtures of two parts of hydrogen with one part of oxygen. The inactivated enzyme is reactivated by molecular hydrogen as well as by hydrogen donors, glucose, pyruvate, formate, f umarate, and succinate (1297) ; the action of succinate could not be confirmed by Lascelles and Still (2651). Cyanide blocks this reactivation and 10"^3 1 cyanide therefore inhibits when added to the aerobic, but not when added to the anaerobic, system (1297,2626).…”

Section: H3cc(oh)2c02h -^Ch3co2h + Co2 + H2mentioning

confidence: 93%

“…The inactivated enzyme is reactivated by molecular hydrogen as well as by hydrogen donors, glucose, pyruvate, formate, f umarate, and succinate (1297) ; the action of succinate could not be confirmed by Lascelles and Still (2651). Cyanide blocks this reactivation and 10"^3 1 cyanide therefore inhibits when added to the aerobic, but not when added to the anaerobic, system (1297,2626).…”

Section: H3cc(oh)2c02h -^Ch3co2h + Co2 + H2mentioning

confidence: 93%

“…It is to be expected that the enzyme also catalyzes the inverse reactions, e.g., the spHtting of formic acid; HCO2H -+ CO2 4-H2. Stickland (2629,2663) have assumed that this reaction is caused by a distinct enzyme, hydrogenlyase, but it is now probable that this is identical with hydrogenase (898,1297,2080). It is also very likely that the development of molecular hydrogen in fermentations, e.g., butyric acid fermentation, is catalyzed by hydrogenase (1507,1513,1590,2105).…”

Section: Mode Of Catalatic and Peroxidative Actionmentioning

confidence: 99%

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Hematin compounds and bile pigments; their constitution, metabolism, and function, by R. Lemberg and J.W. Legge.

Legge¹,

Lemberg²

1949

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II. METHODS or INVESTIGATION* Only the naturally occurring hile pigments of type IXa are discussed.* .\11 tlie al).s()r[)ti()ii curves of the "hiliverdiiis" in Heihiieyers hook (121-i) are ohviously tliose of niixtiirt's of liiliverditi witli hiliruliiii (pages 1(51, 1()7) and other * The term K-urobilin is, however, used by the Fischer school to denote a mixture of side chain isomerides of mesobilene-(b) in contradistinction to mesobilene-(b) IXa.* It is not certain, however, whether the albumin is the only plasma protein able to combine with hematin (c/. Miller and Ailing, 191f9a).* Keilin and Smith {1502a) have been unable to confirm the results of Virtanen and Laine.XII. HEMOGLOBIN CATABOLISM, II * Cf., however, Bittner and Watson {28-3a). CHAPTER XIII FORMATION OF HEMOGLOBIN AND SYNTHESIS OF PORPHYRINSIN THE ANIMAL BODY * The hemoglobin found occasionally in some species of Daphnia (Fox,937aa) does not appear to have an essential physiologic function, although, like the hematin compounds mentioned above, it is passed on in parthenogenetic eggs. Even the chlorocruorin or erythrocruorin of serpulimorphid worms does not appear to be essential (Fox, 937a).Glaucobilin. See Mesobiliverdin. Globan, 211. See also Globin (denatured). Globin, denatured, 240, 258 combination with heme, 232 electrometric titration, 255 in erythrocytes, 525 isoelectric point, 255 renaturation, 259 Globin, native, 230, 258, 568 amino acids. See Hemoglobin. combination, with hematins, 239 with metalloporphyrins, 240 with porphyrins, 240 denaturation, 255 ff. 734 SUBJECT INDEX Globin native (contd.) electrometric titration, 255 differential of globin and hemiglobin, 244 fate in hemogIol>in breakdown, 548, 568 frictional ratio, 250 isoelectric point, 255 molecular weight, 250 oxidation, in autoxidation of hemoglobin, 390 in denaturation, 395, 478 preparation, 258 specificity, 321. See also Hemoglobin. synthesis in vivo, 610 Glutathione as anticatalase, 412 and choleglobin formation, 477, 478, 517 and dehydroascorbic acid, 470, 517, 518 in erythrocyte, 516, 522, 619 and hem/globin, 522 as substrate of cytochrome c, 376 Glycine, in porphyrin s\nthesis, 637 Gmelin reaction, 109, 112 (table), 116, 138 Green hemins, 201, 456, 490. See also Chlorophyll hemins, Pheophorbide kemin, Verdochemochrome.

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Section: H3cc(oh)2c02h -^Ch3co2h + Co2 + H2mentioning

confidence: 93%

Section: H3cc(oh)2c02h -^Ch3co2h + Co2 + H2mentioning

confidence: 93%

Section: Mode Of Catalatic and Peroxidative Actionmentioning

confidence: 99%

See 1 more Smart Citation

Hematin compounds and bile pigments; their constitution, metabolism, and function, by R. Lemberg and J.W. Legge.

Legge¹,

Lemberg²

1949

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“…This reaction was first used by Parkas et al (1934) and studied later in great detail by Hoberman and Rittenberg (1943). Hydrogenase was also shown (Krasna and Rittenberg, 1954b) to catalyze the conversion of para-to orthohydrogen and, on the basis cf this and the deuterium exchange, the mechanism of activation of hydrogen by hydrogenase was postulated to be a heterolytic split of hydrogen to a hydride and a proton, i.e.…”

Section: H2 + Hdo ^Hd + H20mentioning

confidence: 95%

Catalysis of the H₂-HTO Exchange by Hydrogenase. A New Assay for Hydrogenase^*

Anand¹,

Krasna²

1965

Biochemistry

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“…The hydrogenase remains activated after exposure to air. The activation also occurs in the presence of carbon monoxide and is due to activation of the resid-T A he inhibition of the enzyme hydrogenase by carbon monoxide has been observed by many investigators, but with the exception of Hoberman and Rittenberg (1943) and Kempner and Kubowitz ( 1933), all have failed to demonstrate its reversibility by light. In 1962, we demonstrated that the activity of the hydrogenase of Proteus vulgaris which is inhibited by carbon monoxide could be substantially increased by exposing the inhibited enzyme to strong visible light sources (Puree et al, 1962).…”

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confidence: 99%