Studies on the respiratory chain-linked reduced nicotinamide adenine dinucleotide dehydrogenase. XIV. Location of the sites of inhibition of rotenone, barbiturates, and piericidin by means of electron paramagnetic resonance spectroscopy.

نویسندگان

G Palmer

D J Horgan

H Tisdale

T P Singer

H Beinert

چکیده

On the addition of NADH to submitochondrial particles in which NADH oxidase is blocked by rotenone, piericidin A, or Amytal, the g = 1.94 signal of NADH dehydrogenase appears in essentially the same manner as in untreated preparations. However, the appearance of the NADHinduced iron signal of succinate dehydrogenase and of cytochromes b and cl is inhibited by these agents. It is concluded that Amy@?-otenone, and piericidin block NADH oxidation on the O2 side of the non-heme iron of NADH dehydrogenase.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Reaction sites of rotenone, piericidin A, and amytal in relation to the nonheme iron components of NADH dehydrogenase.

The locus of inhibition of nicotinamide adenine dinucleotide, reduced form (NADH) oxidation in mitochondria by rotenone, piercidin A, and barbiturates is considered in the light of available information. Most lines of evidence indicate that the point of inhibition is on the O(2) side of NADH dehydrogenase. Kinetic experiments on the substrate-induced appearance of the electron paramagnetic reso...

متن کامل

Studies on the respiratory chain-linked reduced nicotinamide adenine dinucleotide dehydrogenase. 13. Binding sites of rotenone, piericidin A, and amytal in the respiratory chain.

The binding sites of rotenone, piericidin A, and Amytal in the reduced nicotinamide adenine dinucleotide oxidase chain of heart have been studied with the aid of rotenone6aJ4C. Binding of rotenone continues in a linear manner beyond the point of maximal inhibition of respiration, indicating that rotenone is tightly bound not only at the specific site in the NADH dehydrogenase segment of the res...

متن کامل

Studies on the Respiratory Chain-linked Reduced Nicotinamide Adenine Dinucleotide Dehydrogenase XIII. BINDING SITES OF ROTENONE, PIERICIDIN A, AND AMYTAL IN THE RESPIRATORY CHAIN*

متن کامل

RESPIRATION AND PROTEIN SYNTHESIS IN ESCHERICHIA COLI MEMBRANE-ENVELOPE FRAGMENTS V. On the Reduction of Nonheme Iron and the Cytochromes by Nicotinamide Adenine Dinucleotide and Succinate

The sensitivity of nicotinamide adenine dinucleotide (NADH) oxidase and succinoxidase to metal chelators, the generation of an electron paramagnetic resonance (EPR) signal upon addition of these substrates, and the rate of formation of the EPR signal relative to the rate of the cytochrome reduction suggest the participation of nonheme iron proteins in the respiratory process of Escherichia coli...

متن کامل