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Conformational switching at cytochrome a during steady-state turnover of cytochrome c oxidase.

As an electron transfer-driven proton pump, cytochrome c oxidase (ferrocytochrome-c:oxygen oxidoreductase, EC 1.9.3.1) must alternate between two conformations in each valence state of the redox element associated with ion translocation. Using second derivative absorption spectroscopy, the conformat...

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Hauptverfasser: Copeland, R A, Marine, J, Winoto, A, Gros, P, Dhir, R, Croop, J, Talbot, F, Tanizawa, Y, Koranyi, L I, Welling, C M, Permutt, M A, Yamamori, T, Sioud, M, Drlica, K, Kassavetis, G A, Bartholomew, B, Blanco, J A, Johnson, T E, Geiduschek, E P, Herscovitz, H, Hadzopoulou-Cladaras, M, Walsh, M T, Cladaras, C, Zannis, V I, Small, D M, Lavelle, D, Ducksworth, J, Eves, E, Gomes, G, Keller, M, Heller, P, DeSimone, J, Fortune, N S, Geeves, M A, Ranatunga, K W, Tyson, J J, Clever, J, Yamada, M, Kasamatsu, H, Garcia-Fernàndez, J, Baguñà, J, Saló, E, Ong, B, Willcox, N, Wordsworth, P, Beeson, D, Vincent, A, Altmann, D, Lanchbury, J S, Harcourt, G C, Bell, J I, Newsom-Davis, J, Duffin, R J, Weinberger, H F, Dohmen, R J, Madura, K, Bartel, B, Varshavsky, A, Smith, M H, Cavenagh, M M, Little, J W, Visvikis, A, Thioudellet, C, Oster, T, Fournel-Gigleux, S, Wellman, M, Siest, G, Heaphy, S, Finch, J T, Gait, M J, Karn, J, Singh, M, Le Bonniec, B F, Esmon, C T, Cyert, M S, Kunisawa, R, Kaim, D, Thorner, J, Keller, G A, Warner, T G, Steimer, K S, Hallewell, R A, Choi, K, Frommel, T O, Stern, R K, Perez, C F, Kriegler, M, Tsuruo, T, Roninson, I B, Wang, J, Cao, L G, Wang, Y L, Pederson, T, Fitch, D H, Bailey, W J, Tagle, D A, Goodman, M, Sieu, L, Slightom, J L, Galili, U, Swanson, K, Higuchi, M, Kazazian, H H, Kasch, L, Warren, T C, McGinniss, M J, Phillips, J A, Kasper, C, Janco, R, Antonarakis, S E, Burkhardt, A L, Brunswick, M, Bolen, J B, Mond, J J, Dayan, C M, Londei, M, Corcoran, A E, Grubeck-Loebenstein, B, James, R F, Rapoport, B, Feldmann, M, Migliaccio, G, Migliaccio, A R, Valinsky, J, Langley, K, Zsebo, K, Visser, J W, Adamson, J W, Watts, A G, Sanchez-Watts, G, Emanuel, J R, Levenson, R, Weller, P F, Rand, T H, Goelz, S E, Chi-Rosso, G, Lobb, R R, Hamilton, A J, Bouzayen, M, Grierson, D, Sedgwick, J D, Schwender, S, Imrich, H, Dörries, R, Butcher, G W, ter Meulen, V, Spinella, M J, Malik, A B, Everitt, J, Andersen, T T, Matagne, R F, Remacle, C, Dinant, M, Bruni, R, Taeusch, H W, Waring, A J, Kalvakolanu, D V, Bandyopadhyay, S K, Harter, M L, Sen, G C, Drak, J, Iwasawa, N, Danishefsky, S, Crothers, D M, He, D C, Martin, T, Penman, S, Morton, N E, Lawrence, S, Cox, D R, Jones, J I, D'Ercole, A J, Camacho-Hubner, C, Clemmons, D R, Huang, C J, Huang, F L, Chang, G D, Chang, Y S, Lo, C F, Fraser, M J, Lo, T B, Tiberi, M, Jarvie, K R, Silvia, C, Falardeau, P, Gingrich, J A, Godinot, N, Bertrand, L, Yang-Feng, T L, Fremeau, R T, Caron, M G, Rock, C D, Zeevaart, J A, Rommens, J M, Dho, S, Bear, C E, Kartner, N, Kennedy, D, Riordan, J R, Tsui, L C, Foskett, J K, Fuernkranz, H A, Schwob, J E, Lucas, J J
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Veröffentlicht: 1991
Schlagworte:
Online Zugang:https://ncbi.nlm.nih.gov/pmc/articles/PMC52278/
https://ncbi.nlm.nih.gov/pubmed/1651500
