Results 201 to 210 of about 24,782 (251)
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Oxidoreduction of cytochrome b in the presence of antimycin

Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1972
Abstract 1. The effect of oxidizing equivalents on the redox state of cytochrome b in the presence of antimycin has been studied in the presence and absence of various redox mediators. 2. The antimycin-induced extra reduction of cytochrome b is always dependent on the initial presence of an oxidant such as oxygen.
M K, Wikström, J A, Berden
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Multiple cytochromes b in Mycobacterium phlei

Biochemical and Biophysical Research Communications, 1973
Abstract Electron transport particles from M. phlei contain at least 3 different active forms of cytochrome b, one reduced by NADH, with a λmax at 563 nm (bN563), and the other two reduced by either succinate or NADH, with λmax at 559 and 563 nm (bS559) and (bS563).
N S, Cohen   +3 more
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The triphasic reduction of cytochrome b in the succinate-cytochrome c reductase

Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1981
In the succinate-cytochrome c reductase, the reduction of cytochrome b has been found to be triphasic: an initial rapid partial reduction was followed first by a rapid oxidation and then finally by a slow reduction. The initial reduction of cytochrome b was faster than that of cytochrome c1 and the final slow reduction of cytochrome b began when ...
Y Z, Jin, H L, Tang, S L, Li, C L, Tsou
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Cytochrome b is necessary for the assembly of subunit VII in the cytochrome b-c1 complex of yeast mitochondria

Archives of Biochemistry and Biophysics, 1988
The synthesis and assembly of subunit VII, the Q-binding protein of the cytochrome b-c1 complex, into the inner mitochondrial membrane has been compared in wild-type yeast cells and in a mutant cell line lacking cytochrome b. Both immunoblotting and immunoprecipitation analysis with specific antiserum against subunit VII indicated that this subunit is ...
S, Japa, D S, Beattie
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The enigmatic cytochrome b-559 of oxygenic photosynthesis

Physiologia Plantarum, 1993
The ubiquitous and obligatory association of cytochrome b‐559 with the photosystem II reaction center of oxygenic photosynthesis is a conundrum since it seems not to have a function in the primary electron transport pathway of oxygen evolution. A model for the cytochrome structure that satisfies the cis‐positive rule for membrane protein assembly ...
William A, Cramer   +3 more
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Interaction of cytochrome b₅ and cytochrome c

2010
The interaction and kinetics of electron transfer between cytochrome b₅ and cytochrome c, two well characterised soluble electron transfer proteins, have been investigated by three techniques. First, fluorescence quenching experiments were done with cytochrome b₅ and porphyrin cytochrome c, a fluorescent analogue of cytochrome c.
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Crystalline Cytochrome b 5

Nature, 1959
CYTOCHROME c and b 5 are the only cytochromes isolated from animal tissues in purified soluble forms which are reducible by soluble flavoprotein. Further studies on the enzymatic and chemical properties of cytochrome b 5 are badly needed.
I, RAW, W, COLLI
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Evidence for a cytochrome b in green bacteria

Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1974
Abstract Chemical and photochemical evidence is presented for a low potential cytochrome b (C563) bound to the photochemical reaction center complex of green bacteria. This cytochrome undergoes reversible light-induced oxidation. The midpoint potential lies between 0.0 V and −150 mV.
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Mitochondrial Cytochrome b 560

1987
Cytochrome b 560 the succinate-ubiquinone (Q) reductase region of the mitochondrial electron transfer chain was first reported by Davis et al. (1,2). In spite of the detection of cytochrome b 560 in various succinate -Q1 reductase (3,4), and Complex II (5–7) preparations, this cytochrome has often been regarded as a contaminant of the denatured ...
Chang-An Yu, Linda Yu
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Biogenesis of Cytochrome Oxidase and Cytochrome b in Neurospora crassa

1975
In this article we would like to outline the close cooperation between the mitochondrial and cytoplasmic protein-synthesizing systems in mitochondrial biogenesis. The subject of our studies is two proteins of the mitochondrial membrane, cytochrome oxidase and cytochrome b.
Hanns Weiss   +2 more
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