1987
DOI: 10.1016/0005-2728(87)90164-2
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The distance between cytochromes a and a3 in the azide compound of bovine-heart cytochrome oxidase

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Cited by 14 publications
(6 citation statements)
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“…Thus, the high that we observe may be related to changes in solvation or other structural changes at cytochrome 3-• According to Moser et al (1992), ß in eq 4 should be 1.4 Á-1, but the use of this value with our data gives too short a distance between the two cytochromes in the bacterial oxidase (Table 2). EPR measurements (Ohnishi et al, 1982;Brudvig et al, 1984;Goodman & Leigh, 1987) have put the distance between 12 and 20 Á, and the shorter of these values agrees with a current stmctural model (Hosier et al, 1993) . Earlier, Woodruff (1993), using ß -1.4 Á-1, had found a good agreement between the distance in the model and our measured rate with the bovine enzyme (Oliveberg & Malmstrom, 1991), but his calculation assumed that the reaction is activationless, whereas we find a substantial temperature dependence of this electron transfer (Figure 3).…”
Section: Discussionsupporting
confidence: 79%
“…Thus, the high that we observe may be related to changes in solvation or other structural changes at cytochrome 3-• According to Moser et al (1992), ß in eq 4 should be 1.4 Á-1, but the use of this value with our data gives too short a distance between the two cytochromes in the bacterial oxidase (Table 2). EPR measurements (Ohnishi et al, 1982;Brudvig et al, 1984;Goodman & Leigh, 1987) have put the distance between 12 and 20 Á, and the shorter of these values agrees with a current stmctural model (Hosier et al, 1993) . Earlier, Woodruff (1993), using ß -1.4 Á-1, had found a good agreement between the distance in the model and our measured rate with the bovine enzyme (Oliveberg & Malmstrom, 1991), but his calculation assumed that the reaction is activationless, whereas we find a substantial temperature dependence of this electron transfer (Figure 3).…”
Section: Discussionsupporting
confidence: 79%
“…CuA, which are about 20 Á away from the oxygen binding site (Goodman & Leigh, 1987;Brudvig et al, 1984). Although the mechanism of this communication is unknown, it is most likely mediated by an enzyme conformational change.…”
Section: Discussionmentioning
confidence: 85%
“…This is associated with reduction of either cytochrome LZ or Cu,, and linked to the corresponding changes in cytochrome a in the presence of ligands such as azide [16,27]. Both cytochrome u and Cu, are therefore simple electron transfer centres.…”
Section: Discussionmentioning
confidence: 99%