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spelling pubmed-522782001-08-25 Conformational switching at cytochrome a during steady-state turnover of cytochrome c oxidase. Copeland, R A Proc Natl Acad Sci U S A Research Article As an electron transfer-driven proton pump, cytochrome c oxidase (ferrocytochrome-c:oxygen oxidoreductase, EC 1.9.3.1) must alternate between two conformations in each valence state of the redox element associated with ion translocation. Using second derivative absorption spectroscopy, the conformation of the cytochrome a cofactor has been investigated during steady-state turnover of this enzyme. Resting cytochrome c oxidase displays a transition for ferric cytochrome a at 430 nm. During aerobic steady-state turnover, this band is replaced by a ferrous cytochrome a transition at 450 nm. When anaerobicity is achieved, the transition occurs at 444 nm. The 450-nm-absorbing species is thus the dominant form during turnover, suggesting that conformational transitions of cytochrome a direct electron transfer during catalysis and may direct as well proton translocation in the last step of the respiratory electron transfer chain. 1991-08-15 /pmc/articles/PMC52278/ /pubmed/1651500 Text en
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Copeland, R A
Marine, J
Winoto, A
Gros, P
Dhir, R
Croop, J
Talbot, F
Tanizawa, Y
Koranyi, L I
Welling, C M
Permutt, M A
Yamamori, T
Sioud, M
Drlica, K
Kassavetis, G A
Bartholomew, B
Blanco, J A
Johnson, T E
Geiduschek, E P
Herscovitz, H
Hadzopoulou-Cladaras, M
Walsh, M T
Cladaras, C
Zannis, V I
Small, D M
Lavelle, D
Ducksworth, J
Eves, E
Gomes, G
Keller, M
Heller, P
DeSimone, J
Fortune, N S
Geeves, M A
Ranatunga, K W
Tyson, J J
Clever, J
Yamada, M
Kasamatsu, H
Garcia-Fernàndez, J
Baguñà, J
Saló, E
Ong, B
Willcox, N
Wordsworth, P
Beeson, D
Vincent, A
Altmann, D
Lanchbury, J S
Harcourt, G C
Bell, J I
Newsom-Davis, J
Duffin, R J
Weinberger, H F
Dohmen, R J
Madura, K
Bartel, B
Varshavsky, A
Smith, M H
Cavenagh, M M
Little, J W
Visvikis, A
Thioudellet, C
Oster, T
Fournel-Gigleux, S
Wellman, M
Siest, G
Heaphy, S
Finch, J T
Gait, M J
Karn, J
Singh, M
Le Bonniec, B F
Esmon, C T
Cyert, M S
Kunisawa, R
Kaim, D
Thorner, J
Keller, G A
Warner, T G
Steimer, K S
Hallewell, R A
Choi, K
Frommel, T O
Stern, R K
Perez, C F
Kriegler, M
Tsuruo, T
Roninson, I B
Wang, J
Cao, L G
Wang, Y L
Pederson, T
Fitch, D H
Bailey, W J
Tagle, D A
Goodman, M
Sieu, L
Slightom, J L
Galili, U
Swanson, K
Higuchi, M
Kazazian, H H
Kasch, L
Warren, T C
McGinniss, M J
Phillips, J A
Kasper, C
Janco, R
Antonarakis, S E
Burkhardt, A L
Brunswick, M
Bolen, J B
Mond, J J
Dayan, C M
Londei, M
Corcoran, A E
Grubeck-Loebenstein, B
James, R F
Rapoport, B
Feldmann, M
Migliaccio, G
Migliaccio, A R
Valinsky, J
Langley, K
Zsebo, K
Visser, J W
Adamson, J W
Watts, A G
Sanchez-Watts, G
Emanuel, J R
Levenson, R
Weller, P F
Rand, T H
Goelz, S E
Chi-Rosso, G
Lobb, R R
Hamilton, A J
Bouzayen, M
Grierson, D
Sedgwick, J D
Schwender, S
Imrich, H
Dörries, R
Butcher, G W
ter Meulen, V
Spinella, M J
Malik, A B
Everitt, J
Andersen, T T
Matagne, R F
Remacle, C
Dinant, M
Bruni, R
Taeusch, H W
Waring, A J
Kalvakolanu, D V
Bandyopadhyay, S K
Harter, M L
Sen, G C
Drak, J
Iwasawa, N
Danishefsky, S
Crothers, D M
He, D C
Martin, T
Penman, S
Morton, N E
Lawrence, S
Morton, N E
Cox, D R
Jones, J I
D'Ercole, A J
Camacho-Hubner, C
Clemmons, D R
Huang, C J
Huang, F L
Chang, G D
Chang, Y S
Lo, C F
Fraser, M J
Lo, T B
Tiberi, M
Jarvie, K R
Silvia, C
Falardeau, P
Gingrich, J A
Godinot, N
Bertrand, L
Yang-Feng, T L
Fremeau, R T
Caron, M G
Rock, C D
Zeevaart, J A
Rommens, J M
Dho, S
Bear, C E
Kartner, N
Kennedy, D
Riordan, J R
Tsui, L C
Foskett, J K
Fuernkranz, H A
Schwob, J E
Lucas, J J
Conformational switching at cytochrome a during steady-state turnover of cytochrome c oxidase.
