The electron transport to nitrogenase in Mycobacterium flavum
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Two ferredoxin-type iron-sulfur proteins have been isolated from Mycobacterium flavum 301 grown under nitrogen-fixing, iron-sufficient conditions. No flavodoxin was observed.
These ferredoxins are apparently soluble: they were present in the supernatant fraction after disrupting by decompression. Only small amounts were present in particulate fractions.
The two ferredoxins were separated by chromatography on DEAE-cellulose, Sephadex or electrophoresis.
Both ferredoxins mediated the transfer of electrons from illuminated spinach chloroplasts to a nitrogenase preparation to reduce acetylene. Ferredoxin II was specifically about five times more active than ferredoxin I. Ferredoxin II was also active in the photosynthetic NADP+-reduction whereas ferredoxin I was not.
Both ferredoxins were reversibly reduced by either sodium dithionite, illuminated spinach chloroplasts or hydrogen plus hydrogenase from Clostridium pasteurianum.
Attempts to determine the primary electron donor for nitrogen fixation in Mycobacterium flavum were unsuccessful. Acetylene reduction in Mycobacterium extracts was obtained only with sodium dithionite or illuminated spinach chloroplasts as electron donors. The reduction of the electron carrier (e. g. ferredoxin) rather than the transfer of electrons from the reduced carrier to nitrogenase was rate-limiting.
Key wordsFerredoxin Iron-sulfur proteins Nitrogen fixation Electron transport to nitrogenase Flavodoxin Mycobacterium flavum
acid labile sulfur
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