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Binding of arylazidocytochrome c derivatives to beef heart cytochrome c oxidase: cross-linking in the high- and low-affinity binding sites.
Bisson R, Jacobs B, Capaldi RA. Bisson R, et al. Biochemistry. 1980 Sep 2;19(18):4173-8. doi: 10.1021/bi00559a006. Biochemistry. 1980. PMID: 6251864
Cross-linking to protein was through subunit II of the cytochrome c oxidase complex, as first reported by Bisson et al. [Bisson, R., Azzi, A., Gutweniger, H., Colonna, R., Monteccuco, C., & Zanotti, A. (1978) J. ...
Cross-linking to protein was through subunit II of the cytochrome c oxidase complex, as first reported by Bisson et al. [Bisson
Structure of cytochrome c oxidase.
Capaldi RA, Prochaska L, Bisson R. Capaldi RA, et al. Among authors: bisson r. Adv Exp Med Biol. 1980;132:197-210. doi: 10.1007/978-1-4757-1419-7_21. Adv Exp Med Biol. 1980. PMID: 6252766 No abstract available.
Localization of lipid binding domain(s) on subunit II of beef heart cytochrome c oxidase.
Bisson R, Steffens GC, Buse G. Bisson R, et al. J Biol Chem. 1982 Jun 25;257(12):6716-20. J Biol Chem. 1982. PMID: 6282822 Free article.
Photoactivatable arylazido phospholipids (Bisson, R., and Montecucco, C. (1981) Biochem. J. 193, 757-763) have been used to study the arrangement in the membrane of beef heart cytochrome c oxidase subunit II. ...
Photoactivatable arylazido phospholipids (Bisson, R., and Montecucco, C. (1981) Biochem. J. 193, 757-763) have been used to st …
83 results