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Structure of the nitrogenase MoFe protein: Spatial distribution of the intrinsic metal atoms determined by X-ray anomalous scattering

  • J. T. Bolin
  • A. E. Ronco
  • L. E. Mortenson
  • T. V. Morgan
  • M. Williamson
  • N.-h. Xuong

Abstract

A focal point for discussions of the organization of the metal atoms bound to nitrogenase MoFe protein is the model proposed by Zimmerman et al. on the basis of a series of EPR and Mössbauer experiments [1]. This model defined two types of metal-sulfur clusters, M-centers and P-clusters. The original and current versions of the model both identify the M-centers as FeMo-cofactors. Two are bound per α2β2 tetramer; each comprises 1 Mo and 6–7 Fe atoms. P-clusters account for an additional 16 Fe atoms organized into four Fe4S4 clusters. The current model recognizes two pairs of two distinct types of P-clusters. Thus MoFe protein should bind one FeMo-cofactor and one P-cluster of each type per αβ unit [2].

Keywords

Fe4S4 Cluster MoFe Protein Crystallographic Symmetry General Peak Anomalous Scattering 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Routledge, Chapman & Hall, Inc. 1990

Authors and Affiliations

  • J. T. Bolin
    • 1
  • A. E. Ronco
    • 1
  • L. E. Mortenson
    • 2
  • T. V. Morgan
    • 2
  • M. Williamson
    • 3
  • N.-h. Xuong
    • 3
  1. 1.Biological SciencesPurdue Univ.W. LafayetteUSA
  2. 2.Center for Metalloenzyme StudiesUniv. GeorgiaAthensUSA
  3. 3.Biology Dept.Univ. California-San DiegoLaJollaUSA

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