EPR spectroscopic characterization of an 'iron only' nitrogenase. S = 3/2 spectrum of component 1 isolated from Rhodobacter capsulatus.

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 Lett

journal_title

FEBS letters

authors

Müller A,Schneider K,Knüttel K,Hagen WR

doi

10.1016/0014-5793(92)80472-s

keywords:

subject

Has Abstract

pub_date

1992-05-25 00:00:00

pages

36-40

issue

1

eissn

0014-5793

issn

1873-3468

journal_volume

303

pub_type

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