Results 211 to 220 of about 24,782 (251)
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Cytochrome b of the Respiratory Chain
1985As originally pointed out by Keilin and Hartree (1939), to whom we owe most of the basic definitions in this general field, cytochrome b can be distinguished from the other cytochromes of the respiratory chain, i.e., c and aa 3, on the basis of the following characteristic properties: an oxidation reduction potential permitting its ready reduction by ...
Henry R. Mahler, Philip S. Perlman
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Molecular and General Genetics MGG, 1991
The products of the nuclear genes CBS1 and CBS2 are both required for translational activation of mitochondrial apocytochrome b in yeast. We report the intramitochondrial localization of both proteins by use of specific antisera. Based on its solubilization properties the CBS1 protein is presumed to be a component of the mitochondrial membrane; the ...
U, Michaelis, A, Körte, G, Rödel
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The products of the nuclear genes CBS1 and CBS2 are both required for translational activation of mitochondrial apocytochrome b in yeast. We report the intramitochondrial localization of both proteins by use of specific antisera. Based on its solubilization properties the CBS1 protein is presumed to be a component of the mitochondrial membrane; the ...
U, Michaelis, A, Körte, G, Rödel
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Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1981
1. The kinetics of cytochrome b reduction and oxidation in the ubiquinone-cytochrome b/c2 oxidoreductase of chromatophores from Rhodopseudomonas sphaeroides Ga have been measured both in the presence and absence of antimycin, after subtraction of contributions due to absorption changes from cytochrome c2, the oxidized bacteriochlorophyll dimer of the ...
D P, O'Keefe, P L, Dutton
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1. The kinetics of cytochrome b reduction and oxidation in the ubiquinone-cytochrome b/c2 oxidoreductase of chromatophores from Rhodopseudomonas sphaeroides Ga have been measured both in the presence and absence of antimycin, after subtraction of contributions due to absorption changes from cytochrome c2, the oxidized bacteriochlorophyll dimer of the ...
D P, O'Keefe, P L, Dutton
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Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1970
Abstract 1. Both antimycin and ATP induce a red shift of the b band when added to succinate-reduced rat-heart mitochondria in the absence of oxygen. The intensity of the new band is greater with antimycin than with ATP, and the two effects are not additive, since ATP has only a slight effect in the presence of antimycin. 2.
H J, Wegdam, J A, Berden, E C, Slater
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Abstract 1. Both antimycin and ATP induce a red shift of the b band when added to succinate-reduced rat-heart mitochondria in the absence of oxygen. The intensity of the new band is greater with antimycin than with ATP, and the two effects are not additive, since ATP has only a slight effect in the presence of antimycin. 2.
H J, Wegdam, J A, Berden, E C, Slater
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Assembly of Transmembrane b-Type Cytochromes and Cytochrome Complexes
2016Cytochromes are involved in charge-transfer reactions, and many cytochromes contain a transmembrane domain and are part of membrane-localized electron transfer chains. Protoporphyrin IX (heme b) is the first heme product in the tetrapyrrole/heme biosynthesis pathway.
Koch, Hans-Georg, Schneider, Dirk
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1986
Publisher Summary This chapter describes the purification of neutrophilic leukocytes from peripheral blood, the isolation of their membranes that are enriched in the cytochrome, the preparation of a solubilized oxidase, and the purification of the cytochrome itself.
Anthony W. Segal +3 more
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Publisher Summary This chapter describes the purification of neutrophilic leukocytes from peripheral blood, the isolation of their membranes that are enriched in the cytochrome, the preparation of a solubilized oxidase, and the purification of the cytochrome itself.
Anthony W. Segal +3 more
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1955
Publisher Summary Cytochrome b of mammalian tissue is a hemoprotein which in the reduced (ferrous) form has absorption bands centered at 564 mμ (α), 530 mμ (β), and 430 mμ (γ). In heart muscle extracts which contain both an active succinic dehydrogenase and cytochrome oxidase, the addition of succinate causes reduction of cytochrome b and aeration ...
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Publisher Summary Cytochrome b of mammalian tissue is a hemoprotein which in the reduced (ferrous) form has absorption bands centered at 564 mμ (α), 530 mμ (β), and 430 mμ (γ). In heart muscle extracts which contain both an active succinic dehydrogenase and cytochrome oxidase, the addition of succinate causes reduction of cytochrome b and aeration ...
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Genetics and biogenesis of cytochrome b.
Methods in enzymology, 1984We have reviewed here the genetic methods used for isolating and manipulating nuclear and mitochondrial mutants of bakers' yeast that affect the function and biogenesis of complex III of the mitochondrial respiratory chain. All the methods have been used with success in the past, and it is hoped that this compilation will aid biochemists in using these
P S, Perlman, H R, Mahler
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1975
Publisher Summary Type b cytochromes are electron-carrying proteins, which contain protoheme IX as the prosthetic group. The position of α band of their absorption spectra in the ferrous state ranges from 554 to 566 nm. By the pyridine treatment they give the pyridine-protohemochrome with its α band at 556 nm.
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Publisher Summary Type b cytochromes are electron-carrying proteins, which contain protoheme IX as the prosthetic group. The position of α band of their absorption spectra in the ferrous state ranges from 554 to 566 nm. By the pyridine treatment they give the pyridine-protohemochrome with its α band at 556 nm.
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