description As an electron transfer-driven proton pump, cytochrome c oxidase (ferrocytochrome-c:oxygen oxidoreductase, EC 1.9.3.1) must alternate between two conformations in each valence state of the redox element associated with ion translocation. Using second derivative absorption spectroscopy, the conformation of the cytochrome a cofactor has been investigated during steady-state turnover of this enzyme. Resting cytochrome c oxidase displays a transition for ferric cytochrome a at 430 nm. During aerobic steady-state turnover, this band is replaced by a ferrous cytochrome a transition at 450 nm. When anaerobicity is achieved, the transition occurs at 444 nm. The 450-nm-absorbing species is thus the dominant form during turnover, suggesting that conformational transitions of cytochrome a direct electron transfer during catalysis and may direct as well proton translocation in the last step of the respiratory electron transfer chain.
author Copeland, R A
Marine, J
Winoto, A
Gros, P
Dhir, R
Croop, J
Talbot, F
Tanizawa, Y
Koranyi, L I
Welling, C M
Permutt, M A
Yamamori, T
Sioud, M
Drlica, K
Kassavetis, G A
Bartholomew, B
Blanco, J A
Johnson, T E
Geiduschek, E P
Herscovitz, H
Hadzopoulou-Cladaras, M
Walsh, M T
Cladaras, C
Zannis, V I
Small, D M
Lavelle, D
Ducksworth, J
Eves, E
Gomes, G
Keller, M
Heller, P
DeSimone, J
Fortune, N S
Geeves, M A
Ranatunga, K W
Tyson, J J
Clever, J
Yamada, M
Kasamatsu, H
Garcia-Fernàndez, J
Baguñà, J
Saló, E
Ong, B
Willcox, N
Wordsworth, P
Beeson, D
Vincent, A
Altmann, D
Lanchbury, J S
Harcourt, G C
Bell, J I
Newsom-Davis, J
Duffin, R J
Weinberger, H F
Dohmen, R J
Madura, K
Bartel, B
Varshavsky, A
Smith, M H
Cavenagh, M M
Little, J W
Visvikis, A
Thioudellet, C
Oster, T
Fournel-Gigleux, S
Wellman, M
Siest, G
Heaphy, S
Finch, J T
Gait, M J
Karn, J
Singh, M
Le Bonniec, B F
Esmon, C T
Cyert, M S
Kunisawa, R
Kaim, D
Thorner, J
Keller, G A
Warner, T G
Steimer, K S
Hallewell, R A
Choi, K
Frommel, T O
Stern, R K
Perez, C F
Kriegler, M
Tsuruo, T
Roninson, I B
Wang, J
Cao, L G
Wang, Y L
Pederson, T
Fitch, D H
Bailey, W J
Tagle, D A
Goodman, M
Sieu, L
Slightom, J L
Galili, U
Swanson, K
Higuchi, M
Kazazian, H H
Kasch, L
Warren, T C
McGinniss, M J
Phillips, J A
Kasper, C
Janco, R
Antonarakis, S E
Burkhardt, A L
Brunswick, M
Bolen, J B
Mond, J J
Dayan, C M
Londei, M
Corcoran, A E
Grubeck-Loebenstein, B
James, R F
Rapoport, B
Feldmann, M
Migliaccio, G
Migliaccio, A R
Valinsky, J
Langley, K
Zsebo, K
Visser, J W
Adamson, J W
Watts, A G
Sanchez-Watts, G
Emanuel, J R
Levenson, R
Weller, P F
Rand, T H
Goelz, S E
Chi-Rosso, G
Lobb, R R
Hamilton, A J
Bouzayen, M
Grierson, D
Sedgwick, J D
Schwender, S
Imrich, H
Dörries, R
Butcher, G W
ter Meulen, V
Spinella, M J
Malik, A B
Everitt, J
Andersen, T T
Matagne, R F
Remacle, C
Dinant, M
Bruni, R
Taeusch, H W
Waring, A J
Kalvakolanu, D V
Bandyopadhyay, S K
Harter, M L
Sen, G C
Drak, J
Iwasawa, N
Danishefsky, S
Crothers, D M
He, D C
Martin, T
Penman, S
Morton, N E
Lawrence, S
Morton, N E
