Results 241 to 250 of about 26,184 (298)
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Halobacterium halobium Cytochrome b-558 and Cytochrome b-562: Purification and Some Properties

The Journal of Biochemistry, 1993
Four different membrane-bound b-type cytochromes were found to occur in Halobacterium halobium strain L-33, and two of them, b-558 and b-562, were purified to homogeneity. Cytochrome b-558 showed absorption peaks at 414 and 526 nm in the oxidized form, and peaks at 425, 528, and 558 nm in the reduced form.
T, Fujiwara, Y, Fukumori, T, Yamanaka
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Evaluation of the Cytochrome b5/Cytochrome b5 Reductase Pathway

Current Protocols in Toxicology, 2005
AbstractNADH cytochrome b5 reductase (b5R; EC 1.6.2.2; Diaphorase I; NADH: ferricytochrome b5 oxidoreductase) is an FAD‐containing protein, which, along with the hemoprotein cytochrome b5 (cyt b5), mediates electron transfer from NADH to fatty acid desaturases, P450 oxidases, methemoglobin, and ascorbyl free radical.
Lauren A, Trepanier   +2 more
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Assembly of chloroplast cytochromes b and c

Biochimie, 2000
The synthesis of holocytochromes in plastids is a catalyzed process. Several proteins, including plastid CcsA, Ccs1, possibly CcdA and a thioredoxin, plus at least two additional Ccs factors, are required in sub-stoichiometric amounts for the conversion of apocytochromes f and c(6) to their respective holoforms.
S S, Nakamoto, P, Hamel, S, Merchant
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Utility and Evolution of Cytochrome b in Insects

Molecular Phylogenetics and Evolution, 2001
Cytochrome 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
R B, Simmons, S J, Weller
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Cytochrome b and photosynthetic sulfur bacteria

Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1975
Chromatophores isolated from the purple sulfur bacterium Chromatium and the green sulfur bacterium Chlorobium exhibit absorbance changes in the cytochrome alpha-band region consistent with the presence of a b-type cytochrome. Cytochrome content determined by reduced minus oxidized difference spectra and by heme photochemically active ...
D B, Knaff, B B, Buchanan
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High-energy Forms of Cytochrome b

Nature, 1970
SUB-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   +3 more
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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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