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Published January 23, 2001 | public
Journal Article

Crystal Structure of the All-ferrous [4Fe-4S]^0 Form of the Nitrogenase Iron Protein from Azotobacter vinelandii

Abstract

The structure of the nitrogenase iron protein from Azotobacter vinelandii in the all-ferrous [4Fe-4S]^0 form has been determined to 2.25 Å resolution by using the multiwavelength anomalous diffraction (MAD) phasing technique. The structure demonstrates that major conformational changes are not necessary either in the iron protein or in the cluster to accommodate cluster reduction to the [4Fe-4S]^0 oxidation state. A survey of [4Fe-4S] clusters coordinated by four cysteine ligands in proteins of known structure reveals that the [4Fe-4S] cluster of the iron protein has the largest accessible surface area, suggesting that solvent exposure may be relevant to the ability of the iron protein to exist in three oxidation states.

Additional Information

© 2001 American Chemical Society. Received July 14, 2000; Revised Manuscript Received November 7, 2000. Publication Date (Web): December 21, 2000. This work was supported by the National Institute of Health (Grant GM43144 to B.K.B. and Grant GM45162 to D.C.R.), an NSF graduate fellowship (P.S.), and an NSF postdoctoral fellowship (P.M.T.). This work is based upon research conducted at the Stanford Synchrotron Radiation Laboratory (SSRL), which is funded by the Department of Energy (BES and BER) and the National Institutes of Health (NCRR and NIGMS). The Advanced Light Source is supported by the Director, Office of Energy Research, Office of Basic Energy Sciences, Materials Sciences Division, of the U.S. Department of Energy under Contract DE-AC03-76SF00098 at Lawrence Berkeley National Laboratory. We thank Tina M. Iverson for assistance with data collection and James B. Howard for discussions.

Additional details

Created:
August 19, 2023
Modified:
October 19, 2023