Redox chains in chloroplast envelope membranes: Spectroscopic evidence for the presence of electron carriers, including iron–sulfur centers

AUTOR(ES)

Jäger-Vottero, Pascale

FONTE

The National Academy of Sciences of the USA

RESUMO

We have shown that envelope membranes from spinach chloroplasts contain (i) semiquinone and flavosemiquinone radicals, (ii) a series of iron-containing electron-transfer centers, and (iii) flavins (mostly FAD) loosely associated with proteins. In contrast, we were unable to detect any cytochrome in spinach chloroplast envelope membranes. In addition to a high spin [1Fe]3+ type protein associated with an EPR signal at g = 4.3, we observed two iron–sulfur centers, a [4Fe-4S]1+ and a [2Fe-2S]1+, associated with features, respectively, at g = 1.921 and g = 1.935, which were detected after reduction by NADPH and NADH, respectively. The [4Fe-4S] center, but not the [2Fe-2S] center, was also reduced by dithionite or 5-deazaflavin/oxalate. An unusual Fe-S center, named X, associated with a signal at g = 2.057, was also detected, which was reduced by dithionite but not by NADH or NADPH. Extremely fast spin–relaxation rates of flavin- and quinone-free radicals suggest their close proximity to the [4Fe-4S] cluster or the high-spin [1Fe]3+ center. Envelope membranes probably contain enzymatic activities involved in the formation and reduction of semiquinone radicals (quinol oxidase, NADPH-quinone, and NADPH-semiquinone reductases). The physiological significance of our results is discussed with respect to (i) the presence of desaturase activities in envelope membranes and (ii) the mechanisms involved in the export of protons to the cytosol, which partially regulate the stromal pH during photosynthesis. The characterization of such a wide variety of electron carriers in envelope membranes opens new fields of research on the functions of this membrane system within the plant cell.

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