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Reactions of nitric oxide with cytochrome c oxidase
Abstract
The reactions of nitric oxide (NO) with both oxidized and reduced cytochrome c oxidase are reported. NMR and mass spectroscopy were utilized to determine the products of the reactions; EPR and optical spectroscopy were employed to determine the states of the enzyme produced in each of these reactions. It was found that the enzyme catalyzes the consecutive oxidation and reduction of NO. A different cycle was observed when NO was added to the reduced enzyme, to the oxidized enzyme, or to the oxidized enzyme in the presence of azide. It was possible to observe the state of the enzyme at several points in each of these three cycles by varying the concentration of NO. The reactions of NO all involved a one- or two-electron redox step and could be accounted for by the involvement of only cytochrome a3 and Cua3. On the basis of these results, a mechanism for the reduction of dioxygen by the enzyme is proposed in which cytochrome a3 functions to anchor dioxygen and intermediates while remaining in the ferrous state, whereas Cua3 functions to accept electroins from cytochrome a/Cua and transfer them to dioxygen.
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Citations
Cited by
Brown, G. C., & Cooper, C. E. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)01290-3 · Cited by 1,055
Nitric oxide and mitochondrial respiration
Brown, G. C. (1999) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(99)00025-0 · Cited by 702
Regulation of mitochondrial respiration by nitric oxide inhibition of cytochrome c oxidase
Brown, G. C. (2001) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(00)00238-3 · Cited by 602
Berks, B. C., Ferguson, S. J., Moir, J. W. B., & Richardson, D. J. (1995) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(95)00092-5 · Cited by 596
Richardson, D. J. (2000) · Microbiology · doi:10.1099/00221287-146-3-551 · Cited by 544
Castello, P. R., David, P. S., McClure, T., Crook, Z., & Poyton, R. O. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.02.011 · Cited by 495
Cytochrome c oxidase dysfunction in oxidative stress
Srinivasan, S., & Avadhani, N. G. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.07.021 · Cited by 373
A Europium(III) Complex as an Efficient Singlet Oxygen Luminescence Probe
Song, B., Wang, G., Tan, M., & Yuan, J. (2006) · Journal of the American Chemical Society · doi:10.1021/ja062990f · Cited by 362
WELLBURN, A. R. (1990) · New Phytologist · doi:10.1111/j.1469-8137.1990.tb00467.x · Cited by 310
Mason, M. G., Nicholls, P., Wilson, M. T., & Cooper, C. E. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506562103 · Cited by 233
Castello, P. R., Woo, D. K., Ball, K., Wojcik, J., Liu, L., & Poyton, R. O. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709461105 · Cited by 121
Cooper, C. (2003) · IUBMB Life · doi:10.1080/15216540310001628663 · Cited by 46
Inactivation of nitric oxide by cytochrome c oxidase under steady-state oxygen conditions
Unitt, D. C., Hollis, V. S., Palacios-Callender, M., Frakich, N., & Moncada, S. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.12.002 · Cited by 21
Metadata
- Authors
- Brudvig, G. W., Stevens, T. H., & Chan, S. I.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1980-11-11
- Volume
- 19
- Issue
- 23
- Pages
- 5275-5285
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2062050293
- Cited by
- 237
- References
- 0
- FWCI
- 9.00
- Type
- journal article
- Language
- en
- Open access
- closed
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