Complexes of cobalt(III) with derivatives of oximes as catalysts of electron transfer from the components of the respiratory chain

1984 ◽  
Vol 33 (10) ◽  
pp. 1993-1997
Author(s):  
G. N. Novodarova ◽  
L. L. Kiseleva ◽  
M. Yu. Tuvin ◽  
A. I. Stetsenko ◽  
L. P. Sharova ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Respiratory Chain ◽  
Derivatives Of

scholarly journals Evidence that the inhibition sites of the neurotoxic amine 1-methyl-4-phenylpyridinium (MPP+) and of the respiratory chain inhibitor piericidin A are the same

1991 ◽  
Vol 273 (2) ◽  
pp. 481-484 ◽  
Author(s):  
R R Ramsay ◽  
M J Krueger ◽  
S K Youngster ◽  
T P Singer
Keyword(s):  
Electron Transfer ◽  
Respiratory Chain ◽  
Nadh Dehydrogenase ◽  
Nadh Oxidation ◽  
Submitochondrial Particles ◽  
Alkyl Chains ◽  
Alkyl Derivatives ◽  
Derivatives Of ◽  
Respiratory Chain Inhibitors

1-Methyl-4-phenylpyridinium (MPP+), the neurotoxic bioactivation product of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP), interrupts mitochondrial electron transfer at the NADH dehydrogenase-ubiquinone junction, as do the respiratory chain inhibitors rotenone, piericidin A and barbiturates. Proof that these classical respiratory chain inhibitors and MPP+ react at the same site in the complex NADH dehydrogenase molecule has been difficult to obtain because none of these compounds bind covalently to the target. The 4′-alkyl derivatives of MPP+ inhibit NADH oxidation in submitochondrial particles at much lower concentrations than does MPP+ itself, but still dissociate on washing the membrane preparations, with consequent re-activation of the enzyme. The MPP+ analogues with short alkyl chains prevent the binding of 14C-labelled piericidin A to the membrane and thus must act at the same site, but analogues with alkyl chains longer than heptyl do not prevent binding of [14C]piericidin.

Nanosized non-proteinaceous complexes III and IV mimicking electron transfer of mitochondrial respiratory chain

2021 ◽  
Author(s):  
Iago A. Modenez ◽  
Lucyano J.A. Macedo ◽  
Antonio F.A.A. Melo ◽  
Andressa R. Pereira ◽  
Osvaldo N. Oliveira Jr ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Respiratory Chain ◽  
Mitochondrial Respiratory Chain ◽  
Mitochondrial Respiratory

New 4-Hydroxypyridine and 4-Hydroxyquinoline Derivatives as Inhibitors of NADH-ubiquinone Reductase in the Respiratory Chain

1989 ◽  
Vol 44 (7-8) ◽  
pp. 609-616 ◽  
Author(s):  
Kun Hoe Chung ◽  
Kwang Yun Cho ◽  
Yasuko Asami ◽  
Nobutaka Takahashi ◽  
Shigeo Yoshida
Keyword(s):  
Electron Transport ◽  
Respiratory Chain ◽  
Side Chain ◽  
Pyridine Derivatives ◽  
Transport Function ◽  
Optimal Length ◽  
Structure Activity ◽  
Membrane Effect ◽  
Relationship Of ◽  
Derivatives Of

Many derivatives of 2,3-dim ethoxy-4-hydroxypyridine, which were designed from examination of the structure-activity relationship of piericidins, were tested for inhibition of NADH-UQ reductase. The lipophilic side chain of those compounds was indicated to be a key part for activity and its optimal length was conjectured. By the use of two different phases of assay material, intact mitochondria and submitochondria, the size of a membrane effect was shown to depend on the structure of the side chain. 4-Hydroxyquinoline derivatives were also tested for an analogous role in relation to the electron transport function of menaquinone, and they were proven to be inhibitors of NADH-UQ reductase as good as the pyridine derivatives.

scholarly journals Cultivation at high osmotic pressure confers ubiquinone 8–independent protection of respiration on Escherichia coli

2019 ◽  
Vol 295 (4) ◽  
pp. 981-993 ◽  
Author(s):  
Laura Tempelhagen ◽  
Anita Ayer ◽  
Doreen E. Culham ◽  
Roland Stocker ◽  
Janet M. Wood
Keyword(s):  
Oxidative Stress ◽  
Gene Expression ◽  
Escherichia Coli ◽  
Electron Transfer ◽  
Oxygen Uptake ◽  
Osmotic Pressure ◽  
Respiratory Chain ◽  
Membrane Lipid ◽  
E Coli ◽  
Uptake Rates

