Endergonic Reduction of Mitochondrial Diphosphopyridine Nucleotide by Sarcosine

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Endergonic reduction of mitochondrial diphosphopyridine nucleotide by sarcosine.

The aerobic dehydrogenation of the N-methyl group of sarcosine initiates an energy-requiring reduction of diphosphopyridine nucleotide in intact mitochondria. The formation of DPNH can be measured both spectrophotometrically and by the reduction of acetoacetate. Except in the presence of uncouplers, such as Dicumarol and arsenate, reduction of DPN by sarcosine does not require added adenosine t...

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Reincorporation of Diphosphopyridine Nucleotide into Mitochondrial

The fundamental question whether the pyridine nucleotide coenzymes in mitochondria are bound to enzyme systems in a way which determines their ability to carry out coupled oxidative phosphorylation via the electron transport system has presented itself for a number of years. Although some of the earlier differences between oxidation via external diphosphopyridine nucleotide and via internal dip...

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The reduction of diphosphopyridine nucleotide by sodium dithionite.

It is well known that diphosphopyridine nucleotide (DPN) can be reduced by sodium dithionite to give a product, DPNH, identical with that obtained by enzymic reduction. DPN can also be reduced by ionizing radiations under special conditions (Swallow, 1953), but theproductwas found to possess no coenzyme activity when tested with lactic dehydrogenase (Stein & Swallow, 1954). Barron, Johnson & Co...

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Diphosphopyridine nucleotide pyrophosphatase.

Enzymatic splitting of diphosphopyridine nucleotide (DPN)’ by microorganisms, plants, and animal tissues has been known for many years, but the precise nature of this reaction is not well understood (1). Ohlmeyer (2) first observed that adenylic acid (5-phosphoadenosine) appeared when DPN was incubated with yeast maceration juice. Later Heiwinkel (3) identified adenylic acid as a product of the...

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Influence of metallic chelates on the diphosphopyridine nucleotide oxidase and diphosphopyridine nucleotide-cytochrome c reductase systems.

The need for additional study on the specific relation between metallic ions and metabolic function, especially in the case of the diphosphopyridine nucleotide oxidase system, has been expressed by Mahler (1) and others. This is particularly indicated in view of the fact that a number of the known components of this system contain iron. While it is broadly concluded that iron compounds facilita...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1967

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(19)81453-9