Cox, D R
Jones, J I
D'Ercole, A J
Camacho-Hubner, C
Clemmons, D R
Huang, C J
Huang, F L
Chang, G D
Chang, Y S
Lo, C F
Fraser, M J
Lo, T B
Tiberi, M
Jarvie, K R
Silvia, C
Falardeau, P
Gingrich, J A
Godinot, N
Bertrand, L
Yang-Feng, T L
Fremeau, R T
Caron, M G
Rock, C D
Zeevaart, J A
Rommens, J M
Dho, S
Bear, C E
Kartner, N
Kennedy, D
Riordan, J R
Tsui, L C
Foskett, J K
Fuernkranz, H A
Schwob, J E
Lucas, J J
author_facet Copeland, R A
Marine, J
Winoto, A
Gros, P
Dhir, R
Croop, J
Talbot, F
Tanizawa, Y
Koranyi, L I
Welling, C M
Permutt, M A
Yamamori, T
Sioud, M
Drlica, K
Kassavetis, G A
Bartholomew, B
Blanco, J A
Johnson, T E
Geiduschek, E P
Herscovitz, H
Hadzopoulou-Cladaras, M
Walsh, M T
Cladaras, C
Zannis, V I
Small, D M
Lavelle, D
Ducksworth, J
Eves, E
Gomes, G
Keller, M
Heller, P
DeSimone, J
Fortune, N S
Geeves, M A
Ranatunga, K W
Tyson, J J
Clever, J
Yamada, M
Kasamatsu, H
Garcia-Fernàndez, J
Baguñà, J
Saló, E
Ong, B
Willcox, N
Wordsworth, P
Beeson, D
Vincent, A
Altmann, D
Lanchbury, J S
Harcourt, G C
Bell, J I
Newsom-Davis, J
Duffin, R J
Weinberger, H F
Dohmen, R J
Madura, K
Bartel, B
Varshavsky, A
Smith, M H
Cavenagh, M M
Little, J W
Visvikis, A
Thioudellet, C
Oster, T
Fournel-Gigleux, S
Wellman, M
Siest, G
Heaphy, S
Finch, J T
Gait, M J
Karn, J
Singh, M
Le Bonniec, B F
Esmon, C T
Cyert, M S
Kunisawa, R
Kaim, D
Thorner, J
Keller, G A
Warner, T G
Steimer, K S
Hallewell, R A
Choi, K
Frommel, T O
Stern, R K
Perez, C F
Kriegler, M
Tsuruo, T
Roninson, I B
Wang, J
Cao, L G
Wang, Y L
Pederson, T
Fitch, D H
Bailey, W J
Tagle, D A
Goodman, M
Sieu, L
Slightom, J L
Galili, U
Swanson, K
Higuchi, M
Kazazian, H H
Kasch, L
Warren, T C
McGinniss, M J
Phillips, J A
Kasper, C
Janco, R
Antonarakis, S E
Burkhardt, A L
Brunswick, M
Bolen, J B
Mond, J J
Dayan, C M
Londei, M
Corcoran, A E
Grubeck-Loebenstein, B
James, R F
Rapoport, B
Feldmann, M
Migliaccio, G
Migliaccio, A R
Valinsky, J
Langley, K
Zsebo, K
Visser, J W
Adamson, J W
Watts, A G
Sanchez-Watts, G
Emanuel, J R
Levenson, R
Weller, P F
Rand, T H
Goelz, S E
Chi-Rosso, G
Lobb, R R
Hamilton, A J
Bouzayen, M
Grierson, D
Sedgwick, J D
Schwender, S
Imrich, H
Dörries, R
Butcher, G W
ter Meulen, V
Spinella, M J
Malik, A B
Everitt, J
Andersen, T T
Matagne, R F
Remacle, C
Dinant, M
Bruni, R
Taeusch, H W
Waring, A J
Kalvakolanu, D V
Bandyopadhyay, S K
Harter, M L
Sen, G C
Drak, J
Iwasawa, N
Danishefsky, S
Crothers, D M
He, D C
Martin, T
Penman, S
Morton, N E
Lawrence, S
Morton, N E
Cox, D R
Jones, J I
D'Ercole, A J
Camacho-Hubner, C
Clemmons, D R
Huang, C J
Huang, F L
Chang, G D
Chang, Y S
Lo, C F
Fraser, M J
Lo, T B
Tiberi, M
Jarvie, K R
Silvia, C
Falardeau, P
Gingrich, J A
Godinot, N
Bertrand, L
Yang-Feng, T L
Fremeau, R T
Caron, M G
Rock, C D
Zeevaart, J A
Rommens, J M
Dho, S
Bear, C E
Kartner, N
Kennedy, D
Riordan, J R
Tsui, L C
Foskett, J K
Fuernkranz, H A
Schwob, J E
Lucas, J J
author_sort Copeland, R A
title Conformational switching at cytochrome a during steady-state turnover of cytochrome c oxidase.
