Zobrazeno 1 - 10
of 140
pro vyhledávání: '"B.F. Van Gelder"'
Autor:
B.F. Van Gelder, A.L. Lodder
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1186:67-74
Three preparations of cytochrome c oxidase, the preparation as traditionally prepared in our laboratory as described by Van Buuren (1992; PhD Thesis, University of Amsterdam), a preparation according to Volpe and Caughey (Biochem. Biophys. Res. Commu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dcd268d24486b714fbdf757a3159b718
https://doi.org/10.1016/0005-2728(94)90136-8
https://doi.org/10.1016/0005-2728(94)90136-8
Publikováno v:
Biochimica et biophysica acta. 1185(3)
The oxidation of the redox centres in reduced cytochrome c oxidase by hydrogen peroxide was studied by stopped-flow spectrophotometry in the absence and presence of reduced cytochrome c . The oxidation rate of cytochrome a decreased in the presence o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ca3f9cdc2c2bf408bceb186fd4d539f3
https://pubmed.ncbi.nlm.nih.gov/8180234
https://pubmed.ncbi.nlm.nih.gov/8180234
Autor:
A. C. F. Gorren, P. Nieboer, Henk L. Dekker, Anton O. Muijsers, B.F. Van Gelder, A. B. P. Van Kuilenburg
Publikováno v:
European journal of biochemistry. 205(3)
Human cytochrome c oxidase was purified in a fully active form from heart and skeletal muscle. The enzyme was selectively solubilised with octylglucoside and KCl from submitochondrial particles followed by ammonium sulphate fractionation. The prestea
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1699e465ad6e8dca0eddf4b6ea1b4af9
https://pubmed.ncbi.nlm.nih.gov/1315683
https://pubmed.ncbi.nlm.nih.gov/1315683
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 636:9-16
The kinetics of electron transfer between the isolated enzymes of cytochrome c1 and cytochrome c have been investigated using the stopped-flow technique. The reaction between ferrocytochrome c1 and ferricytochrome c is fast; the second-order rate con
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b1ceb3a168f0cc7b6d32698bcdd96add
https://doi.org/10.1016/0005-2728(81)90069-4
https://doi.org/10.1016/0005-2728(81)90069-4
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 460:290-298
1. 1. Hydrated electrons, produced by pulse radiolysis, react with porphyrin cytochrome c with a bimolecular rate constant of 3 · 10 10 M −1 · s −1 at 21 °C and pH 7.4. 2. 2. After the reduction step an absorbance change with a half-life of 5
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a655d2803fec2802f3b741c81e034aaf
https://doi.org/10.1016/0005-2728(77)90215-8
https://doi.org/10.1016/0005-2728(77)90215-8
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 593:17-23
1. The turnover number and apparent Km of isolated beef-heart cytochrome c oxidase were found to increase continuously when the pH was lowered from 8.6 to 4.6 (turnover number 32-630 s-1). In this pH range neither irreversible denaturation of the enz
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a9a6fa72d01117e3d2a4294c4dd8e9a9
https://doi.org/10.1016/0005-2728(80)90004-3
https://doi.org/10.1016/0005-2728(80)90004-3
Autor:
B.F. Van Gelder, H.F. Kauffman
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 333:218-227
1. 1. Cyanide (100 μM) causes a rapid disappearance of the band (648 nm) of oxidized cytochrome d in particles of Azotobacter vinelandii oxidizing NADH. The rate of disappearance of the band can be related to the rate of inhibition of the oxygen con
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f9ae92d81c3bcc8d9211efe181b6f319
https://doi.org/10.1016/0005-2728(74)90006-1
https://doi.org/10.1016/0005-2728(74)90006-1
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 682:264-272
The light-induced difference spectra of the fully reduced ( a 3+ a 2+ 3 -CO) complex and the mixed-valence carboxycytochrome c oxidase ( a 3+ a 2+ 3 -CO) during steady-state illumination and after flash photolysis showed marked differences. The diffe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aa187592509c8b44ff7ac031cf676b12
https://doi.org/10.1016/0005-2728(82)90107-4
https://doi.org/10.1016/0005-2728(82)90107-4
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 347:215-223
1. The photodissociation reaction of the cytochrome c oxidase-CO compound was studied by EPR at 15 °K. Illumination with white light at both room and liquid N 2 temperatures of the partially reduced cytochrome c oxidase (2 electrons per 4 metals) in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1caa21e716c3118a64883790eeb33bef
https://doi.org/10.1016/0005-2728(74)90046-2
https://doi.org/10.1016/0005-2728(74)90046-2
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 347:321-327
1. Treatment of phosphorylating ATP-Mg particles with antimycin in ethanolic solution results in a shift of the signal of low-spin ferric haem of cytochrome b -562 from g = 3.44 to 3.48. This shift is not caused by the ethanol. 2. The addition of ATP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9dbd64757374c3d1e61d08accb9968c1
https://doi.org/10.1016/0005-2728(74)90056-5
https://doi.org/10.1016/0005-2728(74)90056-5