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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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pubmed-52278 |
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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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US National Library of Medicine |
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PubMed Central |
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Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Correction Correction Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article |
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Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Correction Correction Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article 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/ https://ncbi.nlm.nih.gov/pubmed/1651500 https://ncbi.nlm.nih.gov/pmc/articles/PMC52279/ https://ncbi.nlm.nih.gov/pubmed/1871134 https://ncbi.nlm.nih.gov/pmc/articles/PMC52280/ https://ncbi.nlm.nih.gov/pubmed/1678520 https://ncbi.nlm.nih.gov/pmc/articles/PMC52281/ https://ncbi.nlm.nih.gov/pubmed/1871135 https://ncbi.nlm.nih.gov/pmc/articles/PMC52282/ https://ncbi.nlm.nih.gov/pubmed/1714598 https://ncbi.nlm.nih.gov/pmc/articles/PMC52283/ https://ncbi.nlm.nih.gov/pubmed/1871136 https://ncbi.nlm.nih.gov/pmc/articles/PMC52284/ https://ncbi.nlm.nih.gov/pubmed/1871137 https://ncbi.nlm.nih.gov/pmc/articles/PMC52285/ https://ncbi.nlm.nih.gov/pubmed/1871138 https://ncbi.nlm.nih.gov/pmc/articles/PMC52286/ https://ncbi.nlm.nih.gov/pubmed/1871139 https://ncbi.nlm.nih.gov/pmc/articles/PMC52287/ https://ncbi.nlm.nih.gov/pubmed/1871140 https://ncbi.nlm.nih.gov/pmc/articles/PMC52288/ https://ncbi.nlm.nih.gov/pubmed/1831270 https://ncbi.nlm.nih.gov/pmc/articles/PMC52289/ https://ncbi.nlm.nih.gov/pubmed/1651501 https://ncbi.nlm.nih.gov/pmc/articles/PMC52290/ https://ncbi.nlm.nih.gov/pubmed/1714599 https://ncbi.nlm.nih.gov/pmc/articles/PMC52291/ https://ncbi.nlm.nih.gov/pubmed/1714600 https://ncbi.nlm.nih.gov/pmc/articles/PMC52292/ https://ncbi.nlm.nih.gov/pubmed/11607208 https://ncbi.nlm.nih.gov/pmc/articles/PMC52293/ https://ncbi.nlm.nih.gov/pubmed/1651502 https://ncbi.nlm.nih.gov/pmc/articles/PMC52294/ https://ncbi.nlm.nih.gov/pubmed/1908093 https://ncbi.nlm.nih.gov/pmc/articles/PMC52295/ https://ncbi.nlm.nih.gov/pubmed/1678521 https://ncbi.nlm.nih.gov/pmc/articles/PMC52296/ https://ncbi.nlm.nih.gov/pubmed/1871141 https://ncbi.nlm.nih.gov/pmc/articles/PMC52297/ https://ncbi.nlm.nih.gov/pubmed/1678522 https://ncbi.nlm.nih.gov/pmc/articles/PMC52298/ https://ncbi.nlm.nih.gov/pubmed/1651503 https://ncbi.nlm.nih.gov/pmc/articles/PMC52299/ https://ncbi.nlm.nih.gov/pubmed/1651504 https://ncbi.nlm.nih.gov/pmc/articles/PMC52300/ https://ncbi.nlm.nih.gov/pubmed/1678523 https://ncbi.nlm.nih.gov/pmc/articles/PMC52301/ https://ncbi.nlm.nih.gov/pubmed/1831271 https://ncbi.nlm.nih.gov/pmc/articles/PMC52302/ https://ncbi.nlm.nih.gov/pubmed/1908094 https://ncbi.nlm.nih.gov/pmc/articles/PMC52303/ https://ncbi.nlm.nih.gov/pubmed/1908095 https://ncbi.nlm.nih.gov/pmc/articles/PMC52304/ https://ncbi.nlm.nih.gov/pubmed/1908096 https://ncbi.nlm.nih.gov/pmc/articles/PMC52305/ https://ncbi.nlm.nih.gov/pubmed/1714601 https://ncbi.nlm.nih.gov/pmc/articles/PMC52306/ https://ncbi.nlm.nih.gov/pubmed/1714602 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/ https://ncbi.nlm.nih.gov/pubmed/11607209 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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