Current Research in Photosynthesis pp 2193-2196 | Cite as
Operation of UQH2: CYT C2 Oxidoreductase of R. sphaeroides in the Steady State
Abstract
Measurement of the thermodynamic poise of redox components of electron transfer chains under coupled conditions has been used extensively in the mitochondrial field to analyze through “cross-over points” the contributions to different spans to the work required to drive ATP synthesis, or maintain the proton gradient. In the work described in this paper, a steady state approach has been developed by which the redox poise of the electron transfer chain, the electron flux and H+-gradient could be simultaneously monitored, and the approach to the coupled steady-state (static head) could be followed kinetically on illumination of chromatophores from Rhodobacter sphaeroides.
Keywords
Electron Flux Proton Gradient Rhodobacter Sphaeroides Redox Center Electron Transfer ChainPreview
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References
- 1.Crofts, A. R., Meinhardt, S. W., Jones, K. R. and Snozzi, M.(1983) Biochim. Biophys. Acta, 723, 202–218.PubMedCrossRefGoogle Scholar
- 2.Meinhardt, S.W. and Crofts, A.R. (1982). FEBS Lett., 149, 223–227.CrossRefGoogle Scholar
- 3.Meinhardt, S.W. and Crofts, A.R. (1983). Biochim. Biophys. Acta, 723, 219–230.CrossRefGoogle Scholar
- 4.Venturoli, G., Virgili, M., Melandri, B.A. and Crofts, A.R. (1986) FEBS Lett. 219, 477–484.CrossRefGoogle Scholar
- 5.Cotton, N.P.J., Clark, A.J. and Jackson, J.B. (Eur. J. Biochem. 142, 193–198Google Scholar
- 6.Dutton, P.L., Petty, K.M., Bonner, H.S. and Morse, S.D. (1975) Biochim. Biophys. Acta 387, 536–556.PubMedCrossRefGoogle Scholar