Results 211 to 220 of about 365,101 (261)
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Journal of Inorganic Biochemistry, 1985
The identification of two functionally distinct states, called pulsed and resting, has led to a number of investigations on the conformational variants of the enzyme. However, the catalytic properties of cytochrome oxidase may depend on a number of experimental conditions related to the solvent as well as to the protocol followed to determine the ...
G. Antonini +4 more
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The identification of two functionally distinct states, called pulsed and resting, has led to a number of investigations on the conformational variants of the enzyme. However, the catalytic properties of cytochrome oxidase may depend on a number of experimental conditions related to the solvent as well as to the protocol followed to determine the ...
G. Antonini +4 more
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Charge interactions of cytochrome c with cytochrome c oxidase
International Journal of Biochemistry, 1984The pyridoxal phosphate (PLP) modification of the lysine amino groups in cytochrome c causes decrease in the reaction rate with cytochrome c oxidase. The rate constants for (PLP)2-cyt. c, PLP(Lys 86)-cyt. c, PLP(Lys 79)-cyt. c and native cytochrome c (at pH 7.4, I = 0.02) are 3.6 X 10(-3) sec-1, 5.5 X 10(-3) sec-1, 5.2 X 10(-3) sec-1 and 9.8 X 10(-3 ...
M I, Mitovska +2 more
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The cytochrome c binding site on cytochrome c oxidase
Biochemical and Biophysical Research Communications, 1979Abstract Cytochrome c was chemically coupled to cytochrome c oxidase using the reagent 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC) which couples amine groups to carboxyl residues. The products of this reaction were analyzed on 2.5–27% polyacrylamide gradient gels electrophoretically.
C H, Seiter, R, Margalit, R A, Perreault
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2002
Cytochrome oxidase is the terminal oxidase of most of aerobic organisms and reduces molecular oxygen (O2) to water (1). The electrons and protons required for the formation of water molecules are transferred from both sides of the mitochondrial inner membranes in eukaryotic cells and of the cell membrane in prokaryotic cells (1).
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Cytochrome oxidase is the terminal oxidase of most of aerobic organisms and reduces molecular oxygen (O2) to water (1). The electrons and protons required for the formation of water molecules are transferred from both sides of the mitochondrial inner membranes in eukaryotic cells and of the cell membrane in prokaryotic cells (1).
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The oxidation of cytochrome c by cytochrome c peroxidase
Archives of Biochemistry and Biophysics, 1960Abstract 1. 1. The reaction between cytochrome c and cytochrome c peroxidase is first order in cytochrome c. 2. 2. The reaction is inhibited by both oxidized and reduced cytochrome c. 3. 3. The dependence of the reaction rate on ionic strength suggests that the reaction occurs at oppositely charged active sites on the two proteins. 4.
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Cytochrome c Peroxidase–Cytochrome c Complexes
2015The yeast cytochrome c peroxidase (CCP)–cytochrome c (cytc) electron transfer system has been critically important in deciphering the molecular level details of protein–protein interactions and electron transfer. The crystal structure of the CCP–cytc together with a number mutagenesis, enzymological, and spectroscopic studies have provided a detailed ...
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IUBMB Life, 2013
AbstractCytochromes c are central proteins in energy transduction processes by virtue of their functions in electron transfer in respiration and photosynthesis. They have heme covalently attached to a characteristic CXXCH motif via protein‐catalyzed post‐translational modification reactions.
Despoina A I, Mavridou +2 more
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AbstractCytochromes c are central proteins in energy transduction processes by virtue of their functions in electron transfer in respiration and photosynthesis. They have heme covalently attached to a characteristic CXXCH motif via protein‐catalyzed post‐translational modification reactions.
Despoina A I, Mavridou +2 more
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Biochemistry and Cell Biology, 1989
In this review, protein methylation is outlined in general terms, highlighting the major amino acids that are methylated and some of the proteins in which they are found. The majority of the review examines the methylation of cytochrome c at Lys-77 of lower eukaryotes as a possible model for methylation studies.
W K, Paik, Y B, Cho, B, Frost, S, Kim
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In this review, protein methylation is outlined in general terms, highlighting the major amino acids that are methylated and some of the proteins in which they are found. The majority of the review examines the methylation of cytochrome c at Lys-77 of lower eukaryotes as a possible model for methylation studies.
W K, Paik, Y B, Cho, B, Frost, S, Kim
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Cytochromes c and Cytochrome c Containing Enzymes
1985Porphyrin-containing compounds fulfil many different roles in biological systems. Broadly speaking, they fall into two main categories. There are the carrier molecules in which the substance carried is either oxygen, as in the case of the haemoglobins and myoglobins, or electrons, as in the cytochromes.
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2015
Cytochromes c′ are a group of class IIa cytochromes with pentacoordinate haem centres and are found in photosynthetic, denitrifying and methanotrophic bacteria. Their function remains unclear, although roles in nitric oxide (NO) trafficking during denitrification or in cellular defence against nitrosoative stress have been proposed.
Hough, Michael A, Andrew, Colin R
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Cytochromes c′ are a group of class IIa cytochromes with pentacoordinate haem centres and are found in photosynthetic, denitrifying and methanotrophic bacteria. Their function remains unclear, although roles in nitric oxide (NO) trafficking during denitrification or in cellular defence against nitrosoative stress have been proposed.
Hough, Michael A, Andrew, Colin R
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