Protein Information

Name cytochrome b
Synonyms COB; CYTB; Cytochrome b; Cytochrome b of complex III; MT CYB; MTCYB; mitochondrially encoded cytochrome b; Cytochrome bs…

Compound Information

Name rotenone
CAS

Reference List

PubMed Abstract RScore(About this table)
7774132 Takeshige K: [Superoxide formation and lipid peroxidation by the mitochondrial electron-transfer chain]. Rinsho Shinkeigaku. 1994 Dec;34(12):1269-71.

Superoxide is a stoichiometric precursor of mitochondrial H2O2 because the ratio of O2-/H2O2 generation rates is close to 2.0 and is generated by an autoxidizable component in the NADH dehydrogenase and the ubiquinone-cytochrome b site.
Electrons from NADH are supplied to the reactions from a component between the substrate site and the rotenone-sensitive site of the NADH dehydrogenase.
1(0,0,0,1) Details
16742609 Lloyd D, Chance B: Electron transport in mitochondria isolated from the flagellate Polytomella caeca. Biochem J. 1968 May;107(6):829-837.

Electron transport is inhibited by antimycin A, rotenone, piericidin A and cyanide. 3.
Spectral data indicate that antimycin A inhibits the reoxidation of reduced cytochrome b. 4.
1(0,0,0,1) Details
4985609 Wilson DF, Dutton PL: Energy dependent changes in the oxidation-reduction potential of cytochrome b. Biochem Biophys Res Commun. 1970 Apr 8;39(1):59-64.

1(0,0,0,1) Details
821392 Kot EJ, Olson VL, Rolewic LJ, McClary DO: An alternate respiratory pathway in Candida albicans. Antonie Van Leeuwenhoek. 1976;42(1-2):33-48.

The high rate of respiration of C. albicans in the presence of inhibitors for three sites of electron transport in the conventional oxidative pathway, the inhibition of this respiration by SHAM and its loss by the absence of cytochrome b, indicate an alternate oxidative pathway in this organism which crosses the conventional one at cytochrome b.
Usual concentrations of antimycin A, rotenone and EDTA, individually or in combination, reduced aerobic growth rate and cell yield of Candida albicans to about half its normal level and to about the levels of previously-described acetate-negative, cytochrome-complete and aa3-deficient variants which were little affected by the inhibitors.
1(0,0,0,1) Details
1768276 Lund BO, Miller DM, Woods JS: Mercury-induced H2O2 production and lipid peroxidation in vitro in rat kidney mitochondria. Biochem Pharmacol. 1991 Dec 11;42 Suppl:S181-7.

In mitochondria supplemented with a respiratory chain substrate (succinate or malate/glutamate) and an electron transport inhibitor (antimycin A (AA) or rotenone), Hg (II) (30 nmol/mg protein) increased H2O2 formation approximately 4-fold at the ubiquinone-cytochrome b region (AA-inhibited) and 2-fold at the NADH dehydrogenase region (rotenone-inhibited).
82(1,1,1,2) Details
1664494 Benzi G, Curti D, Pastoris O, Marzatico F, Villa RF, Dagani F: Sequential damage in mitochondrial complexes by peroxidative stress. Neurochem Res. 1991 Dec;16(12):1295-302.

The cerebral peroxidative stress induces: (a) initially, a decrease in brain GSH concentration concomitant with a decrease in the mitochondrial activity of cytochrome oxidase of aa3-type (complex IV), without changes in ubiquinone and cytochrome b populations; (b) subsequently, an alteration in the transfer molecule cytochrome c and, finally, in rotenone-sensitive NADH-cytochrome c reductase (complex I) and succinate dehydrogenase (complex II).
37(0,1,2,2) Details
7236242 Takayanagi R, Takeshige K, Minakami S: NADH- and NADPH-dependent lipid peroxidation in bovine heart submitochondrial particles. Biochem J. 1980 Dec 15;192(3):853-60.

