FMN as a cofactor in the enzymatic reduction of DPN by hydrogen

Repaske, Roy; Seward, C. R.

doi:10.1016/0006-291x(60)90136-4

Cited by 12 publications

(1 citation statement)

References 4 publications

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“…It did not reduce pyridine nucleotides and was particle-bound. Both a soluble hydrogenase-reducing NAD and a particle-bound hydrogenase-re ducing methylene blue have been reported in extracts of Hydroge1fomonas eutropha (112) and Hydrogenomonas, strain H16 (113); however, it is not completely clear whether the soluble hydrogenase-reducing NAD is identi cal to hydrogen dehydrogenase or the NAD-reducing system found in het erotrophic systems (114), as FMN and possibly other factors are required for NAD reduction in extracts of H. eutropha (115,116). Ahrens & Schle gel (117) have reported that the activity of the NAD-reducing hydrogenase is allosterically controlled by the level of NADH2 and the presence of this unique hydrogenase does not appear to be induced specifi cally by autotrophic growth as is carboxydismutase (118).…”

Section: Peckmentioning

confidence: 97%

Energy-Coupling Mechanisms in Chemolithotrophic Bacteria

Peck¹

1968

Annu. Rev. Microbiol.

120

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Section: Peckmentioning

confidence: 97%

Energy-Coupling Mechanisms in Chemolithotrophic Bacteria

Peck¹

1968

Annu. Rev. Microbiol.

120

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Characteristics of hydrogen bacteria

Repaske

1966

Biotech & Bioengineering

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SummaryA brief review of the development of our knowledge about hydrogen bacteria is presented, with emphasis on the characteristics and physiological differences of various Hydrogenomonas species. One species, Hydrogenomonas eutropha, is discussed in greater detail. Nutritional requirements, physical factors affecting growth, and equipment used for culturing 100-ml. shake cultures and 15-1. mass cultures of H . eutropha are described. Cell-free extracts of H . eutropha carry out the oxyhydrogen reaction as demonstrated by the alternate reduction and oxidation of endogenous flavins and cytochromes by molecular hydrogen and oxygen, respectively. Spectra of cell-free extracts of this organism show the presence of cytochromes of the c and bl types. A cytochrome of the o type was also found, but none of the a cytochromes were detected. The sum of a series of enzymatic reactions shown to be catalyzed by these extracts can account for the oxidation of hydrogen by oxygen.

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�ber das Wasserstoff aktivierende System von Hydrogenomonas H16

Eberhardt

1966

Archiv. Mikrobiol.

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FMN as a cofactor in the enzymatic reduction of DPN by hydrogen

Cited by 12 publications

References 4 publications

Energy-Coupling Mechanisms in Chemolithotrophic Bacteria

Energy-Coupling Mechanisms in Chemolithotrophic Bacteria

Characteristics of hydrogen bacteria

�ber das Wasserstoff aktivierende System von Hydrogenomonas H16

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