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On the binding of mammalian cytochrome c in NADH- and succinate-cytochrome c-reductase from Rhodospirillum rubrum

โœ Scribed by Boll, M.

Publisher
Springer-Verlag
Year
1969
Weight
288 KB
Volume
67
Category
Article
ISSN
0003-9276

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โœฆ Synopsis

The effect of a number of salts on the activity of the particulate NADH-cytochrome c-reductase of Rhodospirillum rubrum was investigated. The enzyme was shown to be inhibited by the presence of these salts. With monovalent anions a relationship between the size of the anion and its capacity of inhibition is observed. Di-and trivalent anions inhibit more than do monovalent anions. Di-and trivalent cations cause very strong inhibition of the enzymatic activity. With all ions a relationship of the competitive type exists between cytoehrome c and the ion tested.

Results identical to those described are obtained when the oxidation of sueeinate is measured with cytochrome c as the electron acceptor.

With these inibition experiments it was shown that a complex between mammalian cytoehrome e and the phospholipids of the electron transport particles of

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