Reduced uniquinone-2 also inhibited the peroxidation, but duroquinol, which reduces cytochrome b without reducing endogenous uniquinone, did not.
The reaction was stimulated by rotenone and inhibited by antimycin A when the input was fast, whereas it was not affected by the inhibitors when the input was slow.
1(0,0,0,1) Details
215122 Ragan CI, Heron C: The interaction between mitochondrial NADH-ubiquinone oxidoreductase and ubiquinol-cytochrome c oxidoreductase. Biochem J. 1978 Sep 15;174(3):783-90.

Experiments on the inhibition of the NADH-cytochrome c oxidoreductase activity of mixtures of Complexes I and III by rotenone and antimycin indicate that electron transfer between a unit of Complex I-Complex III and extra molecules of Complexes I or III does not contribute to the overall rate of cytochrome c reduction. 3.
The reduction by NADH of the cytochrome b of mixtures of Complexes I and III is biphasic.
1(0,0,0,1) Details
5053270 Pedersen JI, Flatmark T: Studies on the energy state of isolated brown adipose tissue mitochondria. Biochim Biophys Acta. 1972 Aug 17;275(2):135-47.


The cytochrome b complex as a probe of the energy state of the mitochondrial inner membrane.
1(0,0,0,1) Details
3571184 Nishino H, Ito A: Subcellular distribution of OM cytochrome b-mediated NADH-semidehydroascorbate reductase activity in rat liver. J Biochem. 1986 Dec;100(6):1523-31.

The ratio of the OM cytochrome b-mediated activities of NADH-SDA reductase to rotenone-insensitive NADH-cytochrome c reductase varied among these tissues.
248(3,3,3,8) Details
1148252 Higuti T, Mizuno S, Muraoka S: Stepwise reduction of cytochromes b-562, b-566 and b-558 in rat liver mitochondria. Biochim Biophys Acta. 1975 Jul 8;396(1):36-47.

Addition of succinate to rotenone-KCN-inhibited and ATP-treated rat liver mitochondria under conditions where cytochromes b-566, b-562, c+c1 and a+a3 were already fully reduced, caused reduction of cytochrome b-558 (having an alpha-band at 558 nm, a beta-band at 527 nm and a gamma-band at 426 nm at room temperature) after exhaustion of molecular oxygen in the reaction medium, without any contribution from a long-wavelength species (cytochrome b-566). 4.
82(1,1,1,2) Details
4340268 Norling B, Nelson BD, Nordenbrand K, Ernster L: Evidence for the occurrence in submitochondrial particles of a dual respiratory chain containing different forms of cytochrome b. Biochim Biophys Acta. 1972 Jul 12;275(1):18-32.

1(0,0,0,1) Details
177046 La Monica RF, Marrs BL: The branched respiratory system of photosynthetically grown Rhodopseudomonas capsulata. Biochim Biophys Acta. 1976 Mar 12;423(3):431-9.

In this category were the actions of rotenone on NADH oxidase, antimycin A on cytochrome c reductase and, in M6 and Z-1, cyanide on N,N,N'N'-tetramethyl-p-phenylenediamine oxidase.
These results suggest that the respiratory chain of the parental strain branches at the ubiquinone-cytochrome b region into two pathways, each branch goes to a distinct terminal oxidase, and either may be blocked independently by genetic mutation.
1(0,0,0,1) Details
4346389 Wikstrom MK, Berden JA: Oxidoreduction of cytochrome b in the presence of antimycin. Biochim Biophys Acta. 1972 Dec 14;283(3):403-20.

1(0,0,0,1) Details
40546 Lorusso M, Capuano F, Boffoli D, Stefanelli R, Papa S: The mechanism of transmembrane delta muH+ generation in mitochondria by cytochrome c oxidase. Biochem J. 1979 Jul 15;182(1):133-47.

