Resonance Raman studies of the [4Fe‐4S] to [2Fe‐2S] cluster conversion in the iron protein of nitrogenase
- 24 June 1991
- journal article
- Published by Wiley in FEBS Letters
- Vol. 284 (2) , 165-168
- https://doi.org/10.1016/0014-5793(91)80676-t
Abstract
Resonance Raman spectroscopy has been used to investigate the Fe‐S stretching modes of the [4Fe‐4S]2+ cluster in the oxidized iron protein of Clostridium pasteurianum nitrogenase. The results are consistent with a cubane [4Fe‐4S] cluster having effective Td symmetry with cysteinyl coordination for each iron. In accord with previous optical and EPR studies [(1984) Biochemistry 23, 2118–2122], treatment with the iron chelator α,α′‐dipyridyl in the presence of MgATP is shown to effect cluster conversion to a [2Fe‐2S]2+ cluster. Resonance Raman data also indicate that partial conversion to a [2Fe‐2S]2+ cluster is induced by thionine‐oxidation in the presence of MgATP in the absence of an iron chelator. This result suggests new explanations for the dramatic change in the CD spectrum that accompanies MgATP‐binding to the oxidized Fe protein and the anomalous resonance Raman spectra of thionine‐oxidized Clostridium pasteurianum bidirectional hydrogenase.Keywords
This publication has 20 references indexed in Scilit:
- Fe2S2 protein resonance Raman spectra revisited: structural variations among adrenodoxin, ferredoxin, and red paramagnetic proteinJournal of the American Chemical Society, 1989
- Vibrational spectra and normal mode analysis for [2Fe-2S] protein analogs using sulfur-34, iron-54 and deuterium substitution: coupling of iron-sulfur stretching and sulfur-carbon-carbon bending modesJournal of the American Chemical Society, 1989
- A Simple Anaerobic Cell for Low-Temperature Raman SpectroscopyApplied Spectroscopy, 1988
- Vibrational mode structure and symmetry in proteins and analogs containing Fe4S4 clusters: resonance Raman evidence that HiPIP is tetrahedral while ferredoxin undergoes a D2d distortionJournal of the American Chemical Society, 1987
- Reactions with the oxidized iron protein of Azotobacter vinelandii nitrogenase: formation of a 2Fe centerBiochemistry, 1984
- Resonance Raman spectroscopic evidence for a common [3-iron-4-sulfur] structure among proteins containing three-iron centersJournal of the American Chemical Society, 1983
- Low-temperature magnetic circular dichroism evidence for the conversion of four-iron-sulphur clusters in a ferredoxin from Clostridium pasteurianum into three-iron-sulphur clustersBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1981
- Circular dichroism and magnetic circular dichroism of iron-sulfur proteinsBiochemistry, 1978
- Electron‐Paramagnetic‐Resonance Studies on NitrogenaseEuropean Journal of Biochemistry, 1974
- Electron paramagnetic resonance studies on nitrogenase. II. Interaction of adenosine 5′-triphosphate with azoferredoxinBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1973