Cooperative binding of manganese(II) to chloroplast coupling factor 1 detected by NMR proton relaxation enhancement

Alice E. Haddy, Wayne D. Frasch, Wayne Frasch

Research output: Contribution to journalArticle

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Abstract

The binding of divalent manganese to soluble latent spinach chloroplast coupling factor 1 (CF1) was examined by measurements of the water proton spin-lattice relaxation enhancement (PRE), revealing positive cooperativity between high-affinity sites. A method that used only a single enhancement parameter, εb, for the quantitation of cooperative PRE data was derived. Application to the high-affinity sites yielded a value of 9.01 ± 0.11 for εb. Two high-affinity sites participated in cooperative binding, although the possibility that a third site was present was not eliminated. The apparent binding constant to site ratio, K/n, was found to be 3.4-3.7 μM, giving a value for K of approximately 7 μM.

Original languageEnglish (US)
Pages (from-to)7926-7930
Number of pages5
JournalBiochemistry
Volume24
Issue number27
StatePublished - 1985
Externally publishedYes

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Chloroplast Proton-Translocating ATPases
Spinacia oleracea
Spin-lattice relaxation
Manganese
Protons
Nuclear magnetic resonance
Water

ASJC Scopus subject areas

  • Biochemistry

Cite this

Cooperative binding of manganese(II) to chloroplast coupling factor 1 detected by NMR proton relaxation enhancement. / Haddy, Alice E.; Frasch, Wayne D.; Frasch, Wayne.

In: Biochemistry, Vol. 24, No. 27, 1985, p. 7926-7930.

Research output: Contribution to journalArticle

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