In rat liver mitochondria treated with rotenone, N-ethylmaleimide or oligomycin the expected alkalinization caused by proton consumption for aerobic oxidation of ferrocyanide was delayed with respect to ferrocyanide oxidation, unless carbonyl cyanide p-trifluoromethoxyphenylhydrazone was present. 2.
This shows that the ferricyanide formed accepts electrons passing through the protonmotive segments of the respiratory chain at the level of cytochrome c and/or redox components of the cytochrome b-c1 complex situated on the oxygen side of the antimycin-inhibition site.
1(0,0,0,1) Details
8512585 Lund BO, Miller DM, Woods JS: Studies on Hg (II)-induced H2O2 formation and oxidative stress in vivo and in vitro in rat kidney mitochondria. Biochem Pharmacol. 1993 May 25;45(10):2017-24.

This effect was accompanied by significantly increased H2O2 formation, GSH depletion and TBARS formation linked to both NADH dehydrogenase (rotenone-inhibited) and ubiquinone-cytochrome b (antimycin-inhibited) regions of the electron transport chain.
82(1,1,1,2) Details
4356125 Barnes R, Colleran EM, Jones OT: The electron-transport system of mitochondria from the slime mould Physarum polycephalum. Biochem J. 1973 Jul;134(3):745-51.

P. polycephalum mitochondria oxidized added NADH via a rotenone-insensitive pathway, but the oxidation of malate plus glutamate was rotenone sensitive; both of these substrates reduced much less cytochrome b than did succinate, in both aerobic and anaerobic steady states.
81(1,1,1,1) Details
5133534 Wikstrom MK: Properties of three cytochrome b-like species in mitochondria and submitochondrial particles. Biochim Biophys Acta. 1971 Dec 7;253(2):332-45.

1(0,0,0,1) Details
6263247 Turrens JF, Boveris A: Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria. Biochem J. 1980 Nov 1;191(2):421-7.

In NADH- and antimycin-supplemented submitochondrial particles, rotenone has a biphasic effect: it increases O2- production at the NADH dehydrogenase and it inhibits O2- production at the ubiquinone-cytochrome b site.
32(0,1,1,2) Details
4345350 Barnes R, Connelly JL, Jones OT: The utilization of iron and its complexes by mammalian mitochondria. . Biochem J. 1972 Aug;128(5):1043-55.

The addition of FeCl (3) to anaerobic particles caused an oxidation of cytochrome b when this region of the respiratory chain was isolated by treatment with rotenone and antimycin A.
31(0,1,1,1) Details
1592119 Aldunate J, Coloma-Torres L, Spencer P, Morello A, Ojeda JM, Repetto Y: Effects of 2 (3)-tert-butyl-4-hydroxyanisole (BHA) on in situ mitochondria of Trypanosoma cruzi. FEBS Lett. 1992 May 25;303(1):73-6.

Rotenone did not inhibit the oxygen uptake of the parasite.
Studies with in situ mitochondria confirmed that BHA, an antioxidant food additive, blocks the mitochondrial electron transport chain at the succinate-cytochrome b segment being the molecular basis of this trypanocidal action.
1(0,0,0,1) Details
8392019 Sohal RS: Aging, cytochrome oxidase activity, and hydrogen peroxide release by mitochondria. Free Radic Biol Med. 1993 Jun;14(6):583-8.

Results are interpreted to suggest that partial inhibition of cytochrome c oxidase activity can lead to the stimulation of mitochondrial H2O2 production in the housefly at site (s) other than NADH dehydrogenase and ubisemiquinone/cytochrome b region; a possible source may be glycerophosphate dehydrogenase.
H2O2 release by mitochondria, inhibited with rotenone and antimycin A, was greatly increased upon supplementation with alpha-glycerophosphate; however, the further addition of KCN or myxothiazol, to such preparations, caused a depression of H2O2 generation.
1(0,0,0,1) Details
185865 Muller W, Schewe T: [The systemic fungicide tridermorph as an inhibitor of the respiratory chain of electron transfer particles from beef heart mitochondria]. Acta Biol Med Ger. 1976;35(6):693-707.

