1995
DOI: 10.1021/bi00008a035
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Abstract: Horse heart cytochrome c has been modified by 8-azido-ATP and the electron-transfer activity of the modified cytochrome c's to bovine heart cytochrome c oxidase (CcO) under physiological ionic strengths has been studied by the laser flash photolysis technique with 5-deazariboflavin and EDTA as the electron donor. The intermolecular electron transfer between the redox protein partners was shown to be extremely slow. The 8-azido-ATP-modified system exhibited less than 5% of the intracomplex electron-transfer rat… Show more

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Cited by 7 publications
(13 citation statements)
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References 27 publications
(49 reference statements)
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“…Attachment in the neighboring valley would be expected to inhibit cytochrome c function completely as it is at the site of interaction of the redox partners (2,35). Although this may be construed as compatible with the approximately 85% lowering of electron transfer to cytochrome oxidase shown by the two 8N 3 -ATP adducts (16), it would not be compatible with the smaller 60% inhibition of the transfer from the reductase (16) and the minimal effect that derivatization with 8N 3 -ADP has on binding of cytochrome oxidase and electron transfer (17), assuming the same site is involved.…”
Section: Tnp-8n 3 -Amp-irradiationmentioning
confidence: 99%
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“…Attachment in the neighboring valley would be expected to inhibit cytochrome c function completely as it is at the site of interaction of the redox partners (2,35). Although this may be construed as compatible with the approximately 85% lowering of electron transfer to cytochrome oxidase shown by the two 8N 3 -ATP adducts (16), it would not be compatible with the smaller 60% inhibition of the transfer from the reductase (16) and the minimal effect that derivatization with 8N 3 -ADP has on binding of cytochrome oxidase and electron transfer (17), assuming the same site is involved.…”
Section: Tnp-8n 3 -Amp-irradiationmentioning
confidence: 99%
“…ATP causes the dissociation of cytochrome c and cytochrome oxidase (14). Derivatization of cytochrome c with 8-azido-ATP inhibits both the ability of the protein to exchange electrons with its redox partners and its association with the inner mitochondrial membrane (15)(16)(17). ATP displaces cytochrome c from liposomes constituted of acidic phospholipids (18,19).…”
mentioning
confidence: 99%
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“…Accordingly, when the ATP-binding site of cyt c is occupied by a covalently bound ATP, the electron-transfer activity of cyt c with reductase and oxidase are inhibited to 41 and 11-15%, respectively, of the values measured for the native protein (3). However, the redox potential of the above modified cyt c remains close to the value of the native form (11). Several studies have indicated ATPinduced changes in the structure of cyt c. For example, autooxidation of reduced cyt c takes place upon its gel filtration in the presence of ATP (7), whereas this is not observed in the absence of the nucleotide (12).…”
mentioning
confidence: 92%
“…Studies of the effect of anions on the activity of isolated COX suggested nonspeci c ionic effects, because the interaction between cytochrome c and COX is of electrostatic nature (19,(30)(31)(32). However, speci c binding sites for ATP and ADP have been identi ed on cytochrome c, which in turn may decrease the electron transfer from cytochrome c to the oxidase (33)(34)(35).…”
Section: Interaction Of Adenylic Nucleotides On Coxmentioning
confidence: 99%