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• W1990147299 endingPage "630" @default.
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• W1990147299 abstract "1. Several low-potential electron carriers from different sources can be photoreduced by the system 3,10-dimethyl-5-deazaisoalloxazine/N-tris(hydroxymethyl)methylglycine. The carriers studied were flavodoxin, ferredoxin I and iron-sulfur protein II from Azotobacter vinelandii and the flavodoxins from Desulfovibrio vulgaris and Peptostreptococcus elsdenii. 2. Electron transport to A. vinelandii nitrogenase was studied, employing different preparations of the enzyme: a crude complex; a complex reconstituted from the 0.27 M and 0.38 M NaCl fractions after DEAE-cellulose chromatography; a complex reconstituted from the 0.27 M and 0.38 M NaCl fraction plus iron-sulfur protein II purified from the 0.15 M NaCl fraction. Of all photoreduced carriers tested, only flavodoxin hydroquinone from A. vinelandii catalyzes significant electron transport to these complexes. 3. The time course of oxidation of substrate-amounts of A. vinelandii flavodoxin hydroquinone by catalytic amounts of crude nitrogenase complex shows three characteristic phases: an initial lag phase (1), a phase with constant rate over a range of redox potentials (2) and a final phase with rapidly declining rate (3). It was shown that the Fe-S protein II is responsible for the lag phase; the potential where phase 2 changes into phase 3 is at a higher value in the presence of Fe-S protein II. Pre-reduction of the enzyme photochemically abolishes phase 1 and causes phase 2 to proceed at a higher rate. The rate in phase 2 can be enhanced also by lowering the ‘starting potential’ of the flavodoxin hydroquinone/semiquinone couple. 4. A. vinelandii flavodoxin shuttles between its hydroquinone and semiquinone forms during steady-state electron transfer. Over 90% of the reducing equivalents is recovered in ethylene formed from acetylene. The concentrations of flavodoxin hydroquinone to give half-maximum rate in the acetylene reduction assay is 3–6 μM. A scheme is proposed for the regulation of electron donation to nitrogenase." @default.
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• W1990147299 date "1977-08-01" @default.
• W1990147299 modified "2023-10-17" @default.
• W1990147299 title "Regulation of Nitrogen Fixation by Fe-S Protein II in Azotobacter vinelandii" @default.
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• W1990147299 doi "https://doi.org/10.1111/j.1432-1033.1977.tb11706.x" @default.
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