The inhibition of the NADH-ubiquinone oxydoreductase activity as well as the suppression of the NADH-induced reduction of all cytochromes on the one hand and the insensitivity of the NADH-ferricyanide oxydoreductase system on the other argue in favour of a site of action similar to rotenone.
The partial suppression of the succinate-induced reduction of cytochrome b with simultaneous complete inhibition of the reduction of the other cytochromes indicate an additional site of action analogous to antimycin A.
1(0,0,0,1) Details
9396723 Guidarelli A, Clementi E, Brambilla L, Cantoni O: Mechanism of the antimycin A-mediated enhancement of t-butylhydroperoxide-induced single-strand breakage in DNA. Biochem J. 1997 Dec 15;328 ( Pt 3):801-6.


The hypothesis that these effects are selectively linked to inhibition of the electron transport from cytochrome b to cytochrome c1 is validated by the following observations: (1) two complex III inhibitors, antimycin A and 2-heptyl-4-hydroxyquinoline N-oxide, enhanced the tB-OOH-induced DNA cleavage over the same concentration range as that in which inhibition of oxygen consumption was observed; (2) the complex III inhibitor-mediated enhancement of tB-OOH-induced DNA damage was abolished by the complex I inhibitor rotenone or by glucose omission, and (3) the enhancing effects of antimycin A were not observed in respiration-deficient cells.
0(0,0,0,0) Details
7775420 Gonzalez-Flecha B, Demple B: Metabolic sources of hydrogen peroxide in aerobically growing Escherichia coli. J Biol Chem. 1995 Jun 9;270(23):13681-7.

Compounds that block electron transport at NADH dehydrogenase (rotenone) or between ubiquinone and cytochrome b (antimycin) showed that univalent reduction of O2 can occur at these sites in vivo to form superoxide anion (O2-), in agreement with reports for mammalian mitochondria.
31(0,1,1,1) Details
5160697 Nelson BD, Norling B, Persson B, Ernster L: Effect of thenoyltrifluoroacetone on the interaction of succinate dehydrogenase and cytochrome b in ubiquinone-depleted submitochondrial particles. Biochem Biophys Res Commun. 1971 Sep 17;44(6):1312-20.

1(0,0,0,1) Details
8268305 Kolesova GM, Karnaukhova LV, Segal' NK, Iaguzhinskii LS: [The effect of inhibitors of the Q-cycle on cyano-resistant oxidation of malate by rat liver mitochondria in the presence of menadione]. Biokhimiia. 1993 Oct;58(10):1630-40.

In the presence of myxothiazole and antimycin menadione oxidizes cytochrome b.
In the presence of rotenone, when menadione is reduced by DT-diaphorase, the rate of cyano-resistant respiration decreases approximately twofold; its sensitivity towards myxothiazole and antimycin drops down to 40%.
1(0,0,0,1) Details
647077 Totpvets ZP: [Oxidation of 4-N-(aniline)-5-methoxy-1,2-dioxybenzene via the mitochondrial respiratory chain]. Biokhimiia. 1978 Feb;43(2):260-7.

The site of AMOBQH2 interaction is located in the region of cytochrome b, between rotenone and antimycin block.
31(0,1,1,1) Details
207670 Kenimer EA, Lapp DF: Effects of selected inhibitors on electron transport in Neisseria gonorrhoeae. J Bacteriol. 1978 May;134(2):537-45.

The effects of selected electron transport inhibitors (amytal, rotenone, 2-heptyl-4-hydroxyquinoline, antimycin A1, and potassium cyanide [KCN]) on electron transfer in whole-cell and sonically treated whole-cell preparations of N. gonorrhoeae were examined.
Difference spectra in the presence of 2-heptyl-4-hydroxyquinoline suggest a possible site of interaction of this compound at the substrate side of cytochrome b.
1(0,0,0,1) Details
8216312 Debise R, Touraille S, Durand R, Alziari S: Biochemical consequences of a large deletion in the mitochondrial genome of a Drosophila subobscura strain. Biochem Biophys Res Commun. 1993 Oct 15;196(1):355-62.


