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pro vyhledávání: '"Brian A. C. Ackrell"'
Autor:
Brian A. C. Ackrell
Publikováno v:
Molecular Aspects of Medicine. 23:369-384
Complex II (succinate–ubiquinone oxidoreductase) is the smallest complex in the respiratory chain and contains four nuclear-encoded subunits SdhA, SdhB, SdhC, and SdhD. It functions both as a respiratory chain component and an essential enzyme of t
Publikováno v:
Journal of the American Chemical Society. 119:7434-7439
Protein-film voltammetry reveals the global effects of H/D isotopic substitutions, both in organic substrates and solvent, on bidirectional catalytic electron transport in a mitochondrial respiratory enzyme, succinate dehydrogenase. The voltammetry i
Autor:
Hideto Miyoshi, Brian A. C. Ackrell, Rona R. Ramsay, Victoria Yankovskaya, Thomas P. Singer, Gary Cecchini, Sergei O. Sablin
Publikováno v:
Journal of Biological Chemistry. 271:21020-21024
The structural and catalytic properties of beef heart succinate dehydrogenase (succinate-ubiquinone oxidoreductase, complex II) and Escherichia coli fumarate reductase are remarkably similar. One exception is that whereas electron exchange between th
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1271:211-219
This paper examines the experimental foundations of reports in the literature on mitochondrial diseases involving Complexes I and II of the respiratory chain. Many of the reports may be questioned on the basis of the assay conditions used which disre
Publikováno v:
Journal of Biological Chemistry. 268:815-822
Escherichia coli fumarate reductase (FRD) is a four-subunit enzyme that catalyzes the terminal step in anaerobic respiration to fumarate. The hydrophobic FrdC and FrdD subunits anchor the FrdA and FrdB catalytic subunits to the inner surface of the c
Publikováno v:
Journal of Biological Chemistry. 266:13572-13579
Menaquinol-fumarate oxidoreductase of Escherichia coli is a four-subunit membrane-bound complex that catalyzes the final step in anaerobic respiration when fumarate is the terminal electron acceptor. The enzyme is structurally and catalytically simil
Autor:
Mark T. Werth, Michael K. Johnson, R. P. Gunsalus, Imke Schröder, Anamaria Manodori, Gary Cecchini, Brian A. C. Ackrell
Publikováno v:
Proceedings of the National Academy of Sciences. 87:8965-8969
Site-directed mutants of Escherichia coli fumarate reductase in which each of the four N-terminal cysteine residues in the FrdB subunit, residues 57, 62, 65, and 77, was mutated individually to serine have been constructed, overexpressed, and investi
Publikováno v:
Journal of Biological Chemistry. 265:19560-19567
Fumarate reductase (FRD) of Escherichia coli is a four-subunit membrane-bound complex that is synthesized during anaerobic growth when fumarate is available as a terminal oxidant. The two subunits that comprise the catalytic domain, FrdA and FrdB, ar
Publikováno v:
The Journal of biological chemistry. 281(6)
Mice that lack the mitochondrial form of superoxide dismutase (SOD2) incur severe pathologies and mitochondrial deficiencies, including major depletion of complex II, as a consequence of buildup of endogenous reactive oxygen species (Melov, S., Cosku
Autor:
Elena Maklashina, Brian A. C. Ackrell
Publikováno v:
Aging cell. 3(1)
Summary The bulwark of the mitochondrial theory of aging is that a defective respiratory chain initiates the death cascade. The increased production of superoxide is suggested to result in progressive oxidant damage to cellular components and particu