title_short Conformational switching at cytochrome a during steady-state turnover of cytochrome c oxidase.
title_full Conformational switching at cytochrome a during steady-state turnover of cytochrome c oxidase.
title_fullStr Conformational switching at cytochrome a during steady-state turnover of cytochrome c oxidase.
title_full_unstemmed Conformational switching at cytochrome a during steady-state turnover of cytochrome c oxidase.
title_sort conformational switching at cytochrome a during steady-state turnover of cytochrome c oxidase.
publishDate 1991
url https://ncbi.nlm.nih.gov/pmc/articles/PMC52278/
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https://ncbi.nlm.nih.gov/pmc/articles/PMC52304/
https://ncbi.nlm.nih.gov/pubmed/1908096
https://ncbi.nlm.nih.gov/pmc/articles/PMC52305/
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https://ncbi.nlm.nih.gov/pmc/articles/PMC52306/
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https://ncbi.nlm.nih.gov/pmc/articles/PMC52307/
https://ncbi.nlm.nih.gov/pubmed/1714603
https://ncbi.nlm.nih.gov/pmc/articles/PMC52308/
https://ncbi.nlm.nih.gov/pubmed/1651505
https://ncbi.nlm.nih.gov/pmc/articles/PMC52309/
https://ncbi.nlm.nih.gov/pubmed/1714604
https://ncbi.nlm.nih.gov/pmc/articles/PMC52310/
https://ncbi.nlm.nih.gov/pubmed/1714605
https://ncbi.nlm.nih.gov/pmc/articles/PMC52311/
https://ncbi.nlm.nih.gov/pubmed/1651506
https://ncbi.nlm.nih.gov/pmc/articles/PMC52312/
https://ncbi.nlm.nih.gov/pubmed/1871142
https://ncbi.nlm.nih.gov/pmc/articles/PMC52313/
https://ncbi.nlm.nih.gov/pubmed/1871143
https://ncbi.nlm.nih.gov/pmc/articles/PMC52314/
https://ncbi.nlm.nih.gov/pubmed/1871144
https://ncbi.nlm.nih.gov/pmc/articles/PMC52315/
https://ncbi.nlm.nih.gov/pubmed/1871145
https://ncbi.nlm.nih.gov/pmc/articles/PMC52318/
https://ncbi.nlm.nih.gov/pmc/articles/PMC52319/
https://ncbi.nlm.nih.gov/pubmed/1652751
https://ncbi.nlm.nih.gov/pmc/articles/PMC52320/
https://ncbi.nlm.nih.gov/pubmed/1881884
https://ncbi.nlm.nih.gov/pmc/articles/PMC52321/
https://ncbi.nlm.nih.gov/pubmed/1881885
https://ncbi.nlm.nih.gov/pmc/articles/PMC52322/
https://ncbi.nlm.nih.gov/pubmed/1881886
https://ncbi.nlm.nih.gov/pmc/articles/PMC52323/
https://ncbi.nlm.nih.gov/pubmed/1881887
https://ncbi.nlm.nih.gov/pmc/articles/PMC52324/
https://ncbi.nlm.nih.gov/pubmed/1715565
https://ncbi.nlm.nih.gov/pmc/articles/PMC52325/
https://ncbi.nlm.nih.gov/pubmed/1715566
https://ncbi.nlm.nih.gov/pmc/articles/PMC52326/
https://ncbi.nlm.nih.gov/pubmed/1831904
https://ncbi.nlm.nih.gov/pmc/articles/PMC52327/
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https://ncbi.nlm.nih.gov/pmc/articles/PMC52328/
https://ncbi.nlm.nih.gov/pubmed/1715567
https://ncbi.nlm.nih.gov/pmc/articles/PMC52329/
https://ncbi.nlm.nih.gov/pubmed/1881888
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