Spectrophotometric determination of respiratory complex activities shows that: complex I (5 genes implicated in deletion) presents maximal activity reduced by 40%, whereas that of complex III (concerned by cytochrome b) is lowered by 30%.
1(0,0,0,1) Details
893348 Harris MA, Reddy CA: Hydrogenase activity and the H2-fumarate electron transport system in Bacteroides fragilis. J Bacteriol. 1977 Sep;131(3):922-8.

Inhibition of fumarate reduction by acriflavin, rotenone, 2-heptyl-4-hydroxyquinoline-N-oxide, and antimycin A suggest the involvement of a flavoprotein, a quinone, and cytochrome b in the reduction of fumarate to succinate.
31(0,1,1,1) Details
7358642 Ito A: Cytochrome b5-like hemoprotein of outer mitochondrial membrane: OM cytochrome b. J Biochem. 1980 Jan;87(1):73-80.

Contribution of OM cytochrome b to rotenone-insensitive NADH-cytochrome c reductase activity..
16(0,0,2,6) Details
10844979 Obungu VH, Kiaira JK, Olembo NK, Njogu MR: Pathways of glucose catabolism in procyclic Trypanosoma congolense. Indian J Biochem Biophys. 1999 Oct;36(5):305-11.

Studies of respiration on glucose in procyclic Trypanosoma congolense in the presence of rotenone, antimycin, cyanide, salicylhydroxamic acid and malonate have indicated the presence of NADH dehydrogenase, cytochrome b-c1, cytochrome aa3, trypanosome alternate oxidase and NADH fumarate reductase/succinate dehydrogenase pathway that contributes electrons to coenzyme Q of the respiratory chain.
6(0,0,1,1) Details
210759 Halestrap AP: Stimulation of the respiratory chain of rat liver mitochondria between cytochrome c1 and cytochrome c by glucagon treatment of rats. Biochem J. 1978 Jun 15;172(3):399-405.

Measurement of the cytochrome spectra under uncoupled conditions in the presence of succinate and rotenone demonstrates a crossover between cytochromes c and c (1) when control mitochondria are compared with those from glucagon-treated rats, cytochrome c being more oxidized and cytochrome c (1) more reduced in control mitochondria.
Under conditions where pyruvate metabolism is studied the control mitochondria are generally more oxidized than those from glucagon-treated rats, the redox state of cytochrome b-566 correlating with the rate of pyruvate metabolism in sucrose medium.
3(0,0,0,3) Details
168827 Schwartz AC, Sporkenbach J: The electron transport system of the anaerobic Propionibacterium shermanii: cytochrome and inhibitor studies. Arch Microbiol. 1975 Mar 10;102(3):261-73.

Cytochrome b was reduced by succinate to about 50%, and by NADH, lactate or glycerol-3-phosphate to 80--90%. 3.
The inhibitory effects of amytal and rotenone on NADH oxidation, but not on the oxidation of the other substrates, indicated the presence of the NADH dehydrogenase complex, or "site I region", in the electron transport system of P. shermanii. 4.
3(0,0,0,3) Details
1751550 Gregory RB, Berry MN: On the thyroid hormone-induced increase in respiratory capacity of isolated rat hepatocytes. Biochim Biophys Acta. 1991 Dec 3;1098(1):61-7.


However, less rotenone was required for maximal inhibition of respiration in the hypothyroid state than in cells from euthyroid or hyperthyroid rats, implying that hepatocytes from hypothyroid animals contain less NADH dehydrogenase.
0(0,0,0,0) Details
2321971 Bolter CJ, Chefurka W: Extramitochondrial release of hydrogen peroxide from insect and mouse liver mitochondria using the respiratory inhibitors phosphine, myxothiazol, and antimycin and spectral analysis of inhibited cytochromes. Arch Biochem Biophys. 1990 Apr;278(1):65-72.


