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
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Research Support, Non-U.S. Gov't
MeSH terms
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Binding Sites
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Catalysis
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Catalytic Domain
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Cell Membrane / enzymology
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Crystallography, X-Ray
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Electron Transport
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Escherichia coli / enzymology*
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Formate Dehydrogenases / chemistry*
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Formate Dehydrogenases / metabolism
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Formates / metabolism
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Guanine Nucleotides / chemistry
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Guanine Nucleotides / metabolism
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Hydrogen Bonding
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Iron-Sulfur Proteins / chemistry
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Iron-Sulfur Proteins / metabolism
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Membrane Potentials
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Models, Molecular
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Nitrate Reductases / chemistry
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Nitrate Reductases / metabolism
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Oxidation-Reduction
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Protein Conformation
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Protein Structure, Quaternary
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Protein Subunits
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Proton-Motive Force*
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Protons
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Pterins / chemistry
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Pterins / metabolism
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Vitamin K 2 / chemistry
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Vitamin K 2 / metabolism
Substances
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Formates
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Guanine Nucleotides
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Iron-Sulfur Proteins
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Protein Subunits
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Protons
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Pterins
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formic acid
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Vitamin K 2
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molybdopterin guanine dinucleotide
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Formate Dehydrogenases
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Nitrate Reductases