4 Metal-Containing Flavoprotein Dehydrogenases

Hatefi, Youssef; Stiggall, Diana L.

doi:10.1016/s1874-6047(08)60242-5

Cited by 62 publications

(49 citation statements)

References 256 publications

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“…The preparation was enriched in two polypeptides with apparent mol wt of 67,000 and 30,000 D. These polypeptides migrated with mol wt similar to those reported for the two subunits from both mammalian and yeast SDH (1,4,10,25). The ubiquinone reductase activity to complex 11 (29).…”

Section: Methodssupporting

confidence: 57%

“…Maintenance of an active preparation of SDH in a homogeneous form requires low temperatures, anaero-'Supported in part by a grant from the National Institute of General Medical Sciences (USPHS GM26095) to J. N. S. Cooperative investigation of the United States Department of Agriculture, Agricultural Research biosis, and the presence of protective agents (4,10,25). Partially purified SDH preparations from higher plants have been reported in only a few cases and in none are extensive characterizations of the properties of the resulting products presented (11,12,19).…”

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confidence: 99%

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Succinate Dehydrogenase

Burke

Siedow²,

Moreland³

1982

Plant Physiol.

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A procedure was developed for the partial purification of succinate dehydrogenase from mung bean ( Vigna radiata L.) hypocotyls and soybean (Glycine max ILl Meff. v. Ransom) cotyledons. The procedure utilized a Triton X-100 extraction foDlowed by ammonium sulfate precipitation. The final fraction was enriched in two polypeptides with approximate molecular weights of 67,000 and 30,000 daltons, exhibited a pH optima of 7.0 to 7.5, contained a b-type cytochrome, and exhibited the characteristic ferredoxintype and high potential iron-sulfur protein-type electron paramagnetic resonance signals reported for the iron-sulfur centers of mammalian succinate dehydrogenase. Inhibition constants of 1.15 and 24.6 micromolar for oxaloacetate and malonate, respectively, were obtained.

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Section: Methodssupporting

confidence: 57%

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confidence: 99%

Succinate Dehydrogenase

Burke

Siedow²,

Moreland³

1982

Plant Physiol.

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“…The NADH dehydrogenase system of mitochondria, however, is so complex, "perhaps the most complex of all flavoproteins" (18), that analogy to other proteins may be inappropriate. In the preparations used here, no effort was made to remove membrane phospholipids which are integral to functioning mitochondrial NADH dehydrogenase (19). Theoretically, therefore, the kinetic differences observed could be a reflection of altered amounts or types of mitochondrial phospholipid in cells of the three genotypes.…”

Section: Resultsmentioning

confidence: 99%

Mitrochondrial NADH dehydrogenase in cystic fibrosis.

Shapiro¹,

Feigal²,

Lam³

1979

Proc. Natl. Acad. Sci. U.S.A.

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We have shown that skin fibroblasts from patients with cystic fibrosis (CF) and from carriers for CF [heterozygotes (HZ)] consume more 02 than do their controls. When the mitochondrial electron transport inhibitor rotenone was added to the cells, the relative inhibition of 02 consumption was CF > HZ > controls (P < 0.005 in both comparisons). Because rotenone specifically inhibits NADH dehydrogenase, [NADH:(acceptor) oxidoreductase, EC 1.6.99.31, which is the enzyme of energy-conserving site 1 of the mitochondrial electron transport system, activity and kinetics of this enzyme system were studied in fibroblast homogenates. NADH dehydrogenase activity was equal in cells from the three genotypes. At pH 8.0, affinity of the enzyme for its substrate was CF < HZ = controls; at pH 8.6, affinity was CF> HZ = controls (P < 0.005 for the differences). pH optima for the genotypes were without exception 8.6 (CF), 8.3 (HZ), and 8.0 (control). HZ and control lines were distinguished unequivocally in a blind test on the basis of differences in pH optima. Purified mitochondrial preparations revealed pH optima identical to those found in whole cell homogenates. These data suggest that the mutant gene responsible for CF is expressed in the complex mitochondrial NADH dehydrogenase system.