Other respiratory inhibitors, antimycin, myxothiazol, and rotenone were used with insect mitochondria.
0(0,0,0,0) Details
1171697 Wang CC: Studies of the mitochondria from Eimeria tenella and inhibition of the electron transport by quinolone coccidiostats. Biochim Biophys Acta. 1975 Aug 11;396(2):210-9.


The mitochondrial respiration was inhibited by cyanide, azide, carbon monoxide, antimycin A, and 2-heptyl-4-hydroxyquinoline-N-oxide, but was relatively resistant to rotenone and amytal.
0(0,0,0,0) Details
4323963 Wong DT, Horng JS, Gordee RS: Respiratory chain of a pathogenic fungus, Microsporum gypseum: effect of the antifungal agent pyrrolnitrin. J Bacteriol. 1971 Apr;106(1):168-73.

In mitochondrial preparations, pyrrolnitrin strongly inhibited respiration and the rotenone-sensitive NADH-cytochrome c reductase.
The extent of reduction of flavoproteins by NADH and succinate, measured at 465 - 510 nm, was unaltered; however, the reduction of cytochrome b, measured at 560 - 575 nm, was partially inhibited by pyrrolnitrin.
3(0,0,0,3) Details
7150580 Hatefi Y, Yagi T: Kinetics of cytochrome b oxidation in antimycin-treated submitochondrial particles. Biochemistry. 1982 Dec 7;21(25):6614-8.

By contrast, rotenone, cyanide, BAL (2,3-dimercaptopropanol), and 5-n-undecyl-6-hydroxy-4,7-dioxobenzothiazole [Trumpower, B.
2(0,0,0,2) Details
9824492 Carrasco-Marin E, Paz-Miguel JE, Lopez-Mato P, Alvarez-Dominguez C, Leyva-Cobian F: Oxidation of defined antigens allows protein unfolding and increases both proteolytic processing and exposes peptide epitopes which are recognized by specific T cells. Immunology. 1998 Nov;95(3):314-21.


However, neither rotenone and antimycins (inhibitors of O-2 production at the NADH dehydrogenase and ubiquinone-cytochrome b regions, respectively) nor aminoguanidine (an inducible nitric oxide synthase inhibitor) impaired antigen presentation, thus indirectly discarding the participation of mitochondrial oxidation and reactive nitrogen intermediates (RNI) in antigen processing.
0(0,0,0,0) Details
6513990 Takamiya S, Furushima R, Oya H: Electron transfer complexes of Ascaris suum muscle mitochondria: I. Mol Biochem Parasitol. 1984 Oct;13(2):121-34.


The enzyme preparation catalyzed the reduction of 1.68 mumol cytochrome c min-1 mg-1 protein at 25 degrees C with NADH but not with NADPH, and retained its sensitivity to rotenone, piericidin A and 2-heptyl-4-hydroxyquinoline-N-oxide as with the submitochondrial particles.
0(0,0,0,0) Details
7199109 Il'chenko AP, Komarova GN: [Octanol oxidation by the mitochondria of Torulopsis candida] . Mikrobiologiia. 1981 Nov-Dec;50(6):964-72.

When octanol is oxidized in aerobic conditions, cytochrome b is reduced, with the absorption maxima in alpha, beta and gamma bands being at 555, 526 and 425 nm, respectively.
The cytochrome is reduced in aerobic conditions also in the presence of exogenous NADH and rotenone.
2(0,0,0,2) Details
6093033 Papadimitriou A, Neustein HB, Dimauro S, Stanton R, Bresolin N: Histiocytoid cardiomyopathy of infancy: deficiency of reducible cytochrome b in heart mitochondria. Pediatr Res. 1984 Oct;18(10):1023-8.

Biochemical studies showed markedly decreased succinate-cytochrome c reductase and rotenone-sensitive NADH-cytochrome c reductase activities, while other mitochondrial enzymes were normal.
2(0,0,0,2) Details
147472 Streumer-Svobodova Z, Drahota Z: The development of oxidative enzymes in rat liver mitochondria. . Physiol Bohemoslov. 1977;26(6):525-34.


