Results 261 to 270 of about 50,722 (302)
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Some photoreactions of isolated cytochrome b-559
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1977Cytochrome b-559 was isolated from spinach and the alga Bumilleriopsis filiformis (Xanthophyceae) and characterized by functional properties: (a) It was active as electron acceptor in a diaphorase system using NADPH as donor and ferredoxin and ferredoxin-NADP reductase as redox proteins.
H J, Lach, H, Böhme, P, Böger
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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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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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Partial cytochrome b deficiency and generalized dystonia
Pediatric Neurology, 1990An 18-year-old female had clinical features of idiopathic torsion dystonia with bilateral hypodense putaminal lesions on computed tomography. Mitochondrial encephalomyopathy was suspected because of persistent lactic acidemia and myopathy. Studies of oxidative metabolism on isolated skeletal muscle mitochondria revealed partial cytochrome b deficiency ...
M A, Nigro +4 more
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Plasma Membrane b-Type Cytochromes
1998b-Type cytochromes (cyts) are a class of redox proteins well known from electron-transport chains found in mitochondria, chloroplasts and bacterial cell membranes. Their physiological function is dependent on the oxidation-reduction properties of the non-covalently bound heme prosthetic group.
Han Asard +3 more
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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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[132] Cytochrome b group (bacteria)
1955Publisher Summary This chapter discusses the determination of cytochrome b group form bacteria. The heme-containing pigments that have been called cytochrome b represent a group of proteins which not only differ from one another in physicochemical properties but probably differ as well in their catalytic function in the chain of respiratory enzymes ...
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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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