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“…luteus succinate dehydrogenase shares many of the features observed for similar enzymes isolated from other bacteria and from eukaryotic cells [8,13]. The precipitated enzyme contains equimolar amounts of four polypeptides, with relative molecular masses of 72, 30, 17 and 15 kDa.…”

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confidence: 81%

Characterization of succinate dehydrogenase from Micrococcus luteus (lysodeikticus) by electron‐spin‐resonance spectroscopy

Crowe

Owen

Patil

et al. 1983

European Journal of Biochemistry

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Low-temperature electron spin resonance spectroscopy has been used to study the biophysical properties of succinate dehydrogenase from the gram-positive bacterium Micrococcus luteus. The paramagnetic redox centres of the enzyme were identified in a succinate-dehydrogenase-antigen complex, which had been purified with the aid of monospecific serum from membranes solubilized with Triton X-I 00. The centres were characterized in further detail using the membrane-bound and Triton-solubilized forms of the enzyme. These studies distinguished two types of iron-sulphur centres, viz. a [4Fe-4SJ3+ cluster displaying a narrow signal at g = 2.01 in the oxidized state (conventionally termed centre S-3) and a [2Fe-2S] cluster with an axial signal at g = 2.03 and 1.93 in the reduced state (conventionally termed centre S-1).Centre S-3 had a mid-point redox potential of + 10 mV, a comparatively low value for this type of cluster. The behaviour of the g = 1.93 signal of centre S-I was a complex function of the redox potential, microwave power and temperature of measurement. When measured at low power (i.e. non-saturating conditions), the intensities observed for the g = 1.93 signal poised at various critical potentials in the redox titration were similar. However, the corresponding intensities differed markedly at high power, where conditions were saturating. It is proposed that under saturating conditions the spin-lattice relaxation of the [2Fe-2S] cluster S-I (mid-point potential + 70 mV) is enhanced by centre S-3 between the potential range + 10 -+ 70 mV and by an ESR-silent centre, termed centre S-2, with a mid-point potential of -295 mV.The paramagnetic centres of respiratory enzymes such as the metallo-flavoprotein succinate dehydrogenase can be analyzed conveniently by low-temperature electron spin resonance (ESR) spectroscopy [I]. The succinate dehydrogenases from mammalian, plant and yeast mitochondria as well as from photosynthetic bacteria have been examined in detail by this method [l -71. However, there have been no analogous studies on purified preparations of other bacterial succinate dehydrogenases. At least in part, this can be attributed to problems inherent in the purification of the enzyme from the membrane [8]. We have circumvented some of these problems recently, and have succeeded in isolating a succinate-dehydrogenaseantigen complex from the membranes of Micrococcus luteus 19, 101 and Escherichiu coli [I 1, 121 by selective precipitation with specific anti-(succinate dehydrogenase) immunoglobulins.In terms of its molecular properties, the M . luteus succinate dehydrogenase shares many of the features observed for similar enzymes isolated from other bacteria and from eukaryotic cells [8,13]. The precipitated enzyme contains equimolar amounts of four polypeptides, with relative molecular masses of 72, 30, 17 and 15 kDa. The 72-kDa polypeptide is known to be covalently linked to a flavin prosthetic group. In addition, the antigen complex contains non-haem iron and a h-type cytochrome (cytochrome b-556, [lo])....

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4 Metal-Containing Flavoprotein Dehydrogenases

Cited by 62 publications

References 256 publications

Succinate Dehydrogenase

Succinate Dehydrogenase

Mitrochondrial NADH dehydrogenase in cystic fibrosis.

Characterization of succinate dehydrogenase from Micrococcus luteus (lysodeikticus) by electron‐spin‐resonance spectroscopy

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