Molecular basis of proton motive force generation: structure of formate dehydrogenase-N

Science. 2002 Mar 8;295(5561):1863-8. doi: 10.1126/science.1068186.

Abstract

The structure of the membrane protein formate dehydrogenase-N (Fdn-N), a major component of Escherichia coli nitrate respiration, has been determined at 1.6 angstroms. The structure demonstrates 11 redox centers, including molybdopterin-guanine dinucleotides, five [4Fe-4S] clusters, two heme b groups, and a menaquinone analog. These redox centers are aligned in a single chain, which extends almost 90 angstroms through the enzyme. The menaquinone reduction site associated with a possible proton pathway was also characterized. This structure provides critical insights into the proton motive force generation by redox loop, a common mechanism among a wide range of respiratory enzymes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Catalysis
  • Catalytic Domain
  • Cell Membrane / enzymology
  • Crystallography, X-Ray
  • Electron Transport
  • Escherichia coli / enzymology*
  • Formate Dehydrogenases / chemistry*
  • Formate Dehydrogenases / metabolism
  • Formates / metabolism
  • Guanine Nucleotides / chemistry
  • Guanine Nucleotides / metabolism
  • Hydrogen Bonding
  • Iron-Sulfur Proteins / chemistry
  • Iron-Sulfur Proteins / metabolism
  • Membrane Potentials
  • Models, Molecular
  • Nitrate Reductases / chemistry
  • Nitrate Reductases / metabolism
  • Oxidation-Reduction
  • Protein Conformation
  • Protein Structure, Quaternary
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Protein Subunits
  • Proton-Motive Force*
  • Protons
  • Pterins / chemistry
  • Pterins / metabolism
  • Vitamin K 2 / chemistry
  • Vitamin K 2 / metabolism

Substances

  • Formates
  • Guanine Nucleotides
  • Iron-Sulfur Proteins
  • Protein Subunits
  • Protons
  • Pterins
  • formic acid
  • Vitamin K 2
  • molybdopterin guanine dinucleotide
  • Formate Dehydrogenases
  • Nitrate Reductases

Associated data

  • PDB/1KQF
  • PDB/1KQG