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By P. K. Stumpf, B.J. Miflin

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E. Smith et al, 1976) showed that ATPdependent H2 evolution occurred without a time lag whereas C2H2 reduction and N2 fixation started after 10 and 35 min, respectively, considerably longer than the turnover time of the enzyme. The evidence suggested that a slow chemical modification of the enzyme occurred to form the active site. Similar lag phases were obtained by Thorneley and Eady (1977) working with high Kpl : Kp2 ratios at 10°C. However, it is not clear from these data whether the modification to form the active site is induced by the reducible substrate or not.

Substrate reduction kinetics with heterologous Kpl/Cp2 crosses (B. E. Smith et al, 1976) showed that ATPdependent H2 evolution occurred without a time lag whereas C2H2 reduction and N2 fixation started after 10 and 35 min, respectively, considerably longer than the turnover time of the enzyme. The evidence suggested that a slow chemical modification of the enzyme occurred to form the active site. Similar lag phases were obtained by Thorneley and Eady (1977) working with high Kpl : Kp2 ratios at 10°C.

Similar lag phases were obtained by Thorneley and Eady (1977) working with high Kpl : Kp2 ratios at 10°C. However, it is not clear from these data whether the modification to form the active site is induced by the reducible substrate or not. N2 requires six electrons to reduce to ammonia compared with only two for H2 evolution, so a more reduced form of the MoFe protein might be better able, or even necessary, to reduce N2 (Rivera-Ortiz and Burris, 1975). Such an argument has been used to explain uncoupling of ATP hydrolysis from substrate reduction at high MoFe protein : Fe protein ratios.

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