On the prosthetic group(s) of component II from nitrogenase. EPR of the Fe-protein from Azotobacter vinelandii

FEBS Lett. 1985 Jul 22;187(1):146-50. doi: 10.1016/0014-5793(85)81231-x.

Abstract

The EPR spectrum of the reduced Fe-protein from nitrogenase has been reinvestigated. The dependences on temperature, microwave power, and microwave frequency all suggest that the observed signal represents a magnetically isolated [4Fe-4S]1+(2+;1+) cluster. Also, the signal can be simulated assuming a simple, g-strained S = 1/2 system. However, the integrated intensity amounts to no more than 0.2 spins per protein molecule. It is, therefore, impossible that Fe-protein preparations contain a single type of [4Fe-4S] cluster.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Azotobacter / enzymology*
  • Computers
  • Electron Spin Resonance Spectroscopy
  • Microwaves
  • Nitrogenase*
  • Temperature

Substances

  • Nitrogenase