Printed in Great Britain
نویسندگان
چکیده
Stopped-flow spectrophotometry and e.p.r. spectroscopy were used to study the kinetics of reduction by dithionite of the oxidized Fe protein of nitrogenase from Klebsiella pneumoniae (Kp2.0 ) in the presence of MgADP at 230C at pH7.4. The active reductant, SO2-, produced by the predissociation of S2042= 2SO2-, reacts with Kp20. (MgADP),, with k 3.0 x 106 + 0.4 x 106 M-l' s-1. The inhibition of this reaction by the Mo-Fe protein (Kp 1) has enabled the rate of dissociation of Kp2ox (MgADP)2 from Kpl (the Kp2-binding site on Kp1) to be measured (k 3=6.4+0.8s-'). Comparison with the steady-state rate of substrate reduction shows that the dissociation (k-3) of the complex Kp20x. (MgADP)2-Kp l, which is formed after MgATP-induced electron transfer from Kp2 to Kpl, is the rate-limiting step in the catalytic cycle for substrate reduction.
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