Studies on the electron transfer system IV. The electron transfer particle

Crane, F.L.; Glenn, James L.; Green, D.E.

doi:10.1016/0006-3002(56)90058-0

Cited by 572 publications

(83 citation statements)

References 10 publications

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“…SMPs, which mainly constitute insideout vesicles of the inner mitochondrial membrane, were prepared as described previously (26). Fluorescence measurements were carried out at room temperature on a Shimadzu RF5001 PC spectrofluorimeter (Shimadzu, Duisburg, Germany) using 4-ml quartz cuvettes that contained 2 ml of 10 mM Tris-HCl buffer, pH 7.4.…”

Section: Methodsmentioning

confidence: 99%

Investigations into Calcium-dependent Membrane Association of 15-Lipoxygenase-1

Walther

Wiesner

Kühn

2004

Journal of Biological Chemistry

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Taken together these data suggest that 15-lipoxygenase-1 associates to biomembranes primarily via hydrophobic interactions between surface-exposed apolar amino acid side chains and membrane lipids. Calcium supports membrane binding probably by forming salt bridges between the negatively charged head groups of membrane phospholipids and acidic surface amino acids of the membrane contact plane and this interaction might contribute to overcome repulsive forces.

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Section: Methodsmentioning

confidence: 99%

Investigations into Calcium-dependent Membrane Association of 15-Lipoxygenase-1

Walther

Wiesner

Kühn

2004

Journal of Biological Chemistry

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“…SMPs, which mainly constitute insideout vesicles of the inner mitochondrial membrane, were prepared as described previously (35). The missing amino acids in the crystal structure of the rabbit reticulocyte 15-LOX were modeled in using the SwissPdbViewer (www.expasy.ch/spdbv; Ref.…”

Section: Methodsmentioning

confidence: 99%

The N-terminal Domain of the Reticulocyte-type 15-Lipoxygenase Is Not Essential for Enzymatic Activity but Contains Determinants for Membrane Binding

Walther¹,

Anton²,

Wiedmann³

et al. 2002

Journal of Biological Chemistry

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The rabbit reticulocyte-type 15-lipoxygenase is capable of oxygenating biomembranes and lipoproteins without the preceding action of ester lipid cleaving enzymes. This reaction requires an efficient membrane binding, and the N-terminal ␤-barrel domain of the enzyme has been implicated in this process. To obtain detailed information on the structural requirements for membrane oxygenation, we expressed the rabbit wildtype 15-lipoxygenase, its ␤-barrel deletion mutant (catalytic domain), and several lipoxygenase point mutations as His-tagged fusion proteins in Escherichia coli and tested their membrane binding characteristics. We found that: (i) the ␤-barrel deletion mutant was catalytically active and its enzymatic properties (K M , V max , pH optimum, substrate specificity) were similar to those of the wild-type enzyme; (ii) when compared with the wildtype lipoxygenase, the membrane binding properties of the N-terminal truncation mutant were impaired but not abolished, suggesting a role of the catalytic domain in membrane binding; and (iii) Phe-70 and Leu-71 (constituents of the ␤-barrel domain) but also Trp-181, which is located in the catalytic domain, were identified as sequence determinants for membrane binding. Mutation of these amino acids to more polar residues (F70H, L71K, W181E) impaired the membrane binding capacity of the recombinant enzyme. These data indicate that the C-terminal catalytic domain of the rabbit 15-lipoxygenase is enzymatically active and that the membrane binding properties of the enzyme are determined by a concerted action of the N-terminal ␤-barrel and the C-terminal catalytic domain.

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“…Large scale isolation of mitochondria from beef heart muscle was carried out under conditions that minimized contamination by other cell particulates and by myosin (5,11). Suspensions in 0.5 M sucrose (kept at 0 to 5 °) conformed to the most rigorous standards for preservation of mitochondrial structure and activity.…”

Section: Isolation Of Mitochondriamentioning

confidence: 99%

A Macromolecular Repeating Unit of Mitochondrial Structure and Function

Fernández-Morán

Oda

Blair

et al. 1964

The Journal of Cell Biology

350

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A repeating particle associated with the cristae and the inner membrane of the external envelope has been recognized and characterized in beef heart mitochondria by correlated electron microscopic and biochemical studies. Many thousands (ca. 104 to 105) of these particles, disposed in regular arrays, are present in a single mitochondrion. The repeating particle, called the elementary particle (EP), consists of three parts: (1) a spherical or polyhedral head piece (80 to 100 A in diameter); (2) a cylindrical stalk (about 50 A long and 30 to 40 A wide); and (3) a base piece (40 X 110 A). The base pieces of the elementary particles form an integral part of the outer dense layers of the cristae. The elementary particles can be seen in electron micrographs of mitochondria in situ, of isolated mitochondria, and of submitochondrial particles with a complete electron transfer chain. Negative staining with phosphotungstate is only one of several techniques that can be used for reproducible demonstration of the repeating particles and underlying subunit organization of mitochondrial membranes. A particulate unit containing a complete electron transfer chain can be isolated from beef heart mitochondria. The isolated unit approximates in size that of the elementary particle in situ. The molecular weight of the particle in situ is calculated to be 1.3 X 10 ~. Evidence is presented for identifying the isolated unit with the elementary particle visualized in situ. The elementary particle of the mitochondrion is believed to be a prototype of a class of functional particles or macromolecular assemblies of similar size found in association with membranes generally.

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Studies on the electron transfer system IV. The electron transfer particle

Cited by 572 publications

References 10 publications

Investigations into Calcium-dependent Membrane Association of 15-Lipoxygenase-1

Investigations into Calcium-dependent Membrane Association of 15-Lipoxygenase-1

The N-terminal Domain of the Reticulocyte-type 15-Lipoxygenase Is Not Essential for Enzymatic Activity but Contains Determinants for Membrane Binding

A Macromolecular Repeating Unit of Mitochondrial Structure and Function

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