Abstract:
:The alternative nitrogenase of Rhodobacter capsulatus, isolated from a nifHDK deletion mutant, has been purified to near homogeneity and identified as an 'iron only' nitrogenase. The dithionite-reduced component 1 ('FeFe protein') of this enzyme showed an EPR spectrum consisting of two components: a minor S = 1/2 signal at g = 1.93 and a very characteristic S = 3/2 signal of near-stoichiometric intensity at g = 5.44. This resonance is very close to the highest possible g value (g = 5.46) for the coinciding two intradoublet subspectra of an S = 3/2 system of maximal rhombicity (E/D = 0.33). The deviation from axial symmetry (increasing E/D) correlates with the stability, activity and substrate selectivity of the different (Mo, V, Fe) nitrogenases.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Müller A,Schneider K,Knüttel K,Hagen WRdoi
10.1016/0014-5793(92)80472-skeywords:
subject
Has Abstractpub_date
1992-05-25 00:00:00pages
36-40issue
1eissn
0014-5793issn
1873-3468journal_volume
303pub_type
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