Results 161 to 170 of about 25,921 (203)
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Utility and Evolution of Cytochrome b in Insects
Molecular Phylogenetics and Evolution, 2001Cytochrome b (cyt-b) is widely used in molecular phylogenetic studies of vertebrate, but not invertebrate, taxa. To determine whether this situation is an historical accident or reflects the utility of cyt-b, we compared the abilities of cyt-b, COI, and one nuclear ribosomal gene region (D1 of 28S) to recover intergeneric relationships within the tiger
Rebecca B. Simmons, Susan J. Weller
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Interaction of cytochrome b₅ and cytochrome c [PDF]
, 1989 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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High-energy Forms of Cytochrome b
Nature, 1970SUB-MITOCHONDRIAL particles prepared from horse or ox heart contain two species of cytochrome b in equal amounts, one (bi) affected by antimycin and the other (b) not affected1–3. In addition to its well known inhibitory effect on the respiratory chain, acting between cytochromes b and c1, antimycin brings about an increased reduction of the total ...
E. C. Slater +7 more
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Oxidoreduction of cytochrome b in the presence of antimycin
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1972Abstract 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.
Jan A. Berden, Mårten Wikström
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Multiple cytochromes b in Mycobacterium phlei
Biochemical and Biophysical Research Communications, 1973Abstract 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).
Eitan Bogin +3 more
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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.
Walter Colli, Isaias Raw
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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.
Walter Colli, Isaias Raw
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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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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.
Tateo Yamanaka +2 more
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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.
Tateo Yamanaka +2 more
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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 ...
Diana S. Beattie, Shanker Japa
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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 ...
Diana S. Beattie, Shanker Japa
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Structural Gene of Cytochrome b-562 from the Cytochrome b-c1 Complex of Rhodobacter sphaeroides1
The Journal of Biochemistry, 1987The structural gene coding for cytochrome b-562 isolated from the cytochrome b-c1 complex of Rhodobacter (Rhodopseudomonas) sphaeroides has been cloned. Its nucleotide sequence has been determined and the amino acid sequence was deduced therefrom. It consists of 157 amino acids (Mr 17,237) and contains four hydrophobic segments.
Toshiyuki Miyata +3 more
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