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Supercapacitors Based on c‐Type Cytochromes Using Conductive Nanostructured Networks of Living Bacteria [PDF]
ChemPhysChem, 2012 Supercapacitors have attracted interest in energy storage because they have the potential to complement or replace batteries. Here, we report that c ‐type cytochromes, naturally immersed in a living, electrically conductive microbial biofilm, greatly ...
Nikhil S Malvankar, Derek R Lovley
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Reactions of mercaptans with cytochrome c oxidase and cytochrome c
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 19801. The steady-state oxidation of ferrocytochrome c by dioxygen catalyzed by cytochrome c oxidase, is inhibited non-competitively towards cytochrome c by methanethiol, ethanethiol, 1-propanethiol and 1-butanethiol with Ki values of 4.5, 91, 200 and 330 microM, respectively. 2.
J, Wilms, J, Lub, R, Wever
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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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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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International Journal of Biochemistry, 1978
Abstract Enzymatic methylation of 72 lysyl residue of cytochrome c in lower organisms facilitates its binding to mitochondria, and subsequently plays an important role in the electron transport ...
E, Polastro +4 more
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Abstract Enzymatic methylation of 72 lysyl residue of cytochrome c in lower organisms facilitates its binding to mitochondria, and subsequently plays an important role in the electron transport ...
E, Polastro +4 more
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Current Opinion in Structural Biology, 1996
Within the past year, the structures of the cytochrome c oxidase from the soil bacterium Paracoccus denitrificans and of the metal centers of the cytochrome c oxidase from bovine heart mitochondria, both determined at 2.8 A resolution by X-ray crystallography, have been reported. The structures form a basis for understanding the mechanism of this redox-
C, Ostermeier, S, Iwata, H, Michel
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Within the past year, the structures of the cytochrome c oxidase from the soil bacterium Paracoccus denitrificans and of the metal centers of the cytochrome c oxidase from bovine heart mitochondria, both determined at 2.8 A resolution by X-ray crystallography, have been reported. The structures form a basis for understanding the mechanism of this redox-
C, Ostermeier, S, Iwata, H, Michel
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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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A study of the kinetics of the oxidation of cytochrome c by cytochrome c oxidase
Archives of Biochemistry and Biophysics, 1956Abstract 1. 1. The kinetics of the oxidation of ferrocytochrome c by cytochrome c oxidase were studied spectrophotometrically by observing the rate of decrease in optical density at the α, β, or γ band of ferrocytochrome c as the reduced cytochrome c is oxidized. 2. 2.
H, CONRAD, L, SMITH
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Brownian Dynamics of Cytochrome c and Cytochrome c Peroxidase Association
Science, 1988Brownian dynamics computer simulations of the diffusional association of electron transport proteins cytochrome c (cyt c) and cytochrome c peroxidase (cyt c per) were performed. A highly detailed and realistic model of the protein structures and their electrostatic interactions was used that was based on an atomic-level spatial description.
S H, Northrup, J O, Boles, J C, Reynolds
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