Rotenone-insensitive NADH-cytochrome c reductase activity, which is localized on the outer mitochondrial membrane, remained stable up to the 10th day, and rose between the 10th and the 90th day.
0(0,0,0,0) Details
16934215 Gonzalez B, Martinez S, Chavez JL, Lee S, Castro NA, Dominguez MA, Gomez S, Contreras ML, Kennedy C, Escamilla JE: Respiratory system of Gluconacetobacter diazotrophicus PAL5. Biochim Biophys Acta. 2006 Dec;1757(12):1614-22. Epub 2006 Jul 8.


Strong inhibition by rotenone and capsaicin and resistance to flavone indicated that NADH-quinone oxidoreductase is a NDH-1 type enzyme.
0(0,0,0,0) Details
9813002 Vercesi AE, Rodrigues CO, Uyemura SA, Zhong L, Moreno SN: Respiration and oxidative phosphorylation in the apicomplexan parasite Toxoplasma gondii. J Biol Chem. 1998 Nov 20;273(47):31040-7.

Although ADP phosphorylation was detected in the presence of malate, this activity was rotenone-insensitive and was probably due to the conversion of malate into succinate through a fumarate reductase activity that was detected in mitochondrial extracts.
Atovaquone was shown to inhibit the respiratory chain of T. gondii and mammalian mitochondria between cytochrome b and c1 as occurs with antimycin A1.
1(0,0,0,1) Details
4358869 Wikstrom MK: The different cytochrome b components in the respiratory chain of animal mitochondria and their role in electron transport and energy conservation. Biochim Biophys Acta. 1973 Dec 7;301(2):155-93.

1(0,0,0,1) Details
9395404 Hasegawa E, Kang D, Sakamoto K, Mitsumoto A, Nagano T, Minakami S, Takeshige K: A dual effect of 1-methyl-4-phenylpyridinium (MPP+)-analogs on the respiratory chain of bovine heart mitochondria. Arch Biochem Biophys. 1997 Jan 1;337(1):69-74.

We examined effects of several compounds, structurally related to 1-methyl-4-phenylpyridinium (MPP+), on the NADH-dependent respiration of bovine heart submitochondrial particles. 1-Methyl-4-(3 '-trimethylammoniophenyl) pyridinium (analog 8) as well as MPP+ completely inhibited O2 consumption, reduction of ubiquinone-10, and reduction of cytochrome b in a dose-dependent manner.
The production of superoxide (O2-) induced by MPP+ or analog 8 was to the same extent as that by rotenone, an inhibitor of complex I of the mitochondrial respiratory chain.
1(0,0,0,1) Details
9241135 Hasegawa E, Kang D, Sakamoto K, Mitsumoto A, Nagano T, Minakami S, Takeshige K: A Dual Effect of 1-Methyl-4-phenylpyridinium (MPP+ )-Analogs on the Respiratory Chain of Bovine Heart Mitochondria. Arch Biochem Biophys. 1997 Jan 1;337(1):69-74.

We examined effects of several compounds, structurally related to 1-methyl-4-phenylpyridinium (MPP+ ), on the NADH-dependent respiration of bovine heart submitochondrial particles. 1-Methyl-4-(3'-trimethylammoniophenyl) pyridinium (analog 8) as well as MPP+ completely inhibited O2 consumption, reduction of ubiquinone-10, and reduction of cytochrome b in a dose-dependent manner.
The production of superoxide (O- 2 ) induced by MPP+ or analog 8 was to the same extent as that by rotenone, an inhibitor of complex I of the mitochondrial respiratory chain.
1(0,0,0,1) Details
15479985 Ichikawa H, Kokura S, Aw TY: Role of endothelial mitochondria in oxidant production and modulation of neutrophil adherence. J Vasc Res. 2004 Sep-Oct;41(5):432-44. Epub 2004 Oct 12.

