Nitrogenase redox potentials

The so-called midpoint potential, Em, of protein-bound [Fe-S] clusters controls both the kinetics and thermodynamics of their reactions. Em may depend on the protein chain s polarity in the vicinity of the metal-sulfur cluster and also upon the bulk solvent accessibility at the site. It is known that nucleotide binding to nitrogenase s Fe-protein, for instance, results in a lowering of the redox potential of its [4Fe-4S] cluster by over 100 mV. This is thought to be essential for electron transfer to MoFe-protein for substrate reduction.11 3... 

Biological N2 fixation (1), i.e., the reduction of N2 to NH3 catalyzed by FeMo, FeV, or FeFe nitrogenases, is one of the fundamental synthetic processes of nature (2-4). In spite of intense efforts over the last decades, its molecular mechanism is poorly understood, in particular because the pivotal chemical question has remained unanswered how do nitrogenases achieve to activate and convert the inert N2 molecule to ammonia under ambient conditions and mild redox potentials. 

Biological N2 fixation is catalyzed by Fe/Mo, Fe/V, or FeFe (the Fe-only) nitrogenases (150, 151). The extremely different reaction conditions of the biological and the Haber-Bosch processes of N2 reduction, that is, standard temperature and pressure and biological redox potentials on the one hand, red-hot temperatures and high pressures on the other hand, make the quest for low molecular weight competitive catalysts particularly challenging. 

According to recent data, the property of dithionite as an electron donor for nitrogenase is different from that of the natural donor flavodoxin (Burgess and Lowe, 1996). Flavodoxin from Azotobacter vinelandii has the redox potential equal to -0.515 V for the reversible transition between the semiquinone and hydroquinone forms of flavodoxin. Unlike dithionite, flavodoxin can reversibly reduce the [Fe4S4]+l cluster Av2 by one electron to the [Fe4S4]° state in which all iron ions exist in the ferrous form. It is assumed that, under natural conditions, two electrons can transfer from Av2 to Avl. Flavodoxin reduces both Av2 bound to Avl and free Av2 in a solution. The apparent rate constants of these reactions are 400 s 1 and > 1000 s"1, respectively (Duyvis et al. 1998). 

Figure 3.7. The energy profile of a nitrogenase reaction. Eo is the standard redox potential of the reactants, intermediates and products of the reaction Fd = ferredoxin FeP = Fe protein FeMo = FeMo protein. The arrow indicates the increase of the reduction potential upon ATP hydrolysis (Likhtenshtein 1988a). Reproduced with permission.

The actual activity of other nitrogenase (purported) models towards both uptake and reduction of gaseous depends on the redox potentials of Mo... 

The standard redox potential of the Fe-protein is low, and it becomes even lower when it interacts with MgATP. A specific low-potential electron donor channels electrons from the cell s general metabolism to nitrogenase. In the anaerobe Clostridium pasteurianum it was known to be a ferredoxin the UNF s particular contribution in this area was to show, in parallel with workers in the Netherlands, that the equivalent electron donor in A. chroococcum was a flavodoxin, shuttling between its reduced and semi-quinone forms. 

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