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Biomembranes Part N: Transport in Bacteria, Mitochondria, by Nathan P. Colowick, Nathan P. Kaplan, Sidney Fleischer,

By Nathan P. Colowick, Nathan P. Kaplan, Sidney Fleischer, Becca Fleischer

The severely acclaimed laboratory common, Methods in Enzymology, is among the so much hugely revered guides within the box of biochemistry. due to the fact that 1955, each one quantity has been eagerly awaited, often consulted, and praised by way of researchers and reviewers alike. The sequence includes a lot fabric nonetheless proper this present day - really a vital booklet for researchers in all fields of existence sciences

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Additional info for Biomembranes Part N: Transport in Bacteria, Mitochondria, and Chloroplasts: Protonmotive Force

Sample text

Margoliash, this series, Vol. 53 [18]. 4o U. Bilge, Dissertation, Fachbereich Chemie, Philipps-Universit~t, Marburg 0985). m = 12 m M i cm-~ [G. von Jagow and M. Klingenberg, FEBS Lett. 24, 278 (1972)]. Protein was determined by the L o w r y m e t h o d . 38 b T h e activity was calculated as turnover n u m b e r (mol c y t o c h r o m e c/sec × tool cytoc h r o m e aa3). 25 m M laurylmaltoside, 40/xM reduced c y t o c h r o m e c, and 2 n M c y t o c h r o m e - c oxidase. 7 m M T M P D , 1 m M laurylmaltoside, 20 n M c y t o c h r o m e - c oxidase, and was calculated for infinite c y t o c h r o m e c concentration.

E. Jacobs, Biochim. Biophys. Acta 153, 804 (1968). l0 E. E. Jacobs, E. C. Andrews, W. Cunningham, and F. L. Crane, Biochem. Biophys. Res. Commun. 25, 87 (1966). METHODS IN ENZYMOLOGY, VOL. 126 Copyright © 1986 by Academic Press, Inc. All rights of reproduction in any form reserved. [3] S T R U C T U R E OF CYTOCHROME-C O X I D A S E 23 dimensional crystals follows closely the isolation procedure described by Sun et al. 8. 2 M and the solution allowed to incubate on ice. The pellet, recovered by centrifugation at 78,000 g for 20 min, is resolubilized in Triton X-100 (1 mg/mg protein) in the same buffer.

144, 359 (1982). 13] STRUCTURE OF CYTOCHROME-C OXIDASE 31 FIG. 4. Schematic depiction of the high-affinity binding site for cytochrome c in the cytochrome-c oxidase dimer based on cross-linking studies. the low-resolution structure is between monomers in the cytochrome-c oxidase dimer 12,13 (Fig. 4). Conclusions and Prospects This brief review shows a picture of mammalian cytochrome-c oxidase built up by combining the data of biochemical studies with a low-resolution structure provided by electron microscopy and image reconstruction.

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