The current objectives were to (1) determine the adhesion of human neutrophils to human umbilical vein endothelial cells exposed to antimycin A, a specific inhibitor of the mitochondrial cytochrome b-c (1) complex, and (2) define the mechanisms responsible for the early and late phases of neutrophil hyperadhesivity.
Blockade of electron transport in antimycin A and A/R exposed cells with rotenone, amytal or thenoyltrifluoroacetate, but not myxothiazol, prevented neutrophil adhesion, confirming a role for mitochondrial ROS.
1(0,0,0,1) Details
4749271 Boveris A, Chance B: The mitochondrial generation of hydrogen peroxide. Biochem J. 1973 Jul;134(3):707-16.

It is postulated that in addition to the well-known flavin reaction, formation of H (2) O (2) may be due to interaction with an energy-dependent component of the respiratory chain at the cytochrome b level.
With malate-glutamate, H (2) O (2) formation is sensitive to rotenone.
1(0,0,0,1) Details
2919886 Cino M, Del Maestro RF: Generation of hydrogen peroxide by brain mitochondria: the effect of reoxygenation following postdecapitative ischemia. Arch Biochem Biophys. 1989 Mar;269(2):623-38.

Succinate-supported H2O2 generation was diminished by rotenone and the uncoupler carbonyl cyanide m-chlorphenylhydrazone and enhanced by antimycin A and increased oxygen tensions.
When maximally reduced, the NADH dehydrogenase and the ubiquinone-cytochrome b regions of the electron transport chain are sources of H2O2.
1(0,0,0,1) Details
6289887 Bindoli A, Cavallini L, Jocelyn P: Mitochondrial lipid peroxidation by cumene hydroperoxide and its prevention by succinate. Biochim Biophys Acta. 1982 Sep 15;681(3):496-503.

The results suggest that reduction of mitochondrial ubiquinone may prevent the generation of lipid hydroperoxides but that their subsequent removal may require reduction at or beyond cytochrome b.
Conversely, rotenone and N-ethylmaleimide stimulate the reaction.
1(0,0,0,1) Details
5422599 Slater EC, Lee CP, Berden JA, Wegdam HJ: High-energy forms of cytochrome b. Nature. 1970 Jun 27;226(5252):1248-9.

1(0,0,0,1) Details
1567448 Unnikrishnan LS, Raj RK: Fumarate reductase system of filarial parasite Setaria digitata. Biochem Biophys Res Commun. 1992 Apr 15;184(1):448-53.

This activity is sensitive to rotenone, antimycin A and o-Hydroxy diphenyl.
The fumarate reductase system consisting of NADH-coenzyme Q reductase, cytochrome b like component (s) and succinate dehydrogenase/fumarate reductase is thus very important and hence specific inhibitors of the system may prove useful in the effective control of filariasis.
1(0,0,0,1) Details
2871147 Sugiyama Y, Fujita T, Matsumoto M, Okamoto K, Imada I: Effects of idebenone (CV-2619) and its metabolites on respiratory activity and lipid peroxidation in brain mitochondria from rats and dogs. J Pharmacobiodyn. 1985 Dec;8(12):1006-17.

These facts and results of inhibitor analysis suggest that the action site of CV-2619 is NADH-linked complex I in the mitochondrial respiratory chain and is different from that of inhibitors of oxidative phosphorylation such as rotenone, oligomycin and 2,4-dinitrophenol.
Reduced CV-2619 (2H-CV-2619) was rapidly oxidized through the cytochrome b chain, indicating that the compound functioned simply as an electron carrier of mitochondrial respiratory system.
1(0,0,0,1) Details
5074740 Pedersen JI, Flatmark T: Studies on the energy state of isolated brown adipose tissue mitochondria. Biochim Biophys Acta. 1972 Aug 17;275(2):135-47.


The cytochrome b complex as a probe of the energy state of the mitochondrial inner membrane.
1(0,0,0,1) Details