Ubiquinone 8 (coenzyme Q8 or Q8) mediates electron transfer within the aerobic respiratory chain, mitigates oxidative stress, and contributes to gene expression in Escherichia coli. In addition, Q8 was proposed to confer bacterial osmotolerance by accumulating during growth at high osmotic pressure and altering membrane stability. The osmolyte trehalose and membrane lipid cardiolipin accumulate in E. coli cells cultivated at high osmotic pressure. Here, Q8 deficiency impaired E. coli growth at low osmotic pressure and rendered growth osmotically sensitive. The Q8 deficiency impeded cellular O2 uptake and also inhibited the activities of two proton symporters, the osmosensing transporter ProP and the lactose transporter LacY. Q8 supplementation decreased membrane fluidity in liposomes, but did not affect ProP activity in proteoliposomes, which is respiration-independent. Liposomes and proteoliposomes prepared with E. coli lipids were used for these experiments. Similar oxygen uptake rates were observed for bacteria cultivated at low and high osmotic pressures. In contrast, respiration was dramatically inhibited when bacteria grown at the same low osmotic pressure were shifted to high osmotic pressure. Thus, respiration was restored during prolonged growth of E. coli at high osmotic pressure. Of note, bacteria cultivated at low and high osmotic pressures had similar Q8 concentrations. The protection of respiration was neither diminished by cardiolipin deficiency nor conferred by trehalose overproduction during growth at low osmotic pressure, but rather might be achieved by Q8-independent respiratory chain remodeling. We conclude that osmotolerance is conferred through Q8-independent protection of respiration, not by altering physical properties of the membrane.

scholarly journals Photoinduced electron-transfer chemistry of the bielectrophoric N-phthaloyl derivatives of the amino acids tyrosine, histidine and tryptophan

2011 ◽  
Vol 7 ◽  
pp. 518-524 ◽  
Author(s):  
Axel G Griesbeck ◽  
Jörg Neudörfl ◽  
Alan de Kiff
Keyword(s):  
Amino Acids ◽  
Electron Transfer ◽  
Photoinduced Electron Transfer ◽  
Bond Cleavage ◽  
Derivatives Of

The photochemistry of phthalimide derivatives of the electron-rich amino acids tyrosine, histidine and tryptophan 8–10 was studied with respect to photoinduced electron-transfer (PET) induced decarboxylation and Norrish II bond cleavage. Whereas exclusive photodecarboxylation of the tyrosine substrate 8 was observed, the histidine compound 9 resulted in a mixture of histamine and preferential Norrish cleavage. The tryptophan derivative 10 is photochemically inert and shows preferential decarboxylation only when induced by intermolecular PET.

scholarly journals Five decades of research on mitochondrial NADH-quinone oxidoreductase (complex I)

2018 ◽  
Vol 399 (11) ◽  
pp. 1249-1264 ◽  
Author(s):  
Tomoko Ohnishi ◽  
S. Tsuyoshi Ohnishi ◽  
John C. Salerno
Keyword(s):  
Electron Transfer ◽  
Respiratory Chain ◽  
Complex I ◽  
Proton Translocation ◽  
Atp Synthesis ◽  
Mitochondrial Respiratory Chain ◽  
Proton Pumping ◽  
Entry Site ◽  
Quinone Oxidoreductase ◽  
Terminal Electron Acceptor

AbstractNADH-quinone oxidoreductase (complex I) is the largest and most complicated enzyme complex of the mitochondrial respiratory chain. It is the entry site into the respiratory chain for most of the reducing equivalents generated during metabolism, coupling electron transfer from NADH to quinone to proton translocation, which in turn drives ATP synthesis. Dysfunction of complex I is associated with neurodegenerative diseases such as Parkinson’s and Alzheimer’s, and it is proposed to be involved in aging. Complex I has one non-covalently bound FMN, eight to 10 iron-sulfur clusters, and protein-associated quinone molecules as electron transport components. Electron paramagnetic resonance (EPR) has previously been the most informative technique, especially in membranein situanalysis. The structure of complex 1 has now been resolved from a number of species, but the mechanisms by which electron transfer is coupled to transmembrane proton pumping remains unresolved. Ubiquinone-10, the terminal electron acceptor of complex I, is detectable by EPR in its one electron reduced, semiquinone (SQ) state. In the aerobic steady state of respiration the semi-ubiquinone anion has been observed and studied in detail. Two distinct protein-associated fast and slow relaxing, SQ signals have been resolved which were designated SQNfand SQNs. This review covers a five decade personal journey through the field leading to a focus on the unresolved questions of the role of the SQ radicals and their possible part in proton pumping.

scholarly journals Oxygen Sensing and HIF-1 Activation Does Not Require an Active Mitochondrial Respiratory Chain Electron-transfer Pathway

2001 ◽  
Vol 276 (25) ◽  
pp. 21995-21998 ◽  
Author(s):  
Vickram Srinivas ◽  
Irene Leshchinsky ◽  
Nianli Sang ◽  
Michael P. King ◽  
Alex Minchenko ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Respiratory Chain ◽  
Oxygen Sensing ◽  
Mitochondrial Respiratory Chain ◽  
Electron Transfer Pathway ◽  
Mitochondrial Respiratory
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