Abstract:
:Nitrogenase is a two-component metalloenzyme that catalyzes a MgATP hydrolysis driven reduction of substrates. Aluminum fluoride plus MgADP inhibits nitrogenase by stabilizing an intermediate of the on-enzyme MgATP hydrolysis reaction. We report here the redox properties and electron paramagnetic resonance (EPR) signals of the aluminum fluoride-MgADP stabilized nitrogenase complex of Azotobacter vinelandii. Complex formation lowers the midpoint potential of the [4Fe-4S] cluster in the Fe protein. Also, the two-electron reaction of the unique [8Fe-7S] cluster in the MoFe protein is split in two one-electron reactions both with lower midpoint potentials. Furthermore, a change in spin-state of the two-electron oxidized [8Fe-7S] cluster is observed. The implications of these findings for the mechanism of MgATP hydrolysis driven electron transport within the nitrogenase protein complex are discussed.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Spee JH,Arendsen AF,Wassink H,Marritt SJ,Hagen WR,Haaker Hdoi
10.1016/s0014-5793(98)00827-8subject
Has Abstractpub_date
1998-07-31 00:00:00pages
55-8issue
1-2eissn
0014-5793issn
1873-3468pii
S0014-5793(98)00827-8journal_volume
432pub_type
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