. Biological structure and function; proceedings. Biochemistry; Cytology. 432 HERRICK BALTSCHEFFSKY further to a compound X, which represents the site of action for HOQNO [8] and antimycin A [9], and then to the photochemical oxidant. This is a minimum scheme, based on our own results, and there probably exist more electron carriers in the chain. For example, the participation of cytochromes was indicated in earlier work by Smith and M. Baltscheffsky [10]. In what may be called "the PMS-pathway" added PMS, serving as a link between the flavoprotein and the oxidant, gives a new, "
. Biological structure and function; proceedings. Biochemistry; Cytology. 432 HERRICK BALTSCHEFFSKY further to a compound X, which represents the site of action for HOQNO [8] and antimycin A [9], and then to the photochemical oxidant. This is a minimum scheme, based on our own results, and there probably exist more electron carriers in the chain. For example, the participation of cytochromes was indicated in earlier work by Smith and M. Baltscheffsky [10]. In what may be called "the PMS-pathway" added PMS, serving as a link between the flavoprotein and the oxidant, gives a new, "artificial" Light . ' 1 reductant »- flavoprotein >- X >â oxidant atebnn \ HOQNO antimycin A PMS Fig. I. Electron transport in LIP chromatophores of R. riibrum. electron transport chain. When this pathway is used, the transport of electrons from the reductant to the oxidant along "the physiological pathway" can be ehminated by inhibition at X with HOQNO or antimycin A [9, 11]. Light [ reductant. 1 FMN, FAD menadione PMS, pyocyanine Fig. 2. Electron transport in LIP in spinach chloroplasts. In green plants, the ATP-formation which is linked to cyclic electron transport is almost totally dependent upon the addition of an electron carrier. Our tentative view about the electron transport in isolated spinach chloroplasts is given in Fig. 2. A great similarity is seen between this scheme and that proposed earlier by Jagendorf [12]. The main difference is that flavoprotein has been included as an obligatory member in the physiological electron transport chain. The experimental background for this scheme has been presented earlier [5]. In recent experiments aiming at an estimation of the efficiency of light- induced phosphorylation in vitro we have used three different approaches. Please note that these images are extracted from scanned page images that may have been digitally enhanced for readability - coloration and appearance of these illustrations may not
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