Amino Acids and Derivatives. A Comprehensive Treatise by P. K. Stumpf, B.J. Miflin

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

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Such investigations have not yet been attempted. These considerations, however, do not explain why nitrogenase evolves H2 in the absence of added reducible substrate. III. PHYSIOLOGICAL ASPECTS OF NITROGEN FIXATION The more physiological aspects of nitrogen fixation include electron trans­ port to nitrogenase in vivo, mechanisms to protect the Fe protein of nitro­ genase from damage by oxygen in aerobes, the role of ancillary proteins such as hydrogenase in aerobes and leghemoglobin in bacteroids and means of regulating nitrogenase activity in vivo.

1977) which are diamagnetic when reduced and paramagnetic when oxidized (Fig. 7b) and they operate between the - 2 and - 1 oxidation states. One ferredoxin from each of these bacteria possesses two 4Fe4S clusters with redox potentials almost 700 mV apart. Howard et al. (1976), in an uncompleted analysis of the amino acid sequence of A. vinelandii ferredoxin I, found that seven of the cysteine residues corre­ sponded to those in other ferredoxins but that cys-24 did not. This indicated 41 1. Biochemistry of Nitrogen Fixation a major change in the environment of one of the 4Fe4S clusters in A.

There is also uncertainty about the site of inhibition by MgADP. Some evidence suggests that it may be associated with the MoFe 1. Biochemistry of Nitrogen Fixation 35 protein (B. E. Smith et al, 1976, 1977; Rennie et al, 1978) but it is equally plausible that the rate of dissociation from the oxidized Fe protein is the rate-limiting step in nitrogenase turnover and consequently the site of MgADP inhibition. Finally, perhaps the least understood phenomenon about nitrogenase ac­ tivity is why the